ASGR INHIBITORS

Abstract

Antigen binding proteins that interact with ASGR, ASGR-1 and/or ASGR-2 are described as well as methods of making and using such antigen binding proteins. Methods of treating and preventing cardiovascular disease by administering a pharmaceutically effective amount of ASGR, ASGR-1 and/or ASGR-2 antigen binding proteins. Methods of treating and preventing cardiovascular disease by administering a pharmaceutically effective amount of interfering RNA compositions that reduce expression of ASGR, ASGR-1 and/or ASGR-2 are described.

Description

CROSS REFERENCE TO RELATED APPLICATIONS

This application claims priority to U.S. Provisional Patent Application No. 62/319,740, filed Apr. 7, 2016, U.S. Provisional Patent Application No. 62/259,553, filed Nov. 24, 2015, and U.S. Provisional Patent Application No. 62/234,546, filed Sep. 29, 2015, which are incorporated herein by reference in their entirety.

REFERENCE TO THE SEQUENCE LISTING AND TABLES IN ELECTRONIC FORMAT

This application contains a Sequence Listing which has been submitted electronically in ASCII format and is hereby incorporated by reference in its entirety. Said ASCII copy, created on Sep. 20, 2016, is named APMOL017ASEQUENCE.txt and is 14,773,579 bytes in size. The present application is being filed along with a collection of Tables in electronic format. The collection of Tables is provided as four files entitled TABLE10A.txt, TABLE10B.txt, TABLE10C.txt, and TABLE10D.txt, created and last saved on Sep. 26, 2016, which are 88,431, 356,111, 699,631, and 688,275 bytes in size respectively. The information in the electronic format of the collection of Tables is incorporated herein by reference in its entirety.

FIELD

The field of this invention relates to compositions and methods related to ASGR inhibitors, including but not limited to anti-ASGR, anti-ASGR-1, and/or anti-ASGR-2 antigen binding proteins.

BACKGROUND OF VARIOUS EMBODIMENTS

Cardiovascular disease involving the heart or blood vessels remains a leading cause of global mortality. Cardiovascular disease includes coronary artery disease (CAD) which can lead to angina and myocardial infarction (MI), stroke, hypertensive heart disease, rheumatic heart disease, and other disorders of the cardiovascular system. Medicines for treating cardiovascular disease, and in particular coronary artery disease, have been introduced over the years (e.g., the small molecule class of drugs called statins and the recently approved Repatha®, an antibody targeting PCSK9).

SUMMARY OF VARIOUS EMBODIMENTS

In some aspects, the invention provides an isolated antigen binding protein that binds to human ASGR and inhibits ASGR function. In one embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR and inhibits ASGR binding to ligand. In another embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 and inhibits ASGR-1 binding to ligand and/or ASGR-1 interaction with ASGR-2. In another embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR-2 and inhibits ASGR-2 binding to ligand and/or ASGR-2 interaction with ASGR-1. In yet another embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 and human ASGR-2, and inhibits ASGR-1 and/or ASGR-2 binding to ligand. In some embodiments, the isolated binding protein binds specifically to human ASGR, ASGR-1 and/or ASGR-2.

In some aspects, the invention provides an isolated antigen binding protein, wherein the isolated antigen binding protein binds to human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7. In some aspects, the invention comprises an isolated antigen binding protein, wherein the isolated antigen binding protein binds to human ASGR-1 and comprises one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises one VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and one VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises two VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and two VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and the VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE A, and the VL CDR1, VL CDR2 and VL CDR3, having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE B. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE B. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE B, and the VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE B. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in TABLE B. In still some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE C. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE C. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE C, and the VL CDR1, VL CDR2 and VL CDR3, having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE C. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in TABLE C. In further embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Table 6. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Table 6. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Table 6, and the VL CDR1, VL CDR2 and VL CDR3, having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Table 6. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in Table 6.

In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 3-7. In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Tables 3-7. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 3-7, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Tables 3-7. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Tables 3-7, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Tables 3-7. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table A, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table A, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table B, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table B, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table C, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table C, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table 6. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 6. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table 6, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 6. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table 6, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table 6.

In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising no more than 18 amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55. In some aspects, the invention comprises an isolated antigen binding protein, wherein the isolated antigen binding protein binds to human ASGR-1 and comprises one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising no more than 14 amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising no more than 18amino acid residue substitutions, inserions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising no more than 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises one VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical no more than 18 amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and one VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising no more than 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A, as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and one VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises two VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising up to 18amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and two VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising up to 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A, as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises two VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and two VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 and VH CDR3 having an amino acid sequence identical to or comprising up to 18amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and the VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising up to 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A, as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55.

In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 19A, as depicted in FIG. 55 or in Tables 21-34 as depicted in FIG. 56 or in Tables 49-95 as depicted in FIG. 56. In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 20A, as depicted in FIG. 55, or in Tables 35-48, as depicted in FIG. 56 or in Tables 96-134 as depicted in FIG. 57. In some embodiments, the antigen binding protein comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 19A as depicted in FIG. 55, or in Tables 21-34 as depicted in FIG. 56 or in Tables 49-95 as depicted in FIG. 57, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 20A as depicted in FIG. 55 or in Tables 35-48 as depicted in FIG. 56 or in Tables 96-134 as depicted in FIG. 57. In some embodiments, the antigen binding protein comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Tables 19A as depicted in FIG. 55, or in Tables 21-34 as depicted in FIG. 56 or in Tables 49-95 as depicted in FIG. 57, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table 20A as depicted in FIG. 55 or in Tables 35-48 as depicted in FIG. 56 or in Tables 96-134 as depicted in FIG. 57.

In some aspects, the invention provides an antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by any of the antigen binding proteins disclosed herein. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Tables 2-7. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table 6.

In some aspects, the invention provides an isolated antigen binding protein that competes for binding to human ASGR-1 with any of the antigen binding proteins disclosed herein. In some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Tables 2-7. In some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table B. In still some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table C. In yet another embodiment, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table 6.

In some aspects, the invention provides an isolated antigen binding protein that binds to human ASGR-1 within the carbohydrate recognition domain (“CRD”) (also known as the carbohydrate binding domain or “CBD”) and inhibits human ASGR-1 binding to ligand. In some embodiments, the antigen binding protein binds to human ASGR-1 within residues 148-291, or 149-291, or 150-291, or 151-291, or 152-291, or 153-291, or 154-291, or 155-291 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within Helix α-1. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 within residues 174-186 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within Helix α-2. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within residues 194-206 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 within residues 237-273 or residues 240-267 of SEQ ID NO:5. In some embodiments, the antigen binding protein binds to ASGR-1 having an amino acid sequence that is at least 90% identical to SEQ ID NO:5. In some embodiments, the antigen binding protein is an antibody.

In some aspects, the invention provides an isolated antigen binding protein or an antibody that binds to human ASGR-1 and inhibits human ASGR-1 function. In some embodiments, the isolated antigen binding protein or an antibody binds to human ASGR-1 and inhibits human ASGR-1 from binding to a ligand. In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, : H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, or R263 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR1 at an epitope comprising at least one of the following amino acid residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, or R263 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, or R263 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, : H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, or G252 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, or C269 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, or Q270 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, or D266 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, or Y273 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5).

In some aspects, the invention provides an isolated antigen binding protein or an antibody or a paratope in an antibody that specifically binds to human ASGR-1 and inhibits human ASGR-1 function. In some embodiments, the isolated antigen binding protein or an antibody or a paratope in an antibody specifically binds to human ASGR-1 and inhibits human ASGR-1 from binding to a ligand. In some embodiments, the antigen binding protein or antibody or a paratope in an antibody specifically binds to human ASGR-1 within residues 148-291 of SEQ ID NO:5. In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5).

In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, or D267 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R237, Q240, D242, W244, E253, N265, D266, or D267 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, or R271 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, or C269 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, or Q270 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, or D266 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues of human ASGR-1 (SEQ ID NO:5): D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues of human ASGR-1 (SEQ ID NO:5): H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, or R263 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, or R263 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, or R263 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, : H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, or G252 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270 or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273 or R274 (SEQ ID NO:5).

In some aspects, the invention comprises an isolated antigen binding protein or antibody that specifically binds to human ASGR-1 and inhibits human ASGR-1 function. In some embodiments, the isolated antigen binding protein or antibody that specifically binds to human ASGR-1 inhibits binding of human ASGR-1 binding to a ligand. In some embodiments, the antigen binding protein or antibody specifically binds to human ASGR-1 at a location that overlaps with a location where a ligand binds to human ASGR-1. In some embodiments, the location where a ligand binds to ASGR-1 includes at least one amino acid residue selected from the group consisting of: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, or R271 (SEQ ID NO:5). In some embodiments, an isolated antigen binding protein or an antibody specifically binds to human ASGR-1 at a location that overlaps with a location that a ligand binds to ASGR-1. In some embodiments, the location that a ligand binds to human ASGR-1 includes at least one amino acid residue selected from the group consisting of: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, and Y273 (SEQ ID NO:5).

In some aspects, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 and inhibits human ASGR, ASGR-1 and/or ASGR-2 function, wherein the antigen binding protein does not bind to a variant ASGR-1 protein, and wherein said variant ASGR-1 protein comprises a single mutation of a residue selected the group consisting of: R170, S171, G172, R183, L184, W195, E196, K199, H203, H204, P207, V208, N209, H215, D216, P220, D225, D228, R237, P238, E239, P241, D242, D243, Y245, G246, H247, G248, L249, G251, E253, T259, D260, R263, N265, Q270, R271, P272, R274, and E280 as shown in SEQ ID NO:5. In some embodiments, an isolated antigen binding protein or an antibody is contemplated. An antigen binding protein “does not bind” to a variant ASGR-1 protein when the measured reduction in antibody binding signal to a variant ASGR-1 protein (compared to that determined for binding to wild type ASGR-1) is statistically significant as measured by any number of methods known to one skilled in the art, such as the method described in Example 7E below. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting of: W195, E196, K199, H203, H204, P207, P220, G251, and R263 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of H203, H204, P220, and G251. In some embodiments, the single mutation is selected from the group consisting of W195, E196 and K199. In some embodiments, the single mutation is selected from the group consisting of W195, E196 and H204. In some embodiments, the single mutation is selected from the group consisting W195, K199, and R263. In some embodiments, the single mutation is selected from the group consisting of W195 and E196. In some embodiments, the single mutation is selected from the group consisting of W195 and K199. In some embodiments, the single mutation is selected from the group consisting of W195 or P207. In some embodiments, the single mutation is selected from the group consisting of W195 and R263. In some embodiments, the single mutation is selected from the group consisting of H203 and H204. In some embodiments, the single mutation is selected from the group consisting of K199 and R263. In some embodiments, the single mutation is a mutation of residue W195. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue selected the group consisting of: R170, S171, R183, L184, H215, P220, P238, G246, H247, G248, G251, and N265 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R183, L184, H215, P220, G246, G248, G251, and N265. In some embodiments, the single mutation is selected from the group consisting of L184, P220, P238, H247, and G251. In some embodiments, the single mutation is selected from the group consisting of R170, S171, and L184. In some embodiments, the single mutation is a mutation of residue R183. In some embodiments, the single mutation is a mutation of residue L184. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting of: P241, D242, D243, Y245, G251, E253 and D260 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of P241, D243, Y245, G251, E253 and D260. In some embodiments, the single mutation is selected from the group consisting of P241, D243, and E253. In some embodiments, the single mutation is a mutation of residue D260. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, R237, E239, P241, T259, D260, R263, and N265 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R237, D260 and R263. In some embodiments, the single mutation is selected from the group consisting of R237, T259, D260 and R263. In some embodiments, the single mutation is selected from the group consisting of R170, R237, P241, T259, D260, R263 and N265. In some embodiments, the single mutation is selected from the group consisting of R237, E239, P241, T259, D260, R263 and N265. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, S171, G172, E196, H204, P207, V208, N209, H215, D216, D225, D228, P238, P241, D242, D243, H247, G248, L249, G251, D260, R263, N265, Q270, R271, P272, R274 and E280 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R170, S171, G172, E196, H204, P207, V208, N209, H215, D216, D225, D228, P238, P241, D242, D243, H247, G248, L249, G251, D260, R263, N265, Q270, R271, P272, R274 and E280 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R170, S171, G172, E196, H204, P207, H215, D216, D225, D228, D243, G248, L249, G251, D260, Q270, R271, P272, R274 and E280. In some embodiments, the single mutation is selected from the group consisting of G172, V208, R271, P272 and R274. In some embodiments, the single mutation is selected from the group consisting of G172, R271 and R274. In some embodiments, the single mutation is selected from the group consisting of G172, N209, and R271. In some embodiments, the single mutation is selected from the group consisting of R170, G172, V208, R271 and P272. In some embodiments, the single mutation is selected from the group consisting of G172, V208, P238, R271, P272 and R274. In some embodiments, the single mutation is selected from the group consisting of G172, P238, R271, P272 and R274. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: G172, P238, R271 and R274 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, G172, V208 and R274 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, R183, H215 and Q270 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: P241, T259, and N265 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: P207 and R263 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: G172, P241, D242, H247, L249, N265, R271 and P272 as shown in SEQ ID NO:5. In some embodiments, the antigen binding protein or antibody does not bind to two or more variant ASGR-1 proteins, wherein the variant ASGR-1 proteins comprise the single mutations of the group individually.

In some aspects, the invention comprises a vector comprising a nucleic acid molecule as described herein. In some embodiments, the invention comprises a host cell comprising a nucleic acid molecule as described herein.

In some aspects, the invention comprises a nucleic acid molecule encoding the antigen binding protein as described herein.

In some aspects, the invention comprises a pharmaceutical composition comprising at least one antigen binding protein described herein.

In some aspects, the invention provides a method of treating or preventing a cardiovascular disease comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the relative risk reduction of a cardiovascular event is at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60% in the patient.

In some aspects, the invention provides a method of decreasing the risk of acquiring coronary artery disease or having a myocardial infarction (MI) comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the relative risk reduction of coronary artery disease or MI is at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60% in the patient.

In other aspects, the invention provides a method of reducing blood LDL cholesterol levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, blood LDL cholesterol is reduced by at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, or at least about 90% as compared to a predose level of blood LDL cholesterol in the patient.

In still other aspects, the invention provides a method of reducing non-HDL cholesterol levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, non-HDL cholesterol is reduced by at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, or at least about 90% as compared to a predose level of non-HDL cholesterol in the patient.

In some aspects, the invention provides a method of increasing alkaline phosphatase (“ALP”) levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, ALP levels are increased at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, or at least about 90% as compared to a predose ALP level in the patient. In some embodiments, ALP levels are increased at least about 1.25×, 1.5×, 2×, 2.5×, 3×, 3.5×, 4×, 4.5×, and 5× over pretreatment.

In some aspects, the invention provides a method of antagonizing ASGR, ASGR-1 and/or ASGR-2 in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein.

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1A. ASGR-1 sequence alignments of human (SEQ ID NO: 32699), cynomolgus monkey (cyno) (SEQ ID NO: 32700), dog (SEQ ID NO: 32701), pig (SEQ ID NO: 32702), rat (SEQ ID NO: 32703) and mouse ASGR-1 (SEQ ID NO: 32704). The boxed areas denoting different regions of ASGR-1 (i.e., cytoplasmic, transmembrane, and the carbohydrate binding domain (CBD; also called the carbohydrate recognition domain, or CRD) are representative of the approximate amino acid locations of these regions; the human Y273 amino acid is boxed.

FIG. 1B. Human ASGR-1 sequence alignments (SEQ ID NOS 32705-32710, respectively, in order of appearance).

FIG. 2. ASGR-2 sequence alignments of human (SEQ ID NO: 32713), cyno (SEQ ID NO: 32714), dog (SEQ ID NO: 32716), pig (SEQ ID NO: 32715), rat (SEQ ID NO: 32712) and mouse ASGR-2 (SEQ ID NO: 32711). The boxed areas denoting different regions of ASGR-2 (i.e., cytoplasmic, transmembrane, and the carbohydrate binding domain (CBD; also called the carbohydrate recognition domain, or CRD) are representative of the approximate amino acid locations of these regions.

FIG. 3. Human ASGR-1 (SEQ ID NO: 32717) vs. human ASGR-2v2 (SEQ ID NO: 32718) alignments are provided.

FIG. 4. The del12 variant is associated with a splicing error and frameshift in ASGR-1. (A) Overview of the structure of the ASGR-1 mRNA. Exons 4 and 5 are highlighted (the del12 variant lies within intron 4 between exons 4 and 5 in the unspliced RNA) along with the positions of the PCR primers (red arrows) used to amplify the cDNA. (B) Agarose gel showing the PCR products generated by amplifying cDNA generated from RNA isolated from the blood of del12 carriers and non-carriers. Arrows indicate both the size of the expected PCR product (239 bp) along with the size of the truncated band (217 bp) observed only in del12 heterozygote carriers. (C) Shown is the sequence difference between the full-length (239 bp) and variant (217 bp) cDNA fragments based on Sanger sequencing. The variant sequence in del12 carriers lacks 22 bp at the end of exon 4 compared to the wild-type sequence that results in frame-shift and introduction of a stop codon. (D) Diagrammatic representation of the splicing defect observed in del12 carriers. The sequence around the exon 4-intron 4 boundary (exon 4 sequence in capital letters and intron 4 sequence in small letters) is shown along with the 5′splice site in non-carriers and the cryptic 5′ splice site activated in del12 carriers. (E) Quantification of the full-length (239 bp) and variant (217 bp) cDNA fragments from heterozygote del12 carriers and non-carriers by direct digital counting of sequencing reads generated following sequencing of the amplified cDNA product from carriers and non-carriers of del12 using the Illumina TruSeq method. The percentage of incorrectly spliced ASGR-1 transcript is shown. Note that the incorrectly spliced form was completely undetectable in non-carriers.

FIG. 5. (A) The del12 variant was typed in the indicated populations a total of 41,648 CAD cases and 247,374 controls. For each cohort, the square (diamond in the case of the combined estimate) indicates the estimated odds ratio and the line shows the 95% confidence interval. There was no evidence of heterogeneity across the eight study populations (Phet=0.96). (B) Kaplan-Meier curves for survival to first myocardial infarction in carriers and non-carriers of del12 in ASGR-1 stratified by sex. The proportion of individuals that have not had a myocardial infarction is shown on the y-axis and plotted against age on the x-axis. Males and females are represented separately and a distinction is made between del12 carriers and non-carriers in each case.

FIG. 6. Comparison of relationship between CAD and non-HDL cholesterol levels between previously identified sequence variants and del12 in ASGR-1. Based on the Icelandic population, the estimated odds ratio (OR) of the minor allele for coronary artery disease (CAD, 41,648 cases and 247,374 controls) as a function of the estimated effect of the minor allele on non-HDL cholesterol levels (N=119,146). A full list of the sequence variants included is provided in Table 1.7. The error bars represent 95% confidence intervals. The del12 variant in ASGR-1 is shown. The line indicates the best linear regression fit through the origin.

FIG. 7. Analysis of serum ALP, ALT, and AST from ASGR-1 knockout mice is provided. Panel A is data from the male mice studied and Panel B is data from the female mice.

FIG. 8. RNAi in vitro data in CHO cells transfected with hASGR-1 using construct S1662. Panel A is a western blot demonstrating reduction of expression of human ASGR-1. Panel B is a graphical representation of the relative reduction in expression of human ASGR-1. Panel C demonstrates that CHO cells receiving construct S1662 displays a dramatic reduction in internalization of ligand (β-GalNAc).

FIG. 9. RNAi in vitro data in CHO cells transfected with mASGR-1 using various constructs. Panel A is a western blot demonstrating reduction of expression of mouse ASGR-1. Panel B is a graphical representation of the relative reduction in expression of mouse ASGR-1. Panel C demonstrates that CHO cells receiving the various constructs display a dramatic reduction in internalization of ligand (β-GalNAc).

FIG. 10. RNAi in vitro data in HepG2 cells using construct S1662. Panel A is a western blot demonstrating reduction of expression of human ASGR-1. Panel B is a graphical representation of the relative reduction in expression of human ASGR-1.

FIG. 11. RNAi in vitro data in CHO cells transfected with hASGR-2 using various constructs. Panel A is a western blot demonstrating reduction of expression of human ASGR-2. Panel B is a graphical representation of the relative reduction in expression of human ASGR-2 by the various constructs.

FIG. 12. RNAi in vitro data in CHO cells transfected with mASGR-1 and mASGR-2 using various other constructs. Panel A is a western blot demonstrating reduction of expression of mouse ASGR-1 (anti-mouse ASGR-1 or anti-flag) or mouse ASGR-2 (anti-his). Panel B is a graphical representation of the relative reduction in expression of mouse ASGR-1 by the various constructs. Panel C is a graphical representation of the relative reduction in expression of mouse ASGR-2 by the various constructs.

FIG. 13. RNAi in vitro data in HepG2 cells using various constructs. Panel A is a western blot demonstrating reduction of expression of human ASGR-2. Panel B is a graphical representation of the relative reduction in expression of human ASGR-2 by the various constructs.

FIG. 14. RNAi in vivo data in C57BL/6J mice using various constructs over the course of 7 days with three injections total, one injection at day 0, one injection at day 2 and one injection at day 4. Panel A is a graphical representation of quantitative per data showing the relative reduction in expression of mASGR-1 RNA in the liver. Panel B is a graphical representation of the relative reduction in expression of mASGR-2 RNA in the liver.

FIG. 15. RNAi in vivo data in C57BL/6J mice using various constructs over the course of 7 days with three injections total, one injection at day 0, one injection at day 2, and one injection at day 4. Panel A is a western blot demonstrating reduction of expression of mouse ASGR-1 protein. Panel B is a graphical representation of the relative increase of serum ALP activity.

FIG. 16. RNAi in vivo data in C57BL/6J mice using various constructs over the course of 7 days with one injection at day 0. Panel A is a graphical representation of the relative reduction in expression of mASGR-2 in the liver. Panel B is a graphical representation of the relative reduction in expression of mASGR-1 in the liver.

FIG. 17. RNAi in vivo data in C57BL/6J mice using various ASGR-2 constructs over the course of 7 days with one injection at day 0. The figure is a graphical representation of the relative increase in serum ALP activity.

FIG. 18. Panel A shows a computer representation of the crystal structure of the ASGR-1/lactose complex. Panel B is a computer representation of the observed electron density. Panel C is an enlarged view of the carbohydrate binding domain.

FIG. 19. Panel A shows a computer representation of the crystal structure of the ASGR-1/galactose complex. Panel B is a computer representation of the observed electron density. Panel C is an enlarged view of the carbohydrate binding domain.

FIG. 20. A computer representation of the crystal structure of an enlarged view of the conformational difference of R237 between the ASGR-1/lactose (white) complex and ASGR-1/galactose (black) complex.

FIG. 21. Panel A shows a computer representation of the crystal structure of the ASGR-1/GalNAc complex. Panel B is a computer representation of the observed electron density. Panel C is an enlarged view of the carbohydrate binding domain.

FIG. 22. Panel A shows a depiction of the structure of the ASGR-1 CBD and the 5E5 Fab. Panel B is an enlarged view of the ASGR-1 CBD and 5E5 Fab that represents a disordered carbohydrate binding loop with a dashed line and highlights the indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding. Panel B also incorporates a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 23. Panel A shows a depiction of the structure of the ASGR-1 CB and the 22G5 Fab. Panel B is an enlarged view of the ASGR-1 CBD and 22G5 Fab that represents a disordered carbohydrate binding loop with a dashed line and highlights the indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding. Panel B also incorporates a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 24. A depiction of the structure of the ASGR-1 CBD and the 4A2 Fab.

FIG. 25. An enlarged view of the structure of the ASGR-1 CBD and the 4A2 Fab that shows the CDRs of the 4A2 Fab that interact with ASGR-1 CBD Helix alpha-2 and highlights the indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding. The figure incorporates a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 26. An enlarged view of the structure of the ASGR-1 CBD and the carbohydrate binding loop with and without and the 4A2 Fab that includes a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 27. A depiction of the structure of ASGR-1 CBD and the 7E11 Fab.

FIG. 28. An enlarged view of the structure of the ASGR-1 CBD and the 7E11 Fab. The figure represents a disordered carbohydrate binding loop with a dashed line and highlights the indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding. The figure incorporates a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 29. A depiction of the structure of the ASGR-1 CBD and the 4H6 Fab.

FIG. 30. An enlarged view of structure of the ASGR-1 CBD and the 4H6 Fab. The figure represents a disordered carbohydrate binding loop with a dashed line and highlights the indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding. The figure incorporates a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 31. A depiction of the structure of the ASGR-1 CBD and the 72G9 Fab.

FIG. 32. Panel A is an enlarged view of the structure of ASGR-1 CBD and the 72G9 Fab; and Panel B is a depiction of the structure of ASGR-1 CBD and the 72G9 Fab that also overlays the structure of ASGR-1 CBD and the ligand and highlights the direct inhibition of ASGR-1 CBD and the ligand (GalNAc) binding.

FIG. 33. A depiction of the structure of the ASGR-1 CBD and the 194A4 Fab.

FIG. 34. An enlarged view of the structure of the ASGR-1 CBD and the 194A4 Fab. The figure represents a disordered carbohydrate binding loop with a dashed line and highlights the indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding. The figure incorporates a double-headed arrow which represents a 5 angstrom distance from tip to tip.

FIG. 35. A depiction of the structure of the ASGR-1 CBD and the 54E9 Fab.

FIG. 36. Panel A is an enlarged view of the structure of the ASGR-1 CBD and the 54E9 Fab; and Panel B is a depiction of the structure of the ASGR-1 CBD and the 54E9 Fab that also overlays the structure of ASGR-1 CBD and the ligand and highlights the direct inhibition of ASGR-1 CBD and the ligand (GalNAc) binding.

FIG. 37. Panel A is a depiction of the structure of the ASGR-1 CBD and the 218G4 Fab; and Panel B is an enlarged view of the structure of the ASGR-1 CBD and the 218G4 Fab.

FIG. 38. Panels A and B are enlarged views of the structure of ASGR-1 CBD and the 218G4 Fab that also overlays the structure of ASGR-1 CBD and the ligand. These figures highlight the direct inhibition of ASGR-1 CBD and the ligand (GalNAc) binding when the 218G4 Fab is present.

FIG. 39. A depiction of the structure of the ASGR-1 CBD and the 176H4 Fab.

FIG. 40. An enlarged view of the structure of the ASGR-1 CBD and the 176H4 Fab that also overlays the structure of ASGR-1 CBD and the ligand. This figure highlight the direct inhibition of ASGR-1 CBD and the ligand (GalNAc) binding when the 176H4 Fab is present.

FIG. 41. A depiction of the structure of the ASGR-1 CBD and the 194C10 Fab. This figure depicts represents a disordered carbohydrate binding loop with a dashed line and highlights possible indirect inhibition of ASGR-1 CBD and the ligand (GalNAc) binding.

FIG. 42. An enlarged view of the structure of the ASGR-1 CBD and the 194C10 Fab. This figure shows the CDRs of the 194C10 that interact with the ASGR-1 CBD and highlights that there may be direct inhibition of the ASGR-1 CBD and the ligand (GalNAc) binding.

FIG. 43. Panels A-C are graphical representations showing antibody binding results from human ASGR-1 and human ASGR-2 expressing cells.

FIG. 44. Panel A is a graphical representation of the effect of ASGR-1 antibody, 4A2, on serum LDL cholesterol levels in obese cynomologous monkeys. Panel B is a graphical representation of the effect of ASGR-1 antibody, 4A2, on serum alkaline phosphatase levels in obese cynomologous monkeys. Data is expressed in the % change from baseline.

FIG. 45. Panel A is a graphical representation of the effect of ASGR-1 antibody, 4A2, on serum LDL cholesterol levels in normal cynomologous monkeys. Panel B is a graphical representation of the effect of ASGR-1 antibody, 4A2, on serum alkaline phosphatase levels in normal cynomologous monkeys. Data is expressed in the % change from baseline.

FIG. 46. A coefficient of determination heat map representing the coefficient of determination profiles of test ASGR-1 ligand blocking antibody-reference antibody combinations from an Arginine/Glutamic Acid scanning mutagenesis (Example 7E). Dark shading represents highly similar data, while light shading represents highly dissimilar data. The relative epitope profiling (antibody competition/binding) bin assignments are also indicated.

FIG. 47. A computer representation showing alternative views of the ASGR-1 CBD protein and the surface locations of amino acid residues identified as being important for antibody binding via Arginine/Glutamic Acid scanning mutagenesis (Example 7E). The relative epitope profiling (antibody competition/binding) bin assignments are also indicated. Ligand (GalNAc) is shown as a stick representation (black). The ASGR-1 CBD is shown as a surface representation (light grey). The positions of amino acids identified by Arg/Glu mutational scanning are indicated (dark grey surface). The relative positions of key amino acids in each bin are shown for reference only.

FIG. 48. A table presenting various protein sequences for human, mouse, rat, pig, dog and cynomolgus monkey ASGR, ASGR-1 and ASGR-2 (Table 1).

FIG. 49. Two tables presenting variable light and heavy chain CDR1, CDR2 and CDR3 amino acid sequences for certain antigen binding proteins of the present invention (Table 2A and Table 2B). Table 2A presents the Variable Light Chain CDR1, CDR2 and CDR3, while Table 2B presents the Variable Heavy Chain CDR1, CDR2, and CDR3. The CDR sequences in Tables 2A and 2B are wrapped due to space issues, and unless stated otherwise, should be understood to be a single amino acid sequence.

FIG. 50. A table presenting the amino acid sequences of the light and heavy chain variable domains for certain antigen binding proteins of the present invention are displayed in a table (Table 3). The amino acid sequences of the light and heavy chain variable domains in Table 3 are wrapped due to space issues, and unless stated otherwise, should be understood to be single amino acid sequences.

FIG. 51. A table presenting a protein alignment of light and heavy variable regions for certain antigen binding proteins of the present invention (Table 4). An asterisk “*” denotes a stop codon. Sequences containing a stop codon are represented as distinct sequences in the Sequence Listing, however, these sequences are related. Generally speaking, however, the amino acid sequences of the light and heavy chain variable domains in the protein alignment presented in Table 4 are wrapped due to space issues, and unless stated otherwise, like in the case of sequences with one or more stop codons, should be understood to be single amino acid sequences.

FIG. 52. A table presenting a consensus protein alignment of light and heavy variable regions for certain antigen binding proteins of the present invention (Table 5). An asterisk “*” denotes a stop codon. Sequences containing a stop codon are respresented as distinct sequences in the Sequence Listing, however, these sequences are related. Generally speaking, however, the amino acid sequences of the light and heavy chain variable domains in the consensus protein alignment presented in Table 5 are wrapped due to space issues, and unless stated otherwise, like in the case of sequences with one or more stop codons, should be understood to be single amino acid sequences.

FIG. 53. A table presenting a protein alignment of light and heavy variable regions for certain optimized antigen binding proteins of the present invention (Table 6). The amino acid sequences of the light and heavy chain variable domains in the protein alignment presented in Table 6 are wrapped due to space issues, and unless stated otherwise, should be understood to be single amino acid sequences.

FIG. 54. A table presenting a consensus protein alignment of light and heavy variable regions for certain optimized antigen binding proteins of the present invention (Table 7). The amino acid sequences of the light and heavy chain variable domains in the consensus protein alignment presented in Table 7 are wrapped due to space issues, and unless stated otherwise, should be understood to be single amino acid sequences.

FIG. 55. A group of tables presenting the consensus sequences of various heavy and light chain variable regions (Tables 19A and 20A, respectively), as well as the consensus sequences of CDRs of various heavy and light chain variable regions (Tables 19B and C and Tables 20B and 20C, respectively) for certain antigen binding proteins of the present invention.

FIG. 56. A group of tables presenting the detailed consensus protein alignment of various light and heavy chain variable regions for certain antigen binding proteins of the present invention (Tables 21-48). The shading of amino acid residues in the consensus protein alignment presented in Tables 21-48 denote particular residues that one of ordinary skill in the art may wish to target for engineering.

FIG. 57. A group of tables presenting the consensus protein alignment of various light and heavy chain variable regions for certain antigen binding proteins of the present invention (Tables 49-134).

FIG. 58. A graph depicting the credibility of protein measurements in cynomolgus monkey. Log 10 RFU of mean protein levels in the two species are plotted and the ones with low credibility (light dots) and high credibility (darker dots) are marked.

FIG. 59. Serum protein analysis of cynomolgus monkey treated with anti-ASGR-1 antibodies. Panel A is a graph depicting TNFSF8 protein levels in individual animals of different treatment group across the time points. Panel B is a graph depicting normalized TNFSF8 protein levels (percent of time point 0) in individual animals of different treatment groups across the time points. Panel C is a graph depicting TNFSF8 protein levels in each treatment group (n=3, error bar represents the SEM), and Panel D is a graph depicting the distribution of TNFSF8 protein levels in human ASGR1 del12 carriers and non-carriers.

DETAILED DESCRIPTION OF THE VARIOUS EMBODIMENTS

As shown in Example 1 below, sequence variants in ASGR-1 (which resulted in either a faster degrading ASGR1 or a loss of function ASGR1 mutation) resulted in a lowering in the level of non-HDL cholesterol in humans. This in turn resulted in a decrease in the risk of coronary artery disease experienced by these people. As loss of function mutations in ASGR-1 resulted in both the lowering of non-HDL cholesterol and the lowering of coronary artery disease, antibodies and inhibitory RNA that effectively block ASGR can be used to lower the risk of coronary artery disease.

The present invention is directed to inhibitors of ASGR, ASGR-1 and/or ASGR-2. The present invention provides antigen binding proteins that specifically bind to human ASGR, ASGR-1 and/or ASGR-2 and inhibit human ASGR, ASGR-1 and/or ASGR-2 binding to a ligand. The present invention also provides antigen binding proteins that specifically bind to other species of ASGR, ASGR-1 and/or ASGR-2. The present invention is further directed to methods of treating or preventing cardiovascular disease in a human subject comprising administering an inhibitor of ASGR, ASGR-1 and/or ASGR-2, wherein the ASGR inhibitor an antigen binding protein and/or an interfering RNA (e.g., siRNA or shRNA).

The present invention further provides compositions, kits, and methods relating to antigen binding proteins that specifically bind to human ASGR, human ASGR-1, and/or human ASGR-2. Also provided are nucleic acid molecules comprising a sequence of polynucleotides that encode all or a portion of a polypeptide that specifically binds to human ASGR, human ASGR-1, and/or human ASGR-2. The present invention further provides vectors and plasmids comprising such nucleic acids, and cells or cell lines comprising such nucleic acids and/or vectors and plasmids. The provided methods further include, for example, methods of making, identifying, or isolating antigen binding proteins that bind to human ASGR, human ASGR-1, and/or human ASGR-2, methods of determining whether an antigen binding protein binds to human ASGR, human ASGR-1, and/or human ASGR-2, methods of making compositions, such as pharmaceutical compositions, comprising an antigen binding protein that binds to human ASGR, human ASGR-1, and/or human ASGR-2, and methods for administering an antigen binding protein that binds human ASGR, human ASGR-1, and/or human ASGR-2 to a human subject.

It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention as claimed. In this application, the use of the singular includes the plural unless specifically stated otherwise. In this application, the use of “or” means “and/or” unless stated otherwise. Furthermore, the use of the term “including”, as well as other forms, such as “includes” and “included”, is not limiting. Also, terms such as “element” or “component” encompass both elements and components comprising one unit and elements and components that comprise more than one subunit unless specifically stated otherwise. Also, the use of the term “portion” can include part of a moiety or the entire moiety.

Unless otherwise defined herein, scientific and technical terms used in connection with the present invention shall have the meanings that are commonly understood by those of ordinary skill in the art. Further, unless otherwise required by context, singular terms shall include pluralities and plural terms shall include the singular. Generally, nomenclatures used in connection with, and techniques of, cell and tissue culture, molecular biology, immunology, microbiology, genetics and protein and nucleic acid chemistry and hybridization described herein are those well-known and commonly used in the art. The methods and techniques of the present invention are generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification unless otherwise indicated. See, e.g., Sambrook et al. Molecular Cloning: A Laboratory Manual, 2d ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (1989) and Ausubel et al., Current Protocols in Molecular Biology, Greene Publishing Associates (1992), and Harlow and Lane Antibodies: A Laboratory Manual Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (1990), which are incorporated herein by reference. Enzymatic reactions and purification techniques are performed according to manufacturer's specifications, as commonly accomplished in the art or as described herein. The terminology used in connection with, and the laboratory procedures and techniques of, analytical chemistry, synthetic organic chemistry, and medicinal and pharmaceutical chemistry described herein are those well-known and commonly used in the art. Standard techniques can be used for chemical syntheses, chemical analyses, pharmaceutical preparation, formulation, and delivery, and treatment of patients.

Polynucleotide and polypeptide sequences are indicated using standard one- or three-letter abbreviations. Unless otherwise indicated, polypeptide sequences have their amino termini at the left and their carboxy termini at the right, and single-stranded nucleic acid sequences, and the top strand of double-stranded nucleic acid sequences, have their 5′ termini at the left and their 3′ termini at the right. A particular section of a polypeptide can be designated by amino acid residue number such as amino acids 1 to 50, or by the actual residue at that site such as asparagine to proline. A particular polypeptide or polynucleotide sequence also can be described by explaining how it differs from a reference sequence.

The following terms, unless otherwise indicated, shall be understood to have the following meanings:

The term “inhibitor” as used herein, is a compound that decreases the magnitude of at least one activity or function of a molecule compared to the magnitude of the activity or function observed in the absence of the inhibitor. In some instances, an inhibitor will substantially decrease the magnitude of at least one activity or function of a molecule compared to the magnitude of the activity or function observed in the absence of the inhibitor. In some instances, an inhibitor will completely diminish the magnitude of at least one activity or function of a molecule compared to the magnitude of the activity or function observed in the absence of the inhibitor. Certain exemplary inhibitors include, but are not limited to, proteins, peptides, antibodies, peptibodies, aptamers, antisense oligonucleotides, interfering RNA, carbohydrates or small organic molecules.

The term “isolated molecule” (where the molecule is, for example, a polypeptide, a polynucleotide, antigen binding protein or an antibody) is a molecule that by virtue of its origin or source of derivation (1) is not associated with naturally associated components that accompany it in its native state, (2) is substantially free of other molecules from the same species (3) is expressed by a cell from a different species, or (4) does not occur in nature. Thus, a molecule that is chemically synthesized, or expressed in a cellular system different from the cell from which it naturally originates, will be “isolated” from its naturally associated components. A molecule also may be rendered substantially free of naturally associated components by isolation, using purification techniques well known in the art. Molecule purity or homogeneity may be assayed by a number of means well known in the art. For example, the purity of a polypeptide sample may be assayed using polyacrylamide gel electrophoresis and staining of the gel to visualize the polypeptide using techniques well known in the art. For certain purposes, higher resolution may be provided by using HPLC or other means well known in the art for purification.

The terms “polynucleotide,” “oligonucleotide” and “nucleic acid” are used interchangeably throughout and include DNA molecules (e.g., cDNA or genomic DNA), RNA molecules (e.g., mRNA), analogs of the DNA or RNA generated using nucleotide analogs (e.g., peptide nucleic acids and non-naturally occurring nucleotide analogs), and hybrids thereof. The nucleic acid molecule can be single-stranded or double-stranded. In one embodiment, the nucleic acid molecules of the invention comprise a contiguous open reading frame encoding an antibody, or a fragment, derivative, mutein, or variant thereof, of the invention.

A “vector” is a nucleic acid that can be used to introduce another nucleic acid linked to it into a cell. One type of vector is a “plasmid,” which refers to a linear or circular double stranded DNA molecule into which additional nucleic acid segments can be ligated. Another type of vector is a viral vector (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses), wherein additional DNA segments can be introduced into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors comprising a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) are integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. An “expression vector” is a type of vector that can direct the expression of a chosen polynucleotide.

A nucleotide sequence is “operably linked” to a regulatory sequence if the regulatory sequence affects the expression (e.g., the level, timing, or location of expression) of the nucleotide sequence. A “regulatory sequence” is a nucleic acid that affects the expression (e.g., the level, timing, or location of expression) of a nucleic acid to which it is operably linked. The regulatory sequence can, for example, exert its effects directly on the regulated nucleic acid, or through the action of one or more other molecules (e.g., polypeptides that bind to the regulatory sequence and/or the nucleic acid). Examples of regulatory sequences include promoters, enhancers and other expression control elements (e.g., polyadenylation signals). Further examples of regulatory sequences are described in, for example, Goeddel, 1990, Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. and Baron et al., 1995, Nucleic Acids Res. 23:3605-06.

A “host cell” is a cell that can be used to express a nucleic acid, e.g., a nucleic acid of the invention. A host cell can be a prokaryote, for example, E. coli, or it can be a eukaryote, for example, a single-celled eukaryote (e.g., a yeast or other fungus), a plant cell (e.g., a tobacco or tomato plant cell), an animal cell (e.g., a human cell, a monkey cell, a hamster cell, a rat cell, a mouse cell, or an insect cell) or a hybridoma. Typically, a host cell is a cultured cell that can be transformed or transfected with a polypeptide-encoding nucleic acid, which can then be expressed in the host cell. The phrase “recombinant host cell” can be used to denote a host cell that has been transformed or transfected with a nucleic acid to be expressed. A host cell also can be a cell that comprises the nucleic acid but does not express it at a desired level unless a regulatory sequence is introduced into the host cell such that it becomes operably linked with the nucleic acid. It is understood that the term host cell refers not only to the particular subject cell but to the progeny or potential progeny of such a cell. Because certain modifications may occur in succeeding generations due to, e.g., mutation or environmental influence, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.

ASGR

Genomic database analysis is one manner that allows for the discovery of associations between disease states and particular targets and/or pathways. For example, genetic analysis of patients with familial hypercholesterolemia resulted in the discovery of proprotein convertase subtilisin/kexin type 9 (PCSK9) being involved with regulating serum LDL cholesterol levels and risk of developing coronary artery disease, and ultimately, in the development of the recently approved Repatha®, an anti-hPCSK9 antibody. (see, e.g., Jackson et al., U.S. Pat. No. 8,030,457). Advances in DNA sequencing technology provide the means to sequence the genomes of large numbers of individuals allowing for discovery of rare variants. deCODE Genetics (an Amgen company) has previously reported methods to analyze whole genomes of large numbers of Icelanders in order to search for associations between genetic variants and traits of interest. (Gudbjartsson et al., Nature Genetics; Vol. 47; 5; May 2015; p. 435-444).

This methodology has now been applied in the search for novel genetic variants that affect cardiovascular disease, including cholesterol levels, and the risk for developing coronary artery disease and myocardial infarction (MI). The groundbreaking analysis performed has identified novel sequence variants of the Ashwell-Morell Receptor that are implicated in cardiovascular disease.

In the present invention, whole-genome sequencing of the Icelandic population discovered a rare, 12 base pair deletion (“del12”) in intron 4 of the ASGR-1 gene that is also present in other European ancestry populations. This deletion leads to a frameshift predicted to generate a truncated ASGR-1 receptor subunit that is lacking both the oligomerization and extracellular carbohydrate recognition domains (also known as “CRD,” “carbohydrate binding domain” or “CBD”) or may generate an unstable and rapidly degraded transcript (and therefore no protein) due to nonsense mediated decay. In the present invention, whole-genome sequencing of the Icelandic population also discovered a second rare loss of function variant in the ASGR-1 gene; namely, a 4 base pair insertion in exon 7 (c. 469-472dupAACT or “W158×”). This 4 base pair insertion in exon 7 causes a frameshift and introduces a premature stop codon at amino acid 158 out of the 291 amino acid full length protein (NP_001662.1:p.W158X). This variant is predicted to encode a protein lacking the carbohydrate recognition domain of the receptor or may generate an unstable and rapidly degraded transcript (and therefore no protein) due to nonsense mediated decay. Furthermore, the W158X variant effects all reported refseq transcripts of ASGR-1 regardless of tissue or cell type of expression. Without wishing to be bound by any particular hypothesis, the analysis indicates that del12 and W158X results in lower non-HDL cholesterol levels, protection against CAD and MI, leading to prolonged life. Additionally, the analysis indicates that del12 and W158X also associates with increased levels of circulating ALP and vitamin B12. Supporting this del12 and W158X association with increased levels of ALP are data from mice having a Y272C variant in ASGR-1, showing that these mice exhibit a phenotype of increased plasma ALP (Sabrautzki et al., Mamm. Genome, 23, 416-430, 2012). The Y272 position in mouse ASGR-1 corresponds to the Y273 position in human ASGR-1 (see FIG. 1A).

The Ashwell-Morell Receptor (AMR), originally named the hepatic asialoglycoprotein receptor, was one of the first cellular receptors to be isolated and identified. (Grewal, Methods in Enzymology, Volume 479, Chapter 13, 2010, pp. 223-241). This receptor is also known as the Ashwell Receptor, the hepatic galactose/N-acetylgalactosamine (GalNAc) receptor, or the hepatic lectin receptor. However, this receptor is now more commonly known as “ASGPR,” or simply “ASGR.”

ASGR is a C-type lectin that is expressed on the surface of hepatocytes and is made up of 48 kDa major subunit(s) (ASGR-1) and 40 kDa minor subunit(s) (ASGR-2). (Roggenbuck et al., Autoimmune Highlights, 2012, 3:119-125). Functional variants of ASGR are formed by the oligomerization of the ASGR-1 and ASGR-2 subunits. (Grewal). The receptor complexes can comprise homo-oligomers and hetero-oligomers of the ASGR-1 and ASGR-2 subunits, with (ASGR-1)₂-(ASGR-2)₁ trimer being the most common form and having the highest affinity to substrate. (Grewal). Other identified forms of ASGR include (ASGR-1)₂, (ASGR-1)₃, (ASGR-1)₂-(ASGR-2)₂, (ASGR-1)₃-(ASGR-2)₂. (Grewal).

The polynucleotide and polypeptide sequences for several species of ASGR-1 and ASGR-2 are known. Table 1 presents sequences for human, mouse, rat, pig, dog and cynomolgus. FIGS. 1A, 1B and 2 present sequence alignments of various species of ASGR-1 and ASGR-2, and FIG. 3 presents a sequence alignment between human ASGR-1 and human ASGR-2.

ASGR-1 is a single pass transmembrane protein and is the major subunit of ASGR. The galactose (Gal) or N-acetylgalactosamine (GalNAc) residues of glycoproteins are exposed by removal of sialic acid by sialidases, hence the term asialoglycoprotein for the ligands of ASGR. Although ASGR expression is detected in other tissues, liver is the predominant site of expression. A circulating form of the receptor, generated from ASGR-1 transcripts lacking exon two, has also been reported. (Liu J, Hu B, Yang Y, et al. A new splice variant of the major subunit of human asialoglycoprotein receptor encodes a secreted form in hepatocytes. PloS one 2010; 5:e12934). The del12 and W158X variants are predicted to truncate both the membrane bound and the circulating form of the receptor, and as mentioned above, the W158X variant may generate an unstable and rapidly degraded transcript (and therefore no protein) due to nonsense mediated decay.

The primary reported function of ASGR is to bind and internalize glycoproteins in the circulation that contain terminal galactose or N-acetylgalactosamine residues (asialoglycoproteins), resulting in the clearance of these proteins from the circulation. (Roggenbuck). Reported endogenous ligands include components of the blood coagulation system, such as platelets and Von Willebrand Factor. (Grewal).

As used herein, the terms “ASGR, ASGR-1, and/or ASGR-2 function” or “ASGR, ASGR-1, and/or ASGR-2 activity” includes any biological effect of ASGR, ASGR-1 and/or ASGR-2. In certain embodiments, ASGR function or activity includes the ability of ASGR to interact or bind to a ligand. In some embodiments, ASGR function or activity is represented by the ability of ASGR to interact or bind to sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase. In some embodiments, ASGR function or activity includes any biological activity resulting from ASGR response. Exemplary activities include, but are not limited to, clearance of asialoglycoproteins from the circulation; clearance of IgA from circulation; removal of apoptotic cells; clearance of low density lipoprotein (LDL) and/or the disposal of cellular fibronectin (Roggenbuck).

Given the location of ASGR on the surface of liver hepatocytes and its implication in hepatocyte entry by certain viruses (Roggenbuck), the receptor has become a target of convenience for therapeutics that require delivery to the liver and internalization into the cells. Examples of these uses include the targeted delivery of doxorubicin to hepatocellular carcinoma (Wei et al., Int J Nanomedicine, 2015, 10:5123-37), gene delivery to hepatocytes (D'Souza et al., J Control Release, 2015, 203:126-39), and targeted delivery of siRNA to hepatocytes (Rajeev et al., Chembiochem, 2015, 16(6):903-8).

Although the ASGR and its ability to mediate endocytosis and degradation of desialated glycoproteins has been known for nearly 4 decades, the endogenous ligands and the physiological function of the receptor have been difficult to establish. (Weigel P H, Yik J H. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochimica et biophysica acta 2002; 1572:341-63). It has been reported that ASGR-1−/− mice (lacking any ASGR activity) thrive normally and do not accumulate desialylated glycoproteins in their circulation although they are unable to clear exogenously added asialoglycoproteins, suggesting that under normal physiological condition ASGR is not essential for homeostasis of circulating asialoglycoproteins. (Tozawa R, Ishibashi S, Osuga J, et al. Asialoglycoprotein receptor deficiency in mice lacking the major receptor subunit. Its obligate requirement for the stable expression of oligomeric receptor. The Journal of Biological Chemistry 2001; 276:12624-8).

In contrast to the ASGR-1 knockout mice which lack an apparent phenotype, the present invention has established a clear physiological role for human ASGR-1 in cardiovascular disease, for example, but not limited to, the regulation of non-HDL levels and modulation of CAD and MI risk. The present invention has also demonstrated the association of del12 and W158X with increased levels of circulating ALP and vitamin B12. Furthermore, the present invention shows that disturbing one allele of ASGR-1 appears to have an overall beneficial effect as heterozygotes carriers of del12 live on average 1.5 years longer than non-carriers.

Surprisingly, the various embodiments provided herein demonstrate that the del12 variant and the W158 variant both have an effect on non-HDL levels that is opposite to their effect on ALP and vitamin B12 levels; decreasing non-HDL and increasing ALP and vitamin B12. While not wishing to be bound by any particular hypothesis, it is important to note that the common variant previously described that associates with ALP and LDL cholesterol also has opposing effects on these serum components; hence ASGR-1 may affect the level of these molecules through different mechanisms. It is unlikely that the ALP increase mediated by del12 or W158X reflects an underlying liver disease since other measures of liver function are not affected. Both ALP and the vitamin B12 transporter in the circulation, haptocorrin, are asialylated glycoproteins known to bind ASGR-1 and be cleared from the circulation by the receptor (Tuin A, Huizinga-Van der Vlag A, van Loenen-Weemaes A M, Meijer D K, Poelstra K. On the role and fate of LPS-dephosphorylating activity in the rat liver. American Journal of Physiology Gastrointestinal and Liver Physiology 2006; 290:G377-85; Furger E, Fedosov S N, Lildballe D L, et al. Comparison of recombinant human haptocorrin expressed in human embryonic kidney cells and native haptocorrin. PloS one 2012; 7:e37421; Burger R L, Schneider R J, Mehlman C S, Allen R H. Human plasma R-type vitamin B12-binding proteins. II. The role of transcobalamin I, transcobalamin III, and the normal granulocyte vitamin B12-binding protein in the plasma transport of vitamin B12. The Journal of Biological Chemistry 1975; 250:7707-13; Steirer L M, Park E I, Townsend R R, Baenziger J U. The asialoglycoprotein receptor regulates levels of plasma glycoproteins terminating with sialic acid alpha2,6-galactose. The Journal of Biological Chemistry 2009; 284:3777-83). While not wishing to be bound by any particular hypothesis, the more likely reason for the increased levels of ALP and vitamin B12 in del12 carriers and in W158X carriers is decreased clearance of desialylated forms of these molecules from the circulation, due to reduced number of functional ASGR receptors in del12 carriers and in W158X carriers, suggesting a role for ASGR-1 in maintaining homeostasis of circulating ALP and vitamin B12.

While not wishing to be bound by any particular hypothesis, the decreased levels of non-HDL in del12 carriers and in W158X carriers in the face of reduced ASGR-1 function suggest that ASGR-1 affects non-HDL levels by mechanisms other than direct binding and endocytosis of cholesterol particles. In mice expressing a hypomorphic form of neuraminidase 1 (Neu1), a sialidase that cleaves the sialic acid residues thereby generating substrates for ASGR-1, the LDL receptor (LDLR) is sialylated and this form of the receptor was more stable and took up LDL cholesterol more avidly (LDL levels were decreased in these mice) than the asialylated form of the wild type LDLR (Yang A, Gyulay G, Mitchell M, White E, Trigatti B L Igdoura S A. Hypomorphic sialidase expression decreases serum cholesterol by downregulation of VLDL production in mice Journal of Lipid Research 2012; 53:2573-2585). Both ASGR and LDLR are located in clathrin-coated pits on hepatocytes and ASGR may be capable of interacting with the asialylated form of the LDLR and blocking its activity.

Two novel rare variants in ASGR-1 have been identified herein that play a role in cardiovascular disease, including, but not limited to, lowering non-HDL levels and protecting against CAD and MI. These variants disrupt ASGR-1 protein function. Accordingly, the present invention is further directed to methods of inhibiting ASGR function, methods of inhibiting ASGR-1 function and/or methods of inhibiting ASGR-2 function. The present invention is further directed to molecules (for example, but not limited to, antigen binding proteins or interfering RNA) that inhibit ASGR function, ASGR-1 function and/or ASGR-2 function.

Antigen Binding Proteins

In some embodiments, the invention comprises antigen binding proteins that bind to ASGR, ASGR-1, and/or ASGR-2 of different species, including, but not limited to, human, cynomolgus, porcine, canine, murine and rat. In some embodiments, the antigen binding proteins specifically bind to ASGR, ASGR-1, and/or ASGR-2 of different species, including, but not limited to, human, cynomolgus, porcine, canine, and murine and rat. Exemplary amino acid sequences of human, cyno, dog, pig, rat and mouse ASGR-1 and ASGR-2 are provided in FIGS. 1-3. In some embodiments, the antigen binding proteins further inhibit ASGR, ASGR-1 and/or ASGR-2 from binding to a ligand.

An “antigen binding protein” is a protein comprising an antigen binding fragment that binds to an antigen and, optionally, a scaffold or framework portion that allows the antigen binding fragment to adopt a conformation that promotes binding of the antigen binding protein to the antigen. In the instant application, the antigen is ASGR, ASGR-1 and/or ASGR-2 protein or a fragment thereof. In some embodiments, the antigen binding fragment comprises at least one CDR from an antibody that binds to the antigen, and in some embodiments comprises the heavy chain CDR3 from an antibody that binds to the antigen. In some embodiments, the antigen binding fragment comprises all three CDRs from the heavy chain of an antibody that binds to the antigen or from the light chain of an antibody that binds to the antigen. In still some embodiments, the antigen binding fragment comprises all six CDRs from an antibody that binds to the antigen (three from the heavy chain and three from the light chain). The antigen binding fragment in certain embodiments is an antibody fragment.

Nonlimiting examples of antigen binding proteins include antibodies, antibody fragments (e.g., an antigen binding fragment of an antibody), antibody derivatives, and antibody analogs. Further specific examples include, but are not limited to, a single-chain variable fragment (scFv), a nanobody (e.g. VH domain of camelid heavy chain antibodies; VHH fragment, see Cortez-Retamozo et al., Cancer Research, Vol. 64:2853-57, 2004), a Fab fragment, a Fab′ fragment, a F(ab′)2 fragment, a Fv fragment, a Fd fragment, and a complementarity determining region (CDR) fragment. These molecules can be derived from any mammalian source, such as human, mouse, rat, rabbit, or pig, dog, or camelid. Antibody fragments may compete for binding of a target antigen with an intact antibody and the fragments may be produced by the modification of intact antibodies (e.g. enzymatic or chemical cleavage) or synthesized de novo using recombinant DNA technologies or peptide synthesis. The antigen binding protein can comprise, for example, an alternative protein scaffold or artificial scaffold with grafted CDRs or CDR derivatives. Such scaffolds include, but are not limited to, antibody-derived scaffolds comprising mutations introduced to, for example, stabilize the three-dimensional structure of the antigen binding protein as well as wholly synthetic scaffolds comprising, for example, a biocompatible polymer. See, for example, Korndorfer et al., 2003, Proteins: Structure, Function, and Bioinformatics, Volume 53, Issue 1:121-129 (2003); Roque et al., Biotechnol. Prog. 20:639-654 (2004). In addition, peptide antibody mimetics (“PAMs”) can be used, as well as scaffolds based on antibody mimetics utilizing fibronectin components as a scaffold.

An antigen binding protein can also include a protein comprising one or more antibody fragments incorporated into a single polypeptide chain or into multiple polypeptide chains. For instance, antigen binding proteins can include, but are not limited to, a diabody (see, e.g., EP 404,097; WO 93/11161; and Hollinger et al., Proc. Natl. Acad. Sci. USA, Vol. 90:6444-6448, 1993); an intrabody; a domain antibody (single VL or VH domain or two or more VH domains joined by a peptide linker; see Ward et al., Nature, Vol. 341:544-546, 1989); a maxibody (2 scFvs fused to Fc region, see Fredericks et al., Protein Engineering, Design & Selection, Vol. 17:95-106, 2004 and Powers et al., Journal of Immunological Methods, Vol. 251:123-135, 2001); a triabody; a tetrabody; a minibody (scFv fused to CH3 domain; see Olafsen et al., Protein Eng Des Sel., Vol. 17:315-23, 2004); a peptibody (one or more peptides attached to an Fc region, see WO 00/24782); a linear antibody (a pair of tandem Fd segments (VH-CH1-VH-CH1) which, together with complementary light chain polypeptides, form a pair of antigen binding regions, see Zapata et al., Protein Eng., Vol. 8:1057-1062, 1995); a small modular immunopharmaceutical (see U.S. Patent Publication No. 20030133939); and immunoglobulin fusion proteins (e.g. IgG-scFv, IgG-Fab, 2scFv-IgG, 4scFv-IgG, VH-IgG, IgG-VH, and Fab-scFv-Fc).

In certain embodiments, an antigen binding protein can have, for example, the structure of an immunoglobulin. An “immunoglobulin” is a tetrameric molecule, with each tetramer comprising two identical pairs of polypeptide chains, each pair having one “light” (about 25 kDa) and one “heavy” chain (about 50-70 kDa). The amino-terminal portion of each chain includes a variable region of about 100 to 110 or more amino acids primarily responsible for antigen recognition. The carboxy-terminal portion of each chain defines a constant region primarily responsible for effector function.

Within light and heavy chains, the variable (V) and constant regions (C) are joined by a “J” region of about 12 or more amino acids, with the heavy chain also including a “D” region of about 10 more amino acids. See generally, Fundamental Immunology Ch. 7 (Paul, W., ed., 2nd ed. Raven Press, N.Y. (1989)) (incorporated by reference in its entirety for all purposes). The variable regions of each light/heavy chain pair form the antibody binding site such that an intact immunoglobulin has two binding sites.

Immunoglobulin chains exhibit the same general structure of relatively conserved framework regions (FR) joined by three hypervariable regions, also called complementarity determining regions or CDRs. From N-terminus to C-terminus, both light and heavy chains comprise the domains FR1, CDR1, FR2, CDR2, FR3, CDR3 and FR4.

Human light chains are classified as kappa and lambda light chains. The term “light chain” refers to a polypeptide comprising, from amino terminus to carboxyl terminus, a single immunoglobulin light chain variable region (VL) and a single immunoglobulin light chain constant domain (CL). Heavy chains are classified as mu (μ), delta (Δ), gamma (γ), alpha (α), and epsilon (ε), and define the antibody's isotype as IgM, IgD, IgG, IgA, and IgE, respectively. The term “heavy chain” refers to a polypeptide comprising, from amino terminus to carboxyl terminus, a single immunoglobulin heavy chain variable region (VH), an immunoglobulin heavy chain constant domain 1 (CH1), an immunoglobulin hinge region, an immunoglobulin heavy chain constant domain 2 (CH2), an immunoglobulin heavy chain constant domain 3 (CH3), and optionally an immunoglobulin heavy chain constant domain 4 (CH4). The IgG-class is further divided into subclasses, namely, IgG1, IgG2, IgG3, and IgG4. The IgA-class is further divided into subclasses, namely IgA1 and IgA2. The IgM has subclasses including, but not limited to, IgM1 and IgM2. The heavy chains in IgG, IgA, and IgD antibodies have three domains (CH1, CH2, and CH3), whereas the heavy chains in IgM and IgE antibodies have four domains (CH1, CH2, CH3, and CH4). The immunoglobulin heavy chain constant domains can be from any immunoglobulin isotype, including subtypes. The antibody chains are linked together via inter-polypeptide disulfide bonds between the CL domain and the CH1 domain (i.e. between the light and heavy chain) and between the hinge regions of the antibody heavy chains.

The term “antibody” refers to an intact immunoglobulin of any isotype, and includes, for instance, chimeric, humanized, human, and bispecific antibodies. An “antibody” is a species of an antigen binding protein. An intact antibody will generally comprise at least two full-length heavy chains and two full-length light chains. Antibody sequences can be derived solely from a single species, or can be “chimeric,” that is, different portions of the antibody can be derived from two different species as described further below. Unless otherwise indicated, the term “antibody” also includes antibodies comprising two substantially full-length heavy chains and two substantially full-length light chains provided the antibodies retain the same or similar binding and/or function as the antibody comprised of two full length light and heavy chains. For example, antibodies having 1, 2, 3, 4, or 5 amino acid residue substitutions, insertions or deletions at the N-terminus and/or C-terminus of the heavy and/or light chains are included in the definition provided that the antibodies retain the same or similar binding and/or function as the antibodies comprising two full length heavy chains and two full length light chains. Furthermore, unless explicitly excluded, antibodies include, for example, monoclonal antibodies, polyclonal antibodies, chimeric antibodies, humanized antibodies, human antibodies, bispecific antibodies, and synthetic antibodies. In some sections of the present disclosure, examples of antigen binding proteins are described herein in terms of the hybridoma line number as “number/letter/number” (e.g., 25A4). In these cases, the exact name denotes a specific monoclonal antibody derived from a specific hybridoma having a specific light chain variable region and heavy chain variable region. In some sections of the present disclosure, examples of antigen binding proteins are described herein in terms of “number/letter/number/“dot”/number” (e.g., 25A4.001) or number/letter/number/“dot”/number/“dot”/number (e.g., 25A4.001.001). In these cases, the name denotes a variant of a specific antibody having a light chain variable region and a heavy chain variable region that is related to, but distinct from the antibody derived from a hybridoma. That is, for example, an antigen binding protein named 25A4 is not the same as an antibody named 25A4.001 or an antibody named 25A4.001.001.

A “polyclonal antibody” refers to a population of antibodies that are typically widely varied in composition and binding specificity. A “monoclonal antibody” (“mAb”) as used herein refers to one or more of a population of antibodies having identical sequences. Monoclonal antibodies bind to the antigen at a particular epitope on the antigen.

In some embodiments, the antigen binding protein is a “fragment” or “antigen binding fragment” of an antibody. As used herein and unless otherwise specified, an “antibody fragment” refers to the Fab, Fab′, F(ab′)2, and Fv fragments that contain at least one CDR of an immunoglobulin that is sufficient to confer specific antigen binding to ASGR, ASGR-1 and/or ASGR-2. Antibody fragments may be produced by recombinant DNA techniques or by enzymatic or chemical cleavage of intact antibodies.

A Fab fragment is a monovalent fragment having the VL, VH, CL and CH1 domains; a F(ab′)2 fragment is a bivalent fragment having two Fab fragments linked by a disulfide bridge at the hinge region; a Fd fragment has the VH and CH1 domains; an Fv fragment has the VL and VH domains of a single arm of an antibody; and a dAb fragment has a VH domain, a VL domain, or an antigen-binding fragment of a VH or VL domain (U.S. Pat. Nos. 6,846,634, 6,696,245, US App. Pub. No. 05/0202512, 04/0202995, 04/0038291, 04/0009507, 03/0039958, Ward et al., Nature 341:544-546 (1989)). In certain embodiments, these antibody fragments can be incorporated into single domain antibodies, single-chain antibodies, maxibodies, minibodies, intrabodies, diabodies, triabodies, tetrabodies, v-NAR and bis-scFv (see e.g., Hollinger and Hudson, 2005, Nature Biotechnology, 23, 9, 1126-1136). Other antigen binding proteins envisioned are antibody polypeptides such as those disclosed in U.S. Pat. No. 6,703,199, including fibronectin polypeptide monobodies, the polypeptides as disclosed in U.S. Patent Publication 2005/0238646. In some embodiments, the antibodies comprise at least one CDR set forth in Tables 2 or 6 herein.

A “single-chain variable fragment” (“scFv”) is a fusion protein in which a VL and a VH region are joined via a linker (e.g., a synthetic sequence of amino acid residues) to form a continuous protein chain wherein the linker is long enough to allow the protein chain to fold back on itself and form a monovalent antigen binding site (see, e.g., Bird et al., Science 242:423-26 (1988) and Huston et al., 1988, Proc. Natl. Acad. Sci. USA 85:5879-83 (1988)). For the sake of clarity, a “single-chain variable fragment” is not an antibody or an antibody fragment as defined herein. Diabodies are bivalent antibodies comprising two polypeptide chains, wherein each polypeptide chain comprises VH and VL domains joined by a linker that is too short to allow for pairing between two domains on the same chain, thus allowing each domain to pair with a complementary domain on another polypeptide chain (see, e.g., Holliger et al., 1993, Proc. Natl. Acad. Sci. USA 90:6444-48 (1993), and Poljak et al., Structure 2:1121-23 (1994)). If the two polypeptide chains of a diabody are identical, then a diabody resulting from their pairing will have two identical antigen binding sites. Polypeptide chains having different sequences can be used to make a diabody with two different antigen binding sites. Similarly, tribodies and tetrabodies are antibodies comprising three and four polypeptide chains, respectively, and forming three and four antigen binding sites, respectively, which can be the same or different.

The term “CDR” refers to the complementarity determining region (also termed “minimal recognition units” or “hypervariable region”) within antibody variable sequences. The CDRs permit the antigen binding protein to specifically bind to a particular antigen of interest. There are three heavy chain variable region CDRs (CDRH1, CDRH2 and CDRH3) and three light chain variable region CDRs (CDRL1, CDRL2 and CDRL3). The CDRs in each of the two chains typically are aligned by the framework regions to form a structure that binds specifically to a specific epitope or domain on the target protein. From N-terminus to C-terminus, naturally-occurring light and heavy chain variable regions both typically conform to the following order of these elements: FR1, CDR1, FR2, CDR2, FR3, CDR3 and FR4. A numbering system has been devised for assigning numbers to amino acids that occupy positions in each of these domains. This numbering system is defined in Kabat Sequences of Proteins of Immunological Interest (1987 and 1991, NIH, Bethesda, Md.), or Chothia & Lesk, 1987, J. Mol. Biol. 196:901-917; Chothia et al., 1989, Nature 342:878-883. Complementarity determining regions (CDRs) and framework regions (FR) of a given antibody may be identified using this system. Other numbering systems for the amino acids in immunoglobulin chains include IMGT® (the international ImMunoGeneTics information system; Lefranc et al, Dev. Comp. Immunol. 29:185-203; 2005) and AHo (Honegger and Pluckthun, J. Mol. Biol. 309(3):657-670; 2001). One or more CDRs may be incorporated into a molecule either covalently or noncovalently to make it an antigen binding protein.

In some embodiments, an antigen binding protein of the invention may incorporate the CDR(s) as part of a larger polypeptide chain, may covalently link the CDR(s) to another polypeptide chain, or may incorporate the CDR(s) noncovalently. The antigen binding molecules may comprise at least one of the CDRs described herein incorporated into a biocompatible framework structure. In one example, the biocompatible framework structure comprises a polypeptide or portion thereof that is sufficient to form a conformationally stable structural support, or framework, or scaffold, which is able to display one or more sequences of amino acids that bind to an antigen (e.g., CDRs, a variable region, etc.) in a localized surface region. Such structures can be a naturally occurring polypeptide or polypeptide “fold” (a structural motif), or can have one or more modifications, such as additions, deletions or substitutions of amino acids, relative to a naturally occurring polypeptide or fold. These scaffolds can be derived from a polypeptide of any species (or of more than one species), such as a human, other mammal, other vertebrate, invertebrate, plant, bacteria or virus.

Typically the biocompatible framework structures are based on protein scaffolds or skeletons other than immunoglobulin domains. For example, those based on fibronectin, ankyrin, lipocalin, neocarzinostain, cytochrome b, CP1 zinc finger, PST1, coiled coil, LACI-D1, Z domain and tendamistat domains may be used (See e.g., Nygren and Uhlen, 1997, Current Opinion in Structural Biology, 7, 463-469).

An antigen binding protein may have one or more binding sites. If there is more than one binding site, the binding sites may be identical to one another or may be different. For example, an antibody typically has two identical binding sites, while a “bispecific” or “bifunctional” antibody has two different binding sites. The two binding sites of a bispecific antigen binding protein or antibody will bind to two different epitopes, which can reside on the same or different protein targets.

In some embodiments, the ASGR-1 antigen binding protein is a bispecific antibody. In certain embodiments, a bispecific antibody binds to ASGR, ASGR-1 or ASGR-2 and PCSK9. In some embodiments, a bispecific antibody will bind to the ASGR-1 CBD and will inhibit ASGR-1 function, in addition to binding to PCSK9 and inhibiting the binding of PCSK9 to the LDLR. Methods of making bispecific antibodies are known in the art. One such method of making a “bispecific,” or “bifunctional” antigen binding protein or antibody involves the fusion of hybridomas or linking of Fab′ fragments. See, e.g., Songsivilai and Lachmann, 1990, Clin. Exp. Immunol. 79:315-321; Kostelny et al., 1992, J. Immunol. 148:1547-1553. Another method involves engineering the Fc portion of the heavy chains such as to create “knobs” and “holes” which facilitate heterodimer formation of the heavy chains when co-expressed in a cell. U.S. Pat. No. 7,695,963. Still another method also involves engineering the Fc portion of the heavy chain but uses electrostatic steering to encourage heterodimer formation while discouraging homodimer formation of the heavy chains when co-expressed in a cell. WO 09/089,004, which is incorporated herein by reference in its entirety.

The term “human antibody” includes antibodies having antibody regions such as variable and constant regions or domains which correspond substantially to human germline immunoglobulin sequences known in the art, including, for example, those described by Kabat et al. (1991) (loc. cit.). The human antibodies of the invention may include amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo), for example in the CDRs, and in particular, in CDR3. The human antibodies can have at least one, two, three, four, five, or more positions replaced with an amino acid residue that is not encoded by the human germline immunoglobulin sequence. The definition of human antibodies as used herein also contemplates fully human antibodies, which include only non-artificially and/or genetically altered human sequences of antibodies as those can be derived by using technologies or systems known in the art, such as for example, phage display technology or transgenic mouse technology, including but not limited to the Xenomouse.

A humanized antibody has a sequence that differs from the sequence of an antibody derived from a non-human species by one or more amino acid substitutions, deletions, and/or additions, such that the humanized antibody is less likely to induce an immune response, and/or induces a less severe immune response, as compared to the non-human species antibody, when it is administered to a human subject. In one embodiment, certain amino acids in the framework and constant domains of the heavy and/or light chains of the non-human species antibody are mutated to produce the humanized antibody. In another embodiment, the constant domain(s) from a human antibody are fused to the variable domain(s) of a non-human species. In another embodiment, one or more amino acid residues in one or more CDR sequences of a non-human antibody are changed to reduce the likely immunogenicity of the non-human antibody when it is administered to a human subject, wherein the changed amino acid residues either are not critical for immunospecific binding of the antibody to its antigen, or the changes to the amino acid sequence that are made are conservative changes, such that the binding of the humanized antibody to the antigen is not significantly worse than the binding of the non-human antibody to the antigen. Examples of how to make humanized antibodies may be found in U.S. Pat. Nos. 6,054,297, 5,886,152 and 5,877,293.

The term “chimeric antibody” refers to an antibody that contains one or more regions from one antibody and one or more regions from one or more other antibodies. In one embodiment, one or more of the CDRs are derived from a human anti-ASGR, ASGR-1 or ASGR-2 antibody. In another embodiment, all of the CDRs are derived from a human anti-ASGR, ASGR-1 or ASGR-2 antibody. In another embodiment, the CDRs from more than one human anti-ASGR, ASGR-1 or ASGR-2 antibodies are mixed and matched in a chimeric antibody. For instance, a chimeric antibody may comprise a CDR1 from the light chain of a first human anti-ASGR, ASGR-1 or ASGR-2 antibody, a CDR2 and a CDR3 from the light chain of a second human anti-ASGR, ASGR-1 or ASGR-2 antibody, and the CDRs from the heavy chain from a third anti-ASGR, ASGR-1 or ASGR-2 antibody. Further, the framework regions may be derived from one of the same anti-ASGR, ASGR-1 or ASGR-2 antibodies, from one or more different antibodies, such as a human antibody, or from a humanized antibody. In one example of a chimeric antibody, a portion of the heavy and/or light chain is identical with, homologous to, or derived from an antibody from a particular species or belonging to a particular antibody class or subclass, while the remainder of the chain(s) is/are identical with, homologous to, or derived from an antibody or antibodies from another species or belonging to another antibody class or subclass. Also included are fragments of such antibodies that exhibit the desired biological activity.

A “neutralizing antigen binding protein” or “inhibitory antigen binding protein” or “antagonizing antigen binding protein” (e.g., “neutralizing antibody” or “inhibitory antibody” or “antagonizing antibody”) refers to an antigen binding protein or antibody, respectively, that binds to a target molecule and reduces and/or prevents the biological effect of that target molecule. This can be done, for example, by directly blocking a site on the target molecule through which the target molecule interacts with other molecules (e.g. blocking a ligand binding site of a receptor) or by indirectly blocking a site on the target molecule through which the target molecule interacts with other molecules (such as structural or energetic alterations in the target molecule). In some embodiments, these terms can also denote an antigen binding protein or antibody that prevents the target molecule to which it is bound from performing a biological function. In assessing the binding and/or specificity of an antigen binding protein, e.g., an antibody or immunologically functional fragment thereof, an antibody or fragment can substantially inhibit binding of a target molecule to its binding partner when an excess of antibody reduces the quantity of binding partner bound to the target molecule by at least about 1-20, 20-30%, 30-40%, 40-50%, 50-60%, 60-70%, 70-80%, 80-85%, 85-90%, 90-95%, 95-97%, 97-98%, 98-99%, 99.5%, 99.9% and 100%. In some embodiments, inhibition is complete. The measurement of reduction of binding is done using various assays known to those skilled in the art, (e.g., an in vitro competitive binding assay) and performed using relevant control molecules so that actual inhibition is measured. For example, numerous competition assays are well known in the art, with nonlimiting examples being competition ELISA, use of the BiaCore® platform, the Kinexa® platform, or the like. Further examples include: solid phase direct or indirect radioimmunoas say (MA), solid phase direct or indirect enzyme immunoassay (EIA), sandwich competition assay (see, e.g., Stahli et al., 1983, Methods in Enzymology 9:242-253); solid phase direct biotin-avidin EIA (see, e.g., Kirkland et al., 1986, J. Immunol. 137:3614-3619) solid phase direct labeled assay, solid phase direct labeled sandwich assay (see, e.g., Harlow and Lane, 1988, Antibodies, A Laboratory Manual, Cold Spring Harbor Press); solid phase direct label RIA using 1-125 label (see, e.g., Morel et al., 1988, Molec. Immunol. 25:7-15); solid phase direct biotin-avidin EIA (see, e.g., Cheung, et al., 1990, Virology 176:546-552); and direct labeled RIA (Moldenhauer et al., 1990, Scand. J. Immunol. 32:7-82). Typically, such an assay involves the use of purified antigen bound to a solid surface or cells bearing either of these, an unlabelled test antigen binding protein and a labeled reference antigen binding protein. In some embodiments, in the case of ASGR, ASGR-1 and/or ASGR-2, such a neutralizing antigen binding protein or antibody can diminish the ability of ASGR, ASGR-1 and/or ASGR-2 to bind to a ligand. In some embodiments, the neutralizing ability is characterized and/or described via a competition assay. In some embodiments, the neutralizing ability is described in terms of an IC₅₀ or EC₅₀ value. The antigen binding proteins in at least Table C are strong neutralizers. In some embodiments, the antibodies or antigen binding proteins neutralize by binding to ASGR, ASGR-1 and/or ASGR-2 and preventing ASGR, ASGR-1 and/or ASGR-2 from binding to a ligand, including sugars such as lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars, such as fetuin, orosomucoid and/or alkaline phosphatase (or reducing the ability of ASGR, ASGR-1 and/or ASGR-2 to bind to ligand).

Competitive inhibition can be measured by determining the amount of labelled ligand bound to the solid surface or cells in the presence of the test antigen binding protein. Usually the test antigen binding protein is present in excess. Antigen binding proteins or antibodies identified by competition assay (competing antigen binding proteins or antibodies) include antigen binding proteins binding to the same epitope as the reference antigen binding proteins and antigen binding proteins binding to an adjacent epitope sufficiently proximal to the epitope bound by the reference antigen binding protein for steric hindrance to occur. Usually, when a competing antigen binding protein is present in excess, it will inhibit (e.g., reduce) specific binding of a reference antigen binding protein to a target antigen by at least 40-45%, 45-50%, 50-55%, 55-60%, 60-65%, 65-70%, 70-75% or 75% or more. In some embodiments, binding is inhibited by at least 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, or 95%. In some embodiments, binding is inhibited by at least 80-85%, 85-90%, 90-95%, 95-97%, or 97% or more, including up to 100% inhibition.

In some embodiments, a ligand binding assay is used where cells expressing the target protein (e.g., ASGR-1) are mixed with antigen binding proteins and incubated for a time period, then washed. These cells are then incubated with labelled ligand (e.g., β-GalNAc) for a time period and then washed and analyzed for ligand binding, where reduced ligand binding as compared to a relevant control antigen binding protein indicates inhibition of binding due to the antigen binding protein blocking or inhibiting this binding.

Another manner in which the reduction in binding can be measured is the half maximal inhibitory concentration (IC50). The IC50 measures the amount or concentration of antigen binding protein that is needed to inhibit a given attribute (e.g., ligand binding) by half. In certain embodiments, the antigen binding proteins (e.g., human antibodies) have an IC50 value of 90 nM or less, in another embodiment, an IC50 value of 80 nM or less, in another embodiment, 70 nM or less, in another embodiment, 60 nM or less, in another embodiment, 50 nM or less, in another embodiment, 40 nM or less, in another embodiment, 30 nM or less, in another embodiment 25 nM or less.

In certain embodiments, the antigen binding proteins of the invention bind to an ASGR-1 monomer. In some embodiments, the antigen binding proteins of the invention bind to an ASGR-1 oligomer. In further embodiments, the antigen binding proteins of the invention bind to an ASGR-2 monomer. In some embodiments, the antigen binding proteins of the invention bind to an ASGR-2 oligomer. In certain embodiments, the antigen binding proteins of the invention bind to both ASGR-1 monomers and ASGR-2 monomers. In certain embodiments, the antigen binding proteins of the invention bind to an ASGR oligomer comprising an (ASGR-1)₂-(ASGR-2)₁ trimer. In some embodiments, the antigen binding proteins of the invention bind to an ASGR oligomer comprising an (ASGR-1)₂ dimer. In further embodiments, the antigen binding proteins of the invention bind to an ASGR oligomer comprising an (ASGR-1)₃ trimer. In yet further embodiments, the antigen binding proteins of the invention bind to an ASGR oligomer comprising an (ASGR-1)₂-(ASGR-2)₂ tetramer. In further embodiments, the antigen binding proteins of the invention bind to an ASGR oligomer comprising an (ASGR-1)₃-(ASGR-2)₂ pentamer. In some embodiments, the antigen binding proteins of the invention bind to a multimeric complex comprising at least two subunits of ASGR-1 and/or ASGR-2.

In certain embodiments, the antigen binding proteins (e.g., antibodies, antibody fragments, etc.) bind to ASGR, ASGR-1 and/or ASGR-2 and inhibit ASGR, ASGR-1 and/or ASGR-2 from binding to a ligand, wherein the antigen binding proteins comprise specific amino acid residues at particular positons in the molecule (e.g., in the VH, VL or CDRs). These residues may be involved in the binding properties of desired molecules (e.g., part of the paratope). A “paratope” are used herein is the location in an antibody that binds to the antigen. The paratope can comprise several amino acid residues from the VH and/or VL CDRs, and also can comprise residues from the framework regions. The paratope binds to the antigen's epitope. Paratopes can be determined using methodologies similar to those described determining epitopes. Once the amino acid residues involved in the binding properties of desired molecules, are identified, this information can be used to design antigen binding proteins (e.g., antibodies, antibody fragments, etc.) that can bind to ASGR, ASGR-1 and/or ASGR-2 and inhibit ASGR function (e.g., inhibit ASGR, ASGR-1 and/or ASGR-2 from binding to ligand).

The binding site (or interface) between the representative antibodies and human ASGR-1 can be determined/defined a number of ways. For example, binding of representative antigen binding proteins (e.g., antibodies) to human ASGR-1 was analyzed in Example 10 using X-ray crystallography, and the binding site or interface was determined using distance. The crystal structure of the antibody/huASGR1 complex provides information as to which residues of representative antibodies form the interface with human ASGR-1. As mentioned above, one of ordinary skill in the art may use this information to design antigen binding proteins and antigen binding protein variants, including those that contain variable domains having 90% identity or greater, 95% identity or greater, 97% identity or greater, 99% identity or greater, or those antigen binding protein variants that contain variable domains having 20 or less, 15 or less, or 10 or less, or 5 or less insertions, deletions, and/or substitutions within the light chain and/or heavy chain variable domain of the antigen binding proteins disclosed herein. One may wish to maintain the amino acids within the interface while altering non-interface residues. Thus, in some embodiments, one may design and create antigen binding proteins and antigen binding protein variants of the antigen binding proteins disclosed herein having one or more amino acid additions, substitutions, and/or deletions within one or more CDRs that maintain binding to human ASGR-1 and inhibit ASGR, ASGR-1 and/or ASGR-2 function (e.g., inhibit ASGR, ASGR-1 and or ASGR-2 from binding to ligand).

In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13 or all amino acid residues selected from the group consisting of Q27, R30, D32, H91, Y92, S93, Y94, I2, G28, I29, L33, Q90, P95, and R96 of SEQ ID NO:25010 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or all amino acid residues selected from the group consisting of S30, N31, W52, Y53, D54, S56, N57, Y59, Y101, S102, S103, G104, W105, Y106, D107, Y32, V33, V50, G55, K58, N74, E99, V100, and Y108 of SEQ ID NO:29016. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6 or all amino acid residues selected from the group consisting of Q27, R30, D32, H91, Y92, S93, and Y94 of SEQ ID NO:25010 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or all amino acid residues selected from the group consisting of S30, N31, W52, Y53, D54, S56, N57, Y59, Y101, S102, S103, G104, W105, Y106, and D107 of SEQ ID NO:29016. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or all amino acid residues selected from the group consisting of H31, S33, N34, N36, Y38, W56, Y97, Y98, I29, S32, N35, N37, Y55, T59, Q96, N99, T100 of SEQ ID NO:25164 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26 or all amino acid residues selected from the group consisting of T28, F29, T30, N31, Y32, D33, W50, H52, S55, N57, S99, S100, G101, W102, Y103, Y27, 134, N35, W47, M51, P53, N54, G56, T58, G59, Y104, D106 of SEQ ID NO:29170. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7 or all amino acid residues selected from the group consisting H31, S33, N34, N36, Y38, W56, Y97, Y98 of SEQ ID NO:25164 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or all amino acid residues selected from the group consisting of T28, F29, T30, N31, Y32, D33, W50, H52, S55, N57, S99, S100, G101, W102, Y103 of SEQ ID NO:29170. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18 or all amino acid residues selected from the group consisting of 130, Y32, T91, Y92, S93, T94, 196, I2, Q27, N28, I29, S31, L33, N34, T50, S67, Q89, Q90, P95 of SEQ ID NO:24908 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or all amino acid residues selected from the group consisting of S30, S31, ISO, W52, H53, S56, N57, Y59, S01, M102, G103, T28, F29, F32, G33, H35, W47, I51, D54, K58, D99, L100, G104 of SEQ ID NO:28914. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6 or all amino acid residues selected from the group consisting 130, Y32, T91, Y92, S93, T94, 196 of SEQ ID NO:24908 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or all amino acid residues selected from the group consisting of S30, S31, I50, W52, H53, S56, N57, Y59, S01, M102, G103 of SEQ ID NO:28914. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or all amino acid residues selected from the group consisting of Y32, S91, Y92, R93, Thr94, Pro95, F97, Ile2, Q27, N28, NAG100, Ile29, S30, S31, Q90, and L96 of SEQ ID NO:24362 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or all amino acid residues selected from the group consisting of A33, Val50, Ile51, S52, R53, S54, G55, G56, Y57, Y59, R99, A101, A103, G104, E106, S30, S31, Y32, Met34, N35, W47, S49, Thr58, R72, N74, L100, Val102, and S105 of SEQ ID NO:28368. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, or all amino acid residues selected from the group consisting of Y32, S91, Y92, R93, Thr94, Pro95, and F97 of SEQ ID NO:24362, and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or all amino acid residues selected from the group consisting of A33, Val50, Ile51, S52, R53, S54, G55, G56, Y57, Y59, R99, A101, A103, G104, and E106 of SEQ ID NO:28368. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17 or all amino acid residues selected from the group consisting of Q27, W32, A91, N92, S93, F94, F96, D1, I2, G28, I29, S30, R31, Y49, G50, Q89, Q90, and P95 of SEQ ID NO:24930 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or all amino acid residues selected from the group consisting of Y33, H35, W50, H52, S55, G57, T58, N59, D99, G100, T101, S102, D31, Y32, L34, W47, I51, N54, G56, Y60, Q65, S103, and F104 of SEQ ID NO:28936. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6 or all amino acid residues selected from the group consisting of Q27, W32, A91, N92, S93, F94, and F96 of SEQ ID NO:24930 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or all amino acid residues selected from the group consisting of Y33, H35, W50, H52, S55, G57, T58, N59, D99, G100, T101, and 5102 of SEQ ID NO:28936. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or all amino acid residue selected from the group consisting of Y32, Y49, T50, Q55, S91, H92, S93, F94, F96, S28, I29, T30, N33, L46, S53, L54, S56, Q89, Q90, and P95 of SEQ ID NO:28074 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28 or all amino acid residues selected from the group consisting of G26, F27, T28, S30, S31, Y32, S33, S52, G53, S54, S56, Y57, Y59, R98, G100, S101, R102, V2, F29, N35, S50, T51, S55, I58, R72, G99, G103, F104 and D105 of SEQ ID NO:32080. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8 or all amino acid residues selected from the group consisting of Y32, Y49, T50, Q55, S91, H92, S93, F94, and F96 of SEQ ID NO:28074 and/or heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16 or all amino acid residues selected from the group consisting of G26, F27, T28, S30, S31, Y32, S33, S52, G53, S54, S56, Y57, Y59, R98, G100, S101 and R102 of SEQ ID NO:32080. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 or all amino acid residues selected from the group consisting of V29, S30, I32, Y33, L47, Y50, R55, A56, T57, Y94, G28, N31, L48, I49, G51, N54, G58, I59, S68, G69, D93, and S95 of SEQ ID NO:26814 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or all amino acid residues selected from the group consisting of V31, Y32, Y33, W50, N52, S55, G57, R98, G99, Y100, D101, I102, T204, V2, Y27, T30, L34, N35, P53, N54, G56, T58, N59, A97, L103, and G105 of SEQ ID NO:30820. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or all amino acid residues selected from the group consisting of V29, S30, I32, Y33, L47, Y50, R55, A56, T57, and Y94 of SEQ ID NO:26814 and/or heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or all amino acid residues selected from the group consisting of V31, Y32, Y33, W50, N52, S55, G57, R98, G99, Y100, D101, I102, and T204 of SEQ ID NO:30820. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3 or all amino acid residues selected from the group consisting of N31, Y50, V51, Q54 SEQ ID NO:27482; and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or all amino acid residues selected from the group consisting of N30, S31, Y32, S52, Y54, N55, K59, R98, D100, F101, W102, S103, G104, Y105, K107, D110, V2, Y27, T28, F29, G33, W50, A53, G56, N57, H99, Y106, or G108 of SEQ ID NO:31488. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or all amino acid residues selected from the group consisting of N30, S31, Y32, S52, Y54, N55, K59, R98, D100, F101, W102, S103, G104, Y105, K107, and D110 of SEQ ID NO:31488. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or all amino acid residues selected from the group consisting of Y33, Y50, D51, N53, K54, S57, V34, S52, R55, P56, G58, and G65 of SEQ ID NO:27780 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or all amino acid residues selected from the group consisting of Q1, V2, F27, S30, S31, Y32, Y53, D54, W99, Y100, Y101, Y102, G26, T28, F29, G33, W52, G55, R72, N74, N98, Y103, Y104, D107, and V108 of SEQ ID NO:31786. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5 or all amino acid residues selected from the group consisting of Y33, Y50, D51, N53, K54 and S57 of SEQ ID NO:27780 and/or heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or all amino acid residues selected from the group consisting of Q1, V2, F27, S30, S31, Y32, Y53, D54, W99, Y100, Y101, and Y102 of SEQ ID NO:31786. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or all amino acid residues selected from the group consisting of H31, G32, D33, G34, K35, Y37, 197, Q98, 199, I2, Q27, S28, L29, L30, T36, E55, Q95, S96, P100, and W101 of SEQ ID NO:26536 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or all amino acid residues selected from the group consisting of S31, W52, Y53, D54, Y57, Y59, D102, F103, W104, T28, S30, Y32, G33, W47, I50, I51, S56, K58, Y60, K65, D99, H101, S105, and G106 of SEQ ID NO:30542. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8 or all amino acid residues selected from the group consisting of H31, G32, D33, G34, K35, Y37, 197, Q98, and 199 of SEQ ID NO:26536 and/or heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8 or all amino acid residues selected from the group consisting of S31, W52, Y53, D54, Y57, Y59, D102, F103 and W104 of SEQ ID NO:30542. In some embodiments, the antigen binding protein or the antibody comprises a light chain variable region and/or a heavy chain variable region, wherein the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or all amino acid residues selected from the group consisting of N30, S31, Y33, F50, S54, S68, Y92, E93, W97, S28, V29, G32, L47, G51, A52, S53, R55, A56, G69, Q90, Q91, S94, and S95 of SEQ ID NO:26826 and/or the heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or all amino acid residues selected from the group consisting of R30, Y31, Y33, E50, S54, S56, N58, D98, Y99, G100, S28, Y32, W34, S35, W47, G49, I51, S52, H53, G55, T57, R97, A101, F102 and D103 of SEQ ID NO:30832. In some embodiments, the light chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8 or all amino acid residues selected from the group consisting of N30, S31, Y33, F50, S54, S68, Y92, E93, and W97 of SEQ ID NO:26826 and/or heavy chain variable region comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9 or all amino acid residues selected from the group consisting of R30, Y31, Y33, E50, S54, S56, N58, D98, Y99 and G100 of SEQ ID NO:30832.

In further embodiments, consensus sequences among the antigen binding proteins of the inventions are envisioned. For example, the variable heavy chain and variable light chain regions (VH and VL) and the CDRs (HCDR1/2/3 and LCDR1/2/3) of the invention include consensus sequences derived from groups of related monoclonal antibodies. In some embodiments, the antigen binding proteins (e.g., antibodies) may be related by both sequence homology and function. As described herein, a “consensus sequence” refers to amino acid sequences having conserved amino acids common among a number of sequences and amino acids that vary within given amino acid sequences at certain positions. In some embodiments, the varied amino acid at a certain position is a substitution. In some embodiments, the varied amino acid at a certain position is a deletion. In some embodiments, the varied amino acid at a certain position is an addition or insertion. These varied amino acids will be apparent to one of skill in the art when analyzing particular antibody VH, VL and/or CDR sequences.

For example, antibody sequences were analyzed using the following methodology. The Smith-Waterman algorithm was used to align amino acid sequences against translated IMGT germline V, D and J genes. The V gene was located first, then the J gene was located in the region downstream from located V gene, and finally the D gene was located in the region between V and J regions. Note, that since D gene is a relatively short sequence that is located in the hypervariable CDR3 region, a spurious match is possible and as such, was taken into consideration.

Sequences from each group were then subjected to sequence similarity alignment interrogation using a program that employs a standard ClustalW algorithm (see, Thompson et al., 1994, Nucleic Acids Res. 22:4673-4680). In some cases, the Biosum cost matrix was used with a gap creation penalty of 50 was employed along with a gap extension penalty of 0.1. The sequence logos were generated by Geneious (v8.1.7, Biomatters) once the alignments were made and then exported as PDF images. The consensus sequences were generated in Geneious (v8.1.7, Biomatters) with a 0% threshold and exported as FASTA files. Amino acids that varied within each group were noted with the notation X within each consensus sequence. See Table 19A VH Consensus 1-14 and Table 20A VL Consensus 1-14 in FIG. 55, and Tables 21-48 in FIG. 56 for the consensus sequences resulting from this analysis. In other cases, the consensus sequences were generated in Abinitio. See Table 19A VH Consensus-15-60 and Table 20A VL Consensus 15-54 in FIG. 55, and Tables 49-134 in FIG. 57 for the consensus sequences resulting from this analysis.

Alternatively, different methods of analysis readily available to one of skill in the art can be used. For example, consensus sequences can be determined using standard phylogenic analyses of the CDRs corresponding to the VH (i.e., Variable Heavy, etc.) & VL (i.e., Variable Light, etc.) of antibodies. For example, amino acid sequences corresponding to the entire variable domains of either VH or VL can be converted to FASTA formatting for ease in processing comparative alignments and inferring phylogenies. Next, framework regions of these sequences can be replaced with an artificial linker sequence so that examination of the CDRs alone can be performed without introducing any amino acid position weighting bias due to coincident events (e.g., such as unrelated antibodies that serendipitously share a common germline framework heritage) while still keeping CDRs contiguous within the same sequence corresponding to a VH or VL. VH or VL sequences of this format can then be subjected to sequence similarity alignment interrogation using a program that employs a standard ClustalW-like algorithm (see, Thompson et al., 1994, Nucleic Acids Res. 22:4673-4680). A gap creation penalty of 8.0 can be employed along with a gap extension penalty of 2.0. This program likewise generated phylograms (phylogenic tree illustrations) based on sequence similarity alignments using either UPGMA (unweighted pair group method using arithmetic averages) or Neighbor-Joining methods (see, Saitou and Nei, 1987, Molecular Biology and Evolution 4:406-425) to construct & illustrate similarity and distinction of sequence groups via branch length comparison and grouping. The original sequence alignments generated can be employed to empirically examine and document the occurrence of amino acids tolerated at each position with a consensus group. Consensus sequences for the groups of similar sequences within each CDR can then be prepared.

In another type of approach, CDR consensus sequences can be determined for each separate CDR, independently of their contiguous context within the same sequence corresponding to a VH or VL. In this approach the consensus sequences can be determined by aligning each H-CDR1, H-CDR2, H-CDR3, L-CDR1, L-CDR2, and L-CDR3 in groups, i.e., by aligning the individual H-CDR1 sequences of the antigen binding proteins to determine a H-CDR1 consensus sequence, by aligning the individual H-CDR2 sequences of the antigen binding proteins to determine a H-CDR2 consensus sequence, by aligning the individual H-CDR3 sequences of the antigen binding proteins to determine a H-CDR3 consensus sequence, by aligning the individual L-CDR1 sequences of the antigen binding proteins to determine a L-CDR1 consensus sequence, by aligning the individual L-CDR2 sequences of the antigen binding proteins to determine a L-CDR2 consensus sequence, and by aligning the individual L-CDR3 sequences of the antigen binding proteins to determine a L-CDR3 consensus sequence. Similarities between sequences within each individual CDR sequences can be identified. Consensus sequences for the groups of similar sequences within each CDR can then be prepared.

Various emobodiments of Variable Heavy chain (VH) Consensus amino acid sequences of the present invention are set forth in Table 19A of FIG. 55 (CDRs are underlined, with the first being CDR1). Various embodiments of VH CDR Consensus amino acid sequences of the present invention are set forth in Tables 19B and 19C of FIG. 55. In some cases, an “X” is present in the amino acid sequences set forth in Tables 19A and 19B which signifies that more than one amino acid (or no amino acid) may be present at this location (see FIGS. 56 and 57 for details of the consensus protein alignment). In some cases a “-” is present in Table 19A (which is the result of the consensus alignment) and signifies that no amino acid is present at the location (see FIGS. 56 and 57 for details of the consensus protein alignment). The VH Consensus sequences and the VH CDR Consensus sequences are based on analysis of 8 or more aligned VH/VH CDR antibody sequences, as described above. In some cases, the VH/VH CDR Consensus sequence is based on analysis of 25 or more, 50 or more, 75 or more, or 100 or more aligned VH antibody sequences. In one case, the VH/VH CDR Consensus sequence is based on analysis of 149 aligned VH antibody sequences.

Various emobodiments of Variable Light chain (VL) Consensus amino acid sequences of the present invention are set forth in Table 20A of FIG. 55 (CDRs are underlined, with the first being CDR1). Various embodiments of VL CDR Consensus amino acid sequences of the present invention are set forth in Tables 20B and 20C of FIG. 55. As mentioned above, in some cases, an “X” is present in the amino acid sequences set forth in Tables 20A and 20B which signifies that more than one amino acid (or no amino acid) may be present at this location (see FIGS. 56 and 57 for details of the consensus protein alignment). In some cases a “-” is present in Table 20A (which is the result of the consensus alignment) and signifies that no amino acid is present at the location (see FIGS. 56 and 57 for details of the consensus protein alignment). The VL Consensus sequences and the VL CDR Consensus sequences are based on analysis of 8 or more aligned VL/VL CDR antibody sequences, as described above. In some cases, the VL/VL CDR Consensus sequence is based on analysis of 25 or more, 50 or more, 75 or more, or 100 or more, 125 or more, or 150 or more aligned VL antibody sequences. In one case, the VL/VL CDR Consensus sequence is based on analysis of 209 aligned VL antibody sequences.

As discussed above, the consensus sequences in certain embodiments can comprise substitutions, deletions, or additions/insertions at different positions in the sequence. Specific examples of these substitutions, deletions, or additions/insertions can be found in Tables 19C and 20C of FIG. 55, as well as Tables 21-48 of FIG. 56 and Tables 49-134 of FIG. 57, all of which are included herein. However, in no way should the amino acid substitutions, deletions, or additions/insertions exemplified in Tables 19A-C and 20A-C in FIG. 55 or in Tables 21-48 in FIG. 56 or in Tables 49-134 in FIG. 57 be construed to limit the invention to only those amino acid substitutions, deletions, or additions at any position in the identified consensus sequences (VH, VL and/or CDRs) with any amino acid is contemplated herein.

In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein at least one VH CDR is a VH1 CDR selected from Table 19B or Table 19C as depicted in FIG. 55. In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein at least one VH CDR is a VH2 CDR selected from Table 19B or Table 19C as depicted in FIG. 55. In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein at least one VH CDR is a VH3 CDR selected from Table 19B or Table 19C as depicted in FIG. 55. In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein the VH1 CDR, the VH2 CDR and the VH3 CDR is selected from Table 19B or Table 19C as depicted in FIG. 55.

In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein at least one VL CDR is a VL1 CDR selected from Table 20B or Table 20C as depicted in FIG. 55. In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein at least one VL CDR is a VL2 CDR selected from Table 20B or Table 20C as depicted in FIG. 55. In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein at least one VL CDR is a VL3 CDR selected from Table 20B or Table 20C as depicted in FIG. 55. In certain embodiments, the antigen binding proteins of the invention comprise 3 VH CDRs and 3 VL CDRs, wherein the VL1 CDR, the VL2 CDR and the VL3 CDR is selected from Table 20B or Table 20C as depicted in FIG. 55.

In some embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions of a VH. In some embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions of a VL. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VH1 CDR. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VH2 CDR. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VH3 CDR. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VL1 CDR. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VL2 CDR. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VL3 CDR.

In some embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions of a VH consensus sequence. In some embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions of a VL consensus sequence. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VH1 CDR Consensus sequence. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VH2 CDR Consensus sequence. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VH3 CDR Consensus sequence. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VL1 CDR Consensus sequence. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VL2 CDR Consensus sequence. In further embodiments, antigen binding proteins comprise no more than one, two, three, four, five, or six amino acid additions, deletions or substitutions within a VL3 CDR Consensus sequence.

In some embodiments, framework consensus sequences are encompassed by the present invention. Examples of these framework consensus sequences and additions, deletions or substitutions are shown in Tables 21-48 in FIG. 56 and Tables 49-134 in FIG. 57 herein.

In a further embodiment, the antigen binding proteins of the invention bind to ASGR of different species, including, but not limited to, human, cynomolgus, porcine, canine, murine and rat. In some embodiments, the antigen binding proteins of the invention bind to human. In some embodiments, the antigen binding proteins of the invention bind to cynomolgus ASGR. In some embodiments, the antigen binding proteins of the invention bind to porcine ASGR. In some embodiments, the antigen binding proteins of the invention bind to canine ASGR. In some embodiments, the antigen binding proteins of the invention bind to murine ASGR. In some embodiments, the antigen binding proteins of the invention bind to rat ASGR. In some embodiments, the antigen binding proteins specifically bind to ASGR of the different species.

In some embodiments, the antigen binding proteins of the invention bind to ASGR-1 of different species, including, but not limited to, human, cynomolgus, porcine, canine, murine and rat. In some embodiments, the antigen binding proteins of the invention bind to human ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to cynomolgus ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to porcine ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to canine ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to murine ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to rat ASGR-1. In some embodiments, the antigen binding proteins specifically bind to ASGR-1 of the different species.

In some embodiments, the antigen binding proteins of the invention binds to ASGR-2 of different species, including, but not limited to, human, cynomolgus, porcine, canine, murine and rat. In some embodiments, the antigen binding proteins of the invention bind to human ASGR-2. In some embodiments, the antigen binding proteins of the invention bind to cynomolgus ASGR-2. In some embodiments, the antigen binding proteins of the invention bind to porcine ASGR-2. In some embodiments, the antigen binding proteins of the invention bind to canine ASGR-2. In some embodiments, the antigen binding proteins of the invention bind to murine ASGR-2. In some embodiments, the antigen binding proteins of the invention bind to rat ASGR-2. In some embodiments, the antigen binding proteins specifically bind to ASGR-2 of the different species.

In some embodiments, the antigen binding proteins of the invention bind to ASGR, ASGR-1 and/or ASGR-2 from two or more different species, and/or bind ASGR, ASGR-1 and/or ASGR-2 from the same species. For example, but not limited to: an antibody that binds human and cynomolgus ASGR-1; an antibody that binds to human, cynomolgus and porcine ASGR-1; an antibody that binds to human, cynomolgus, rat and murine ASGR-2; an antibody that binds human ASGR-1 and human ASGR-2; an antibody that binds human and cynomolgus ASGR-1 and ASGR-2. In some embodiments, the antigen binding proteins specifically bind to ASGR, ASGR-1 and/or ASGR-2 from two or more different species and/or specifically bind ASGR, ASGR-1 and/or ASGR-2 from the same species.

As discussed herein, the ASGR receptor, and ASGR-1 and/or ASGR-2 separately, internalize into the cell upon ligand binding. Accordingly, in certain embodiments, the invention provides antigen binding proteins that inhibit or reduce internalization of ASGR, ASGR-1 and/or ASGR-2. In certain embodiments, the antigen binding proteins of the invention reduce ligand binding and also inhibit internalization of ASGR, ASGR-1 and/or ASGR-2. In some embodiments, the antigen binding proteins of the invention inhibit internalization without necessarily inhibiting ligand binding.

In some embodiments, the antigen binding proteins (e.g., antibodies) of the invention are pH and/or calcium insensitive molecules, as well as binding to ASGR, ASGR-1 and/or ASGR-2 and inhibiting the binding to a ligand. It is envisioned that these properties are desired to reduce or prevent the molecule from disassociating from the receptor during the endocytotic process in order to extend the half-life of the molecule. In some embodiments, the antigen binding proteins (e.g., antibodies) with pH-independent binding to its antigen such that the affinity for the antigen binding at physiological pH (i.e., pH 7.4) is similar to that at endosomal pH (i.e., pH 5.5-6.0). In some embodiments, the antigen binding proteins (e.g., antibodies) with calcium-independent binding to its antigen such that the affinity for the antigen binding at assay conditions (i.e., 1 mM calcium) is similar to that in the absence of exogenously added calcium. In some embodiments, the antigen binding proteins with both pH- and calcium-independent binding to its antigen such that the affinity for the antigen binding at physiologic pH and in the presence of calcium is similar to that at endosomal pH (i.e., pH 5.5-6.0) and in the absence of calcium. Any number of methods known to one skilled in the art can be used to measure pH and/or calcium insensitivity, such as the method described in Example 7C below.

ASGR-1, an asialoglycoprotein receptor, contains an N-term cytosolic domain, a transmembrane domain, a stalk region and a carbohydrate recognition domain (CRD) (alternatively known as the carbohydrate binding domain, or “CBD”). The carbohydrate recognition domain (“CRD”) structure of ASGR-1 is reported in literature (M. Meier et al, JMB (2000)300, 857-865). The structure of ASGR-1 at a higher resolution than reported, and also when bound to various ligands (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase) is provided herein (see Example 10 and FIGS. 18-21 herein). Given the importance of this domain to the function of ASGR-1, in some embodiments, it is desirable to target this domain with the antigen binding proteins of the present invention.

Accordingly, in some embodiments, the antigen binding proteins of the invention bind to the CBD of ASGR-1. In certain embodiments, the antigen binding proteins of the invention bind to the CBD of human ASGR-1. In certain embodiments, the antigen binding proteins of the invention bind to the CBD of SEQ ID NO:5. In some embodiments, the antigen binding proteins of the invention bind to amino acid residues selected from the group consisting of 148-291, 149-291, 150-291, 151-291, 152-291, 153-291, and 154-291 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within Helix α-1 or Helix α-2. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within residues 174-186 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within residues 194-206 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD at the same or overlapping binding site as where a ligand binds (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase or other sugars and glycoproteins capable of binding to ASGR, ASGR-1, and/or ASGR-2). In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within residues 237-273 or residues 240-267 of SEQ ID NO:5. In some embodiments, the antigen binding proteins of the invention bind to the CBD of cynomolgus ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to the CBD of porcine ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to the CBD of canine ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to the CBD of murine ASGR-1. In yet some embodiments, the antigen binding proteins of the invention bind to the CBD of rat ASGR-1. In yet some embodiments, the antigen binding proteins of the invention bind to the CBD of two or more different ASGR-1 species, for example, but not limited to, human ASGR-1 and cynomolgus ASGR-1, or human ASGR-1, cynomolgus ASGR-1 and canine ASGR-1, or human ASGR-1 and murine ASGR-1.

In further embodiments, the antigen binding proteins of the invention bind to ASGR-1 and inhibit binding of ligand to ASGR-1. In a specific embodiment, the ligands that are inhibited include, but are not limited to, sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase or other sugars and glycoproteins capable of binding to ASGR, ASGR-1, and/or ASGR-2.

The tyrosine at position 272 of murine ASGR-1 (position 273 of human ASGR-1 (SEQ ID NO:5)) appears to be important for protein stability, as it displays hydrogen bonding to D266 of murine ASGR-1 and several van der Waals contacts to other residues of murine ASGR-1 (N208, W210, H256, and R270). Additionally, by analogy with other lectins, Y272 of murine ASGR-1 may play a role in carbohydrate binding and function of ASGR-1. Accordingly, in some embodiments, the antigen binding proteins of the invention bind to or interact with Y273 of human ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to ASGR-1 at an epitope that comprises Y273 of human ASGR-1. In some embodiments, the antigen binding proteins of the invention bind to ASGR-1 at an epitope that results in Y273 of human ASGR-1 being unable to take part in binding ligand.

Analysis of the crystal structure of hASGR-1 revealed specific amino acids that are involved in the interaction between hASGR-1 and the ligands (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). Accordingly, in further embodiments, the antigen binding proteins of the invention bind to or interact with at least one of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least one of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least one of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase).

In further embodiments, the antigen binding proteins of the invention bind to or interact with at least one of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least one of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least one of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase).

In some embodiments, the antigen binding proteins of the invention bind to or interact with at least two of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least three of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least four of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least five of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least six of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least seven of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least eight of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least nine of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least ten of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least eleven of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least twelve of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least thirteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least fourteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least fifteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least sixteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least seventeen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least eighteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least nineteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least twenty of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264.

In some embodiments, the antigen binding proteins of the invention bind to or interact with at least two of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least three of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least four of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least five of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least six of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least seven of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least eight of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least nine of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least ten of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least eleven of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind to or interact with at least all of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273.

In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least two of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least three of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least four of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least five of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least six of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least seven of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least eight of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least nine of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least ten of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least eleven of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least twelve of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least thirteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least fourteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least fifteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least sixteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least seventeen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least eighteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least nineteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least twenty of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264.

In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least two of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least three of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least four of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least five of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least six of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least seven of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least eight of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least nine of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least ten of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising at least eleven of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273. In some embodiments, the antigen binding proteins of the invention bind at an epitope comprising all of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273.

In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least two of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least three of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least four of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g, sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least five of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g, sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least six of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g, sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least seven of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least eight of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g, sugars including but not limited to lactose, galactose, and/or GalNAc or glycoproteins displaying such sugars including but not limited to fetuin, orosomucoid and/or alkaline phosphatase). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least nine of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least ten of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least eleven of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least twelve of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least thirteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least fourteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least fifteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least sixteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least seventeen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least eighteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least nineteen of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least twenty of Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, F258, R263, or W264 with a ligand (e.g., lactose, galactose and/or GalNAc).

In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least two of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least three of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least four of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least five of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least six of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least seven of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least eight of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least nine of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least ten of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of at least eleven of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc). In further embodiments, the antigen binding proteins of the invention bind to hASGR-1 and block or reduce the binding or interaction of all of Q240, D242, W244, E253, N265, D266, D267, R237, P238, H257, T259, or Y273 with a ligand (e.g., lactose, galactose and/or GalNAc).

In order to relate unique antigen binding protein sequence features to specific functions or binding characteristics, sequences from antigen binding proteins of the invention from various characterization bins can be analyzed. For example, antigen binding proteins of the invention can be tested for their ability to bind a variety of binning probes (e.g., membrane preps from cells expressing ASGR-1 from different species or soluble huASGR-1). For each unique binding bin, the heavy and light chain sequences from each of the antigen binding proteins can be compared and claded based on, for example: 1. the unique VDJ and VJ rearrangements; 2. divergence from germline (ie. unique somatic hypermutation); and 3. relatedness to other antigen binding proteins of the same bin. Accordingly, in certain embodiments, the antigen binding proteins comprising the same or similar sequence features and patterns, will have substantially the same or similar binding characteristics. In specific embodiments, these antigen binding proteins can bind to the same or similar epitope with varying affinities.

The exemplary antigen binding proteins described herein have properties based on the epitope on ASGR, ASGR-1 and/or ASGR-2 that is bound by the antigen binding protein. The term “epitope” includes any determinant capable of being bound by an antigen binding protein, such as an antibody. An epitope is a region of an antigen that is bound by, or interacts with, an antigen binding protein that targets that antigen, and when the antigen is a protein, includes specific amino acids that directly contact, or interact with, the antigen binding protein. An epitope can be formed both by contiguous amino acids or non-contiguous amino acids juxtaposed by tertiary folding of a protein. A “linear epitope” is an epitope where an amino acid primary sequence comprises the recognized epitope. A linear epitope typically includes at least 3 or at least 4, and more usually, at least 5 or at least 6 or at least 7, for example, about 8 to about 10 amino acids in a unique sequence.

A “conformational epitope”, in contrast to a linear epitope, is a group of discontinuous amino acids (e.g., in a polypeptide, amino acid residues that are not contiguous in the polypeptide's primary sequence but that, in the context of the polypeptide's tertiary and quaternary structure, are near enough to each other to be bound by an antigen binding protein). Epitope determinants can include chemically active surface groupings of molecules such as amino acids, sugar side chains, phosphoryl or sulfonyl groups, and can have specific three dimensional structural characteristics, and/or specific charge characteristics. Generally, antigen binding proteins specific for a particular target molecule will preferentially recognize an epitope on the target molecule in a complex mixture of proteins and/or macromolecules.

Methods of characterizing the epitope bound by an antigen binding protein are well known in the art, including, but not limited to, binning (competition and/or cross-competition) (Miller et al “Epitope binning of murine monoclonal antibodies by a multiplexed pairing assay” J Immunol Methods (2011) 365, 118-25), peptide mapping (e.g., PEPSPOT™) (Albert et al “The B-cell Epitope of the Monoclonal Anti-Factor VIII Antibody ESH8 Characterized by Peptide Array Analysis” 2008 Thromb Haemost 99, 634-7), mutagenesis methods such as chimeras (Song et al “Epitope Mapping of Ibalizumab, a Humanized Anti-CD4 Monoclonal Antibody with Anti-HIV-1 Activity in Infected Patients” J. Virol. (2010) 84, 6935-6942), alanine scanning (Cunningham and Wells “High-resolution epitope mapping of HGH-receptor interactions by alanine-scanning mutagenesis” Science (1989) 244, 1081-1085), arginine scanning (Lim et al “A diversity of antibody epitopes can induce signaling through the erythropoietin receptor” Biochemistry (2010) 49, 3797-3804), HD exchange methods (Coates et al “Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry” Rapid Commun. Mass Spectrom. (2009) 23 639-647), NMR cross saturation methods (Morgan et al “Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-saturation” Biochemistry (2005) 44, 518-23), and crystallography (Gerhardt et al “Structure of IL-17A in complex with a potent, fully human neutralizing antibody” J. Mol. Biol (2009) 394, 905-21). The methods vary in the level of detail they provide as to the amino acids comprising the epitope.

Antigen binding proteins of the present invention include those that have an identical or overlapping epitope with an exemplary antigen binding protein described in Tables 2-7. In some embodiments, the antigen binding protein has an identical epitope as to the exemplary antigen binding proteins. In other embodiments, the antigen binding protein binds only a subset of the same amino acids as the exemplary antigen binding protein. In some embodiments, antigen binding proteins that might bind to any of the epitopes that are bound by the antibodies listed in Tables A, B, C or 6 are especially useful.

In certain embodiments, the antigen binding proteins of the present invention have an identical or overlapping epitope to the antigen binding proteins in Table 2-7 and comprise a) a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of the antigen binding proteins described in Tables 2-7; b) a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of the antigen binding proteins set forth in Tables 2-7; or c) the light chain variable domain of a) and the heavy chain variable domain of b).

In certain embodiments, the antigen binding protein of the present invention has an identical or overlapping epitope to the antigen binding proteins selected from the group consisting of 25A4, 4H6, 4A2, 5E5, 7E11, 54E9, 22G5, 194A4, 218G4, 176H4 and 194C10 wherein the antigen binding protein comprises a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 25A4 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 25A4; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 4H6 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 4H6; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 4A2 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 4A2; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 5E5 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 5E5; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 7E11 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 7E11; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 54E9 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 54E9; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 22G5 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 22G5; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 194A4 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 194A4; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 218G4G4 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 218G4; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 176H4 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 176H4; those comprising a light chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 194C10 and a heavy chain variable domain having at least 90% identity, at least 95% identity, or is identical to the amino acid sequence of 194C10.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibodies in Tables 2-7, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in Table 2; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in Table 2; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in Table 2; and a heavy chain variable domain comprising a) an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in Table 2; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in Table 2; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in Table 2.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibodies in Tables A, B, C or 6, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in Tables A, B, C or 6; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in Tables A, B, C or 6; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in Tables A, B, C or 6; and a heavy chain variable domain comprising a) an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in Tables A, B, C or 6; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in Tables A, B, C or 6; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in Tables A, B, C or 6.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 25A4, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:480; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:8492; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:16504; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:4488; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:12500; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:20512.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 4H6, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:894; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:8906; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:16918; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:4902; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:12914; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:20926.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 4A2, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:1130; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:9142; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:17154; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:5136; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:13148; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:21160.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 5E5, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:974; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:8986; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:16998; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:4982; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:12994; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:21006.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 7E11, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:872; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:8884; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:16896; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:4880; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:12892; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:20904.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 54E9, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:3448; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:11460; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:19472; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:7452; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:15464; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:23476.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 22G5, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:326; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:8338; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:16350; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:4334; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:12346; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:20358.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 194A4, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:2780; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:10792; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:18804; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:6786; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:14798; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:22810.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 218G4, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:3746; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:11758; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:19770; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:7750; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:15762; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:23774.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 176H4, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:2502; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:10514; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:18526; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:6508; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:14520; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:22532.

In certain embodiments, the ASGR-1 antigen binding protein of the invention has an identical or overlapping epitope as the antibody, 194C10, and comprises a light chain variable domain comprising an LCDR1 having no more than three amino acid additions, deletions, or substitutions from the LCDR1 sequence set forth in SEQ ID NO:2792; an LCDR2 having no more than three amino acid additions, deletions, or substitutions from the LCDR2 sequence set forth in SEQ ID NO:10804; and an LCDR3 having no more than three amino acid additions, deletions, or substitutions from the LCDR3 sequence set forth in SEQ ID NO:18816; and a heavy chain variable domain comprising an HCDR1 having no more than three amino acid additions, deletions, or substitutions from the HCDR1 sequence set forth in SEQ ID NO:6798; an HCDR2 having no more than three amino acid additions, deletions, or substitutions from the HCDR2 sequence set forth in SEQ ID NO:14810; and an HCDR3 having no more than three amino acid additions, deletions, or substitutions from the HCDR3 sequence set forth in SEQ ID NO:22822.

Antigen binding proteins that have an identical or overlapping epitope will often compete for binding to the antigen, ASGR, ASGR1 and/or ASGR2. Thus, in certain embodiments, an antigen binding protein (e.g., antibody or antibody fragment thereof) of the invention competes with the antigen binding proteins described in Tables 2-7. In some embodiments, an antigen binding protein (e.g., antibody or antibody fragment thereof) of the invention competes with the antigen binding proteins described in Tables A, B and C. In some embodiments, an antigen binding protein (e.g., antibody or antibody fragment thereof) of the invention competes with the antigen binding proteins described in Table 6. To “compete” or “competition” means the antigen binding proteins compete for the same epitope or binding site on a target. Such competition can be determined by an assay in which the reference antigen binding protein (e.g., antibody or antibody fragment thereof) prevents or inhibits specific binding of a test antigen binding protein. Numerous types of competitive binding assays can be used to determine if a test molecule competes with a reference molecule for binding. Examples of assays that can be employed include solid phase direct or indirect radioimmunoassay (RIA), solid phase direct or indirect enzyme immunoassay (EIA), sandwich competition assay (see, e.g., Stahli et al. (1983) Methods in Enzymology 9:242-253), solid phase direct biotin-avidin EIA (see, e.g., Kirkland et al., (1986) J. Immunol. 137:3614-3619), solid phase direct labeled assay, solid phase direct labeled sandwich assay, Luminex (Jia et al “A novel method of Multiplexed Competitive Antibody Binning for the characterization of monoclonal antibodies” J. Immunological Methods (2004) 288, 91-98) and surface plasmon resonance ((Song et al “Epitope Mapping of Ibalizumab, a Humanized Anti-CD4 Monoclonal Antibody with Anti-HIV-1 Activity in Infected Patients” J. Virol. (2010) 84, 6935-6942). An exemplary method of determining competition is described in Example 7D. Usually, when a competing antigen binding protein is present in excess, it will inhibit binding of a reference antigen binding protein to a common antigen by at least 50%, 55%, 60%, 65%, 70%, or 75%. In some instances, binding to ASGR-1 is inhibited by at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or more.

Besides competition, antigen binding proteins (e.g., antibodies or antibody fragments thereof) with identical, overlapping, or similar epitopes may be affected by mutagenesis of ASGR, ASGR-1 and/or ASGR-2 similarly. In brief, the domain(s)/region(s) containing residues that are in contact with or are buried by an antibody can be identified by mutating specific residues in ASGR, ASGR-1 and/or ASGR-2 (e.g., a wild-type antigen) and determining whether the antigen binding protein can bind the mutated or variant ASGR, ASGR-1 and/or ASGR-2 protein. By making a number of individual mutations, residues that play a direct role in binding or that are in sufficiently close proximity to the antibody such that a mutation can affect binding between the antigen binding protein and antigen can be identified. From the knowledge of these amino acids, the domain(s) or region(s) of the antigen that contain residues in contact with the antigen binding protein or covered by the antibody can be elucidated. Such a domain can include the binding epitope of an antigen binding protein. As mentioned above, one specific example of this general approach utilizes an arginine/glutamic acid scanning protocol (see, e.g., Nanevicz, T., et al., 1995, J. Biol. Chem., 270:37, 21619-21625 and Zupnick, A., et al., 2006, J. Biol. Chem., 281:29, 20464-20473). In general, arginine and glutamic acids are substituted (typically individually) for an amino acid in the wild-type polypeptide because these amino acids are charged and bulky and thus have the potential to disrupt binding between an antigen binding protein and an antigen in the region of the antigen where the mutation is introduced. Arginine residues that exist in the wild-type antigen are replaced with glutamic acid. A variety of such individual mutants are obtained and the collected binding results analyzed to determine what residues affect binding. In Example 7E, scanning arginine/glutamic acid mutagenesis was performed using the human ASGR-1 CBD domain and the effect on exemplary antibodies was determined. Included with the scope of the invention are ASGR, ASGR-1 and/or ASGR-2 antigen binding proteins having characteristics such that they are affected in a similar way as an exemplary antibody to mutagenesis.

Example 7E describes one such arginine/glutamic acid scanning of ASGR-1 for ASGR-1 antigen binding proteins provided herein. A series of mutant ASGR-1 antigens were created, with each mutant antigen having a single mutation. Binding of each mutant ASGR-1 antigen with various ASGR-1 antigen binding proteins was measured and compared to the ability of the selected antigen binding proteins to bind to human ASGR-1 (SEQ ID NO:5). In certain embodiments, binding of an antigen binding protein of the present invention to ASGR-1 is inhibited by a single mutation in ASGR-1, wherein the single mutation is selected from the group consisting of R170, S171, G172, R183, L184, W195, E196, K199, H203, H204, P207, V208, N209, H215, D216, P220, D225, D228, R237, P238, E239, P241, D242, D243, Y245, G246, H247, G248, L249, G251, E253, T259, D260, R263, N265, Q270, R271, P272, R274, and E280 as shown in SEQ ID NO:5. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 4A2 and their binding to ASGR-1 is inhibited a mutation of any of W195, E196, K199, H204, P207, and R263. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 4B3 and their binding to ASGR-1 is inhibited by a mutation of any of H203, H204, P220, and G251. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 5E5 and their binding to ASGR-1 is inhibited by a mutation of any of W195, K199, and R263. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 6G7 and their binding to ASGR-1 is inhibited by a mutation of any of R183, L184, H215, P220, P238, G246, H247, G248, G251, and N265. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 149D11 and their binding is inhibited by a mutation of any of R170, S171, and L184. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 175F4 and their binding is inhibited by a mutation of R183. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 17H6 and their binding is inhibited by a mutation of any of P241, D242, D243, Y245, G251, and E253. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 194A4 and their binding is inhibited by a mutation of D260. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 60C12 and their binding is inhibited by a mutation of any of R170, R237, E239, P241, T259, D260, R263, and N265. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 65D5 and their binding is inhibited by a mutation of any of R237, T259, D260 and R263. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 190F8 or 191G1and their binding is inhibited by a mutation of any of R170, S171, G172, E196, H204, P207, V208, N209, H215, D216, D225, D228, P238, D243, G248, L249, G251, D260, Q270, R271, P272, R274 and E280. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 199A7 and their binding is inhibited by a mutation of any of R170, R183, H215 and Q270. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 146B6 and their binding is inhibited by a mutation of any of P241, T259, and N265. In some embodiments, the ASGR-1 antigen binding proteins share the attributes of antibody 193E7 and their binding is inhibited by a mutation of any of P207 and R263. In some embodiments, any of two or more, three or more, four or more, five or more, six or more, seven or more, eight or more nine or more, ten or more, or all of the single mutations of the aforementioned groups individually inhibit binding of the ASGR-1 antigen binding protein to ASGR-1.

Binding of various anti-ASGR-1 antigen binding proteins (e.g., antibodies 5E5, 22G5, 7E11, 4A2, 4H6, 72G9, 194A4, 54E9, 218G4, 176H4 and 194C10) were further analyzed using X-ray crystallography. The results from the X-ray crystallography were highly correlated with the results from the Arginine/Glutamic acid mutagenesis profiling described above and in Example 7E. The interface between an antigen binding protein and the antigen can be determined/defined a number of ways. In Examples 10B-L, the interface was determined by selecting interface residues having at least one atom within a predefined distance to its partner protein. In some embodiments, ASGR-1 residues that are within the interface with antibody, 5E5, as determined by distance of 8 {acute over (Å)} or less are: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, or W264 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 5E5, as determined by distance of 5 {acute over (Å)} or less are: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, or R263 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 5E5, including those wherein any of: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, or W264 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 5E5, including those wherein any of: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, or P238 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 22G5, as determined by distance of 8 {acute over (Å)} or less are: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 22G5, as determined by distance of 5 {acute over (Å)} or less are: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, or W275 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 5E5, including those wherein any of: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 5E5, including those wherein any of: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, or W275 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 4A2, as determined by distance of 8 {acute over (Å)} or less are: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 4A2, as determined by distance of 5 {acute over (Å)} or less are: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, or R274 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 4A2, including those wherein any of: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 4A2, including those wherein any of: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 7E11, as determined by distance of 8 {acute over (Å)} or less are: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, or W264 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 7E11, as determined by distance of 5 {acute over (Å)} or less are: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, or R263 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 7E11, including those wherein any of: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, or W264 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 7E11, including those wherein any of are within the surface: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, or R263 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 4H6, as determined by distance of 8 {acute over (Å)} or less are: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 4H6, as determined by distance of 5 {acute over (Å)} or less are: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, or R263 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 4H6, including those wherein any of: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 4H6, including those wherein any of are within the surface: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, or R263 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 72G9, as determined by distance of 8 {acute over (Å)} or less are: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, or C269 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 72G9, as determined by distance of 5 {acute over (Å)} or less are: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, or Q270 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 72G9, including those wherein any of: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 72G9, including those wherein any of: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, or Q270 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 194A4, as determined by distance of 8 {acute over (Å)} or less are: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, or W264 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 194A4, as determined by distance of 5 {acute over (Å)} or less are: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, or G252 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 194A4, including those wherein any of: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, or W264 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 194A4, including those wherein any of are within the surface: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, or G252 (SEQ ID NO:5) within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 194C10, as determined by distance of 8 {acute over (Å)} or less are: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270 or W275 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 194C10, as determined by distance of 5 {acute over (Å)} or less are: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273 or R274 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 194C10, including those wherein any of: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 194C10, including those wherein any of: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 54E9, as determined by distance of 8 {acute over (Å)} or less are: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, or D266 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 54E9, as determined by distance of 5 {acute over (Å)} or less are: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, or Y273 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 54E9, including those wherein any of: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, or D266 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 54E9, including those wherein any of: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, or Y273 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 218G4, as determined by distance of 8 {acute over (Å)} or less are: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 218G4, as determined by distance of 5 {acute over (Å)} or less are: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 218G4, including those wherein any of: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, or W275 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 218G4, including those wherein any of: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273 or R274 (SEQ ID NO:5) are within the interface.

In some embodiments, ASGR-1 residues that are within the interface with antibody, 176H4, as determined by distance of 8 {acute over (Å)} or less are: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, ASGR-1 residues that are within the interface with antibody, 176H4, as determined by distance of 5 {acute over (Å)} or less are: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273 or R274 (SEQ ID NO:5). In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 176H4, including those wherein any of: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275 (SEQ ID NO:5) are within the interface. In certain embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 176H4, including those wherein any of: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274 (SEQ ID NO:5) are within the interface.

In some embodiments, the ASGR-1 residues that are involved in ligand binding are also in close proximity to the areas where antibodies 72G9, 54E9, 218G4 or 176H4 bind and can be useful for manipulating ASGR-1 binding to ligand. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 72G9 and the ligand (e.g., GalNAc), including those wherein any of Q240, D242, W244, E239, P241, D243, Y245, G246, G252, R237, E253, P238, H247, C255, or V268 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 72G9 and the ligand (e.g., GalNAc), including those wherein any of Q240, D242, or W244 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 72G9 and the ligand (e.g., GalNAc), including those wherein any of Q240, D242, W244, E239, P241, D243, Y245, G246 or G252 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 72G9 and the ligand (e.g., GalNAc), including those wherein any of Q240, D242, W244, R237 or E253 (SEQ ID NO:5) are within the interface. As noted in the examples below, the extent of inhibition resulting from 72G9 is lower than other direct blocking antibodies provided herein. While not intended to be limiting, this is understood to occur due to the nature of the relative orientations of the ASGR-1 protein and the antibody when bound to one another. For example, when the 72G9 antibody is bound to ASGR-1, there is still sufficient space for a ligand to reach the binding site, to some (althouth lesser) extent. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 54E9 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, D242, H257, T259, N265, D267, Y273, P238, E239, D260, R263, R271, E253, D266, D243, F258, or W264 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 54E9 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, D242, H257, T259, N265, D267, or Y273 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 54E9 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, D242, H257, T259, N265, D267, Y273, P238, E239, D260, R263, or R271 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 54E9 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, D242, H257, T259, N265, D267, Y273, E253 or D266 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 218G4 and the ligand (e.g., GalNAc), including those wherein any of N209, H257, N265, D267, Y273, D260, R271, R237, T259, D266, F258 or V268 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 218G4 and the ligand (e.g., GalNAc), including those wherein any of N209, H257, N265, D267, or Y273 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 218G4 and the ligand (e.g., GalNAc), including those wherein any of N209, H257, N265, D267, Y273, D260 or R271 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 218G4 and the ligand (e.g., GalNAc), including those wherein any of N209, H257, N265, D267, Y273. R237, T259 or D266 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 176H4 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, W244, E253, H257, T259, N265, D267, Y273, G246, H247, D260, R271, D266, P238, E239, Y245, F258, R263, W264, or V268 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 176H4 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, W244, E253, H257, T259, N265, D267, or Y273 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 176H4 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, W244, E253, H257, T259, N265, D267, Y273, G246, H247, D260, or R271 (SEQ ID NO:5) are within the interface. In some embodiments, the ASGR-1 antigen binding protein forms an interface with ASGR-1 that overlaps with that of antibody 176H4 and the ligand (e.g., GalNAc), including those wherein any of N209, R237, Q240, W244, E253, H257, T259, N265, D267, Y273, or D266 (SEQ ID NO:5) are within the interface.

As discussed above, the binding interaction between huASGR-1 and ligand (e.g., lactose, galactose, GalNAc), as well as the binding interaction between huASGR-1 and various embodiments of the antigen binding proteins (e.g., antibodies) of the present invention was evaluated using x-ray crystallography as described in Example 10. The binding interaction between huASGR-1 and various embodiments of the antigen binding proteins (e.g., antibodies) of the present invention was also evaluated using methodologies, including epitope binning as described in Example 7D, and arginine/glutamic acid mutational profiling as described in Example 7E. A summary of the data obtained through these methodologies is set forth in Table D below. This summary illustrates the various binding characteristics of representative antigen binding proteins (e.g., antibodies) of the present invention and their ability to directly and/or indirectly inhibit ligand binding to huASGR-1. In some embodiments, antibodies that interact with residues in common across different ligands can result in a similar form of inhibition (direct) across the various ligands. Examples of such residues are underlined and in bold in Table D.

TABLE D
Summary of Binding Characteristics of Representative Antigen Binding Proteins Derived
from Examples 7 and 10.
		Interaction Site	Interaction Site
Ligand/mAb	mAb Epitope	(crystal structure <5	(crystal structure 5-8
Name	(bin)	angstroms)	angstroms)	R/E scan
Ligand/	ND	Q240, D242, W244,	N209, R237, P238,	ND
Lactose		E253, N265, D266,	E239, P241, D243,
		D267	Y245, G246, H247,
			G252, C255, H257,
			T259, D260, V268,
			R271, Y273
Ligand/	ND	R237, D240, D242,	N209, P238, E239,	ND
Galactose		W244, E253, N265,	P241, D243, Y245,
		D266, D267	G246, H247, G252,
			C255, H257, T259,
			V268, R271, Y273
Ligand/	ND	N209, R237, D240,	P238, E239, P241,	ND
GalNAc		D242, W244, E253,	D243, Y245, G246,
		H257, T259, N265,	H247, G252, C255,
		D266, D267, Y273	F258, D260, R263,
			W264, V268, R271
5E5 -	A	H161, E162, W195,	V159, E160, R163,	W195, K199
Interaction is		E196, Q198, K199,	T193, S194, E197,
representative		F200, Q202, H203,	V201, I205, G206,
of indirect		H204, G232, F233,	P207, Y229, E230,
inhibition of		K234, N235, W236,	T231, E239, F258,
ligand		R237, P238, D261,	T259, D260, W264
binding		G262, R263
4A2 -	A	R170, W195, E196,	N157, V159, F168,	W195
Interaction is		K199, Q202, H203,	S169, S171, S194,
representative		H204, I205, G206,	Q198, F200, V201,
of indirect		P207, V208, F233,	T210, R237, E239,
inhibition of		K234, N235, W236,	Q240, F258, T259,
ligand		P238, D260, D261,	W264
binding		G262, R263, R274
7E11 -	A	H161, S194, W195,	E160, E162, V192,	W195
Interaction is		E196, Q198, K199,	T193, E197, V201,
representative		F200, Q202, H203,	H204, Y229, E230,
of indirect		F233, K234, N235,	T231, G232, E239,
inhibition of		W236, R237, P238,	Q240, P241, D261,
ligand		R263	G262, W264
binding
4H6 -	A	H161, E162, T193,	R163, V192, E197,	ND
Interaction is		S194, W195, E196,	Q198, H203, P207,
representative		K199, Q202, T231,	D228, E230, W236,
of indirect		G232, F233, K234,	R237, D260, G262,
inhibition of		N235, P238, D261,	W264
ligand		R263
binding
22G5 -	B	W167, S171, G172,	P155, N157, W158,	R183, L184,
Interaction is		K173, A174, A176,	F168, S169, R170,	H215, P220,
representative		D177, N180, Y181,	W175, A178, D179,	G246, G248,
of indirect		R183, L184, E185,	C182, A187, W211,	G251, N265
inhibition of		D186, Q270, P272,	C269, R271, Y273,
ligand		W275	R274, C277, T279
binding
194A4 -	C	T193, S194, W195,	H161, E162, V191,	D260
Interaction is		E196, P220, W221,	V192, E197, Q198,
representative		G226, T227, D228,	D216, G219, K222,
of indirect		Y229, E230, T231,	W223, D225, R263,
inhibition of		G232, F233, K234,	W264
ligand		N235, W236, R237,
binding		P238, E239, G252
72G9 -	C	D216, Q217, N218,	H215, K222, T231,	P241, D242,
Interaction is		G219, P220, W221,	G232, R237, P238,	D243, Y245,
representative		Y229, E230, K234,	H247, G248, E253,	G251, E253
of direct		W236, E239, Q240,	C255, D266, V268,
inhibition of		P241, D242, D243,	C269
ligand		W244, Y245, G246,
binding		L249, G250, G251,
		G252, D254, Q270
54E9 -	E	W195, N209, N235,	Q198, Q202, P207,	R237, E239,
Interaction is		R237, P238, E239,	V208, F233, W236,	P241, T259,
representative		Q240, D242, H257,	D243, E253, F258,	D260, R263,
of direct		T259, D260, D261,	G262, W264, D266	N265
inhibition of		R263, N265, D267,
ligand		R271, Y273
binding
218G4 -	L/O	R170, S171, G172,	W167, F168, S169,	R171, G172,
Interaction is		A174, H204, I205,	K173, W175, D177,	P238, R274
representative		G206, P207, V208,	Y181, Q202, H203,
of direct		N209, H257, D260,	T210, W211, R237,
inhibition of		N265, D267, Q270,	F258, T259, D261,
ligand		R271, P272, Y273,	D266, V268, C269,
binding		R274	W275
176H4 -	L/R	R170, S171, G172,	S169, W175, A176,	G172, P241,
Interaction is		K173, A174, D177,	A178, T210, W211,	D242, H247,
representative		P207, V208, N209,	W236, P238, E239,	L249, N265,
of direct		R237, Q240, W244,	D242, Y245, G250,	R271, P272
inhibition of		G246, H247, G248,	G251, F258, D261,
ligand		L249, E253, H257,	G262, R263, W264,
binding		T259, D260, N265,	D266, V268, C269,
		D267, Q270, R271,	W275
		P272, Y273, R274
194C10 -	L/T	N157, R170, S171,	V156, W158, V159,	R170, G172,
Interaction is		G172, Q202, H203,	H161, W167, F168,	V208, R274
representative		H204, I205, G206,	S169, K173, K199,
of direct		P207, V208, N209,	F200, V201, W211,
and/or indirect		T210, D260, R271,	R237, H257, F258,
inhibition of		P272, Y273, R274	T259, D261, D267,
ligand binding			V268, Q270, W275

In some embodiments, the antibody can directly inhibit ASGR-1 CBD/Ligand binding. While described herein in greater detail, and while not intended to be limiting by theory, such an interaction can denote that the antibody interacts with the section of ASGR-1 CBD that binds to its ligand directly, such that a paratope or other section of an antigen binding protein (e.g., antibody) directly obstructs the ligand's access to the binding site in ASGR1 CBD. An antigen binding protein or antibody can be designated as a direct inhibitor when it has one or more of the characteristics of the direct inhibitors provided herein, including the examples below (such as example 10, or the crystal structures referenced therein). Some examples of direct inhibition are shown by 72G9, 54E9, 218G4 and 176H4 and are indicated in Table D. In some embodiments, a direct inhibitor can bind to one or more of residues 237-273 or residues 240-267 of SEQ ID NO:5 of ASGR-1.

In some embodiments, the antigen binding protein or antibody can indirectly inhibit ASGR-1 CBD/Ligand binding. While described herein in greater detail, and while not intended to be limiting by theory, this denotes that the antigen binding protein or antibody binds to ASGR-1 CBD, but need not directly obstruct the ligand's access to the binding site in ASGR-1 CBD. An antigen binding protein or antibody can be designated as an indirect inhibitor when it has one or more of the characteristics of the indirect inhibitors provided herein, including the examples below (such as example 10 or the crystal structures provided therein). Some examples of indirect inhibition are shown by 5E5, 4A2, 7E11, 4H6, 22G5, 194A4, and are indicated in Table D. While not limiting, it is noted that indirect inhibition can occur from a variety of interactions or rearrangements. For example, indirect inhibition may occur from a conformational rearrangement of the carbohydrate binding loop occurs which could impair the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). In some embodiments, an indirect inhibitor can bind to one or more of the residues in ASGR-1 CBD helix alpha 1 and/or helix alpha 2. In some embodiments, the antibody binds to ASGR-1 and results in the disordering of the CBD.

In some embodiments, an antigen binding protein or antibody can have characteristics of both direct and indirect inhibition and/or bind to areas on ASGR-1 CBD that are common to both types of inhibition. Of course, such an embodiment may have sufficient inhibition capability through its direct, indirect, or both direct and indirect interactions.

In some embodiments, the distinction between direct and indirect inhibition need not be made. In some embodiments, denoting that an antigen binding protein or antibody provides direct or indirect inhibition means that it provides at least that form of inhibition (e.g., ASGR-1 CBD/Ligand blocking). In some embodiments, an antigen binding protein or antibody that provides direct inhibition, may also provide indirect aspects as well (such as other conformational changes). In addition, as shown in Table D, as the interation between ASGR-1 CBD and its ligands can vary for each of the noted three ligands, what may be a direct or indirect interaction for one ligand, need not be direct or indirect for another. While the antibodies provided herein that have the properties of direct and/or indirect inhibition will function accordingly, and the guidance provided herein allows for one to screen for and produce additional such antibodies, the fact that an antibody simply binds to ASGR-1 CBD does not necessarily mean that it will bind at the relevant locations on ASGR-1 to allow for direct or indirect inhibition.

In some embodiments, an isolated antigen binding protein that binds to human ASGR and inhibits ASGR function is provided. In one embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR and inhibits ASGR binding to ligand. In another embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 and inhibits ASGR-1 binding to ligand and/or ASGR-1 interaction with ASGR-2. In another embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR-2 and inhibits ASGR-2 binding to ligand and/or ASGR-2 interaction with ASGR-1. In yet another embodiment, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 and human ASGR-2, and inhibits ASGR-1 and/or ASGR-2 binding to ligand. In some embodiments, the isolated binding protein binds specifically to human ASGR, ASGR-1 and/or ASGR-2.

In some embodiments, an isolated antigen binding protein is provided, wherein the isolated antigen binding protein binds to human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7. In some embodiments, the invention comprises an isolated antigen binding protein, wherein the isolated antigen binding protein binds to human ASGR-1 and comprises one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises one VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and one VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises two VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and two VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Tables 3-7, and the VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in Tables 3-7. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE A, and the VL CDR1, VL CDR2 and VL CDR3, having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in TABLE A. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE B. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE B. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE B, and the VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE B. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in TABLE B. In still some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE C. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE C. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in TABLE C, and the VL CDR1, VL CDR2 and VL CDR3, having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in TABLE C. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in TABLE C. In further embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Table 6. In some embodiments, the isolated antigen binding protein comprises the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Table 6. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VH of any of the sequences set forth in Table 6, and the VL CDR1, VL CDR2 and VL CDR3, having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions, deletions or insertions in each CDR relative to the VL of any of the sequences set forth in Table 6. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and VL CDR3 having an amino acid sequence identical to any of the sequences set forth in Table 6.

In some embodiments, an isolated antigen binding protein is provided, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 3-7. In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Tables 3-7. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 3-7, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Tables 3-7. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Tables 3-7, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Tables 3-7. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table A, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table A, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table B, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table B, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table C, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table C, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table 6. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 6. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table 6, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 6. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Table 6, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table 6.

In some embodiments, an isolated antigen binding protein is provided, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising no more than 18 amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55. In some aspects, the invention comprises an isolated antigen binding protein, wherein the isolated antigen binding protein binds to human ASGR-1 and comprises one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising no more than 14 amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising no more than 18amino acid residue substitutions, inserions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising no more than 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one or more VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and one or more VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises one VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical no more than 18 amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table19A, as depicted in FIG. 55, and one VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising no more than 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A, as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises one VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and one VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises two VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising up to 18 amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and two VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising up to 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A, as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises two VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and two VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55. In some embodiments, the isolated antigen binding protein comprises the VH CDR1, VH CDR2 and VH CDR3 having an amino acid sequence identical to or comprising up to 18amino acid residue substitutions, insertions or deletions in each CDR relative to the VH of any of the sequences set forth in Table 19A, as depicted in FIG. 55, and the VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising up to 14amino acid residue substitutions, insertions or deletions in each CDR relative to the VL of any of the sequences set forth in Table 20A, as depicted in FIG. 55. In some embodiments, the invention provides an isolated antigen binding protein, wherein the antigen binding protein binds human ASGR-1 and comprises the VH CDR1, VH CDR2 or VH CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 19B or 19C, as depicted in FIG. 55, and the VL CDR1, VL CDR2 or VL CDR3 having an amino acid sequence identical to or comprising a conservative subsitutuion of any of the amino acid sequences set forth in Tables 20B or 20C, as depicted in FIG. 55.

In some embodiments, an isolated antigen binding protein is provided, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 19A, as depicted in FIG. 55 or in Tables 21-34 as depicted in FIG. 56 or in Tables 49-95 as depicted in FIG. 56. In some aspects, the invention provides an isolated antigen binding protein, wherein the antigen binding protein specifically binds human ASGR-1 and comprises a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 20A, as depicted in FIG. 55, or in Tables 35-48, as depicted in FIG. 56 or in Tables 96-134 as depicted in FIG. 57. In some embodiments, the antigen binding protein comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Tables 19A as depicted in FIG. 55, or in Tables 21-34 as depicted in FIG. 56 or in Tables 49-95 as depicted in FIG. 57, and a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 20A as depicted in FIG. 55 or in Tables 35-48 as depicted in FIG. 56 or in Tables 96-134 as depicted in FIG. 57. In some embodiments, the antigen binding protein comprises a heavy chain variable domain having any of the VH domain amino acid sequences set forth in Tables 19A as depicted in FIG. 55, or in Tables 21-34 as depicted in FIG. 56 or in Tables 49-95 as depicted in FIG. 57, and a light chain variable domain having any of the VL domain amino acid sequences set forth in Table 20A as depicted in FIG. 55 or in Tables 35-48 as depicted in FIG. 56 or in Tables 96-134 as depicted in FIG. 57.

In some embodiments, an antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by any of the antigen binding proteins disclosed herein is provided. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Tables 2-7. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table B. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table C. In some embodiments, the invention provides an isolated antigen binding protein that specifically binds to human ASGR-1 at an epitope that is bound by at least one of the antigen binding proteins set forth in Table 6.

In some embodiments, the invention provides an isolated antigen binding protein that competes for binding to human ASGR-1 with any of the antigen binding proteins disclosed herein. In some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Tables 2-7. In some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table A. In some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table B. In still some embodiments, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table C. In yet another embodiment, the invention provides an isolated antigen binding protein that competes for binding with any of the antigen binding proteins set forth in Table 6.

In some embodiments, an isolated antigen binding protein that binds to human ASGR-1 within the carbohydrate recognition domain (“CRD”) (also known as the carbohydrate binding domain or “CBD”) and inhibits human ASGR-1 binding to ligand is provided. In some embodiments, the antigen binding protein binds to human ASGR-1 within residues 148-291, or 149-291, or 150-291, or 151-291, or 152-291, or 153-291, or 154-291, or 155-291 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within Helix α-1. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 within residues 174-186 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within Helix α-2. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 CBD within residues 194-206 of SEQ ID NO:5. In some embodiments, the invention comprises an isolated antigen binding protein that binds to human ASGR-1 within residues 237-273 or residues 240-267 of SEQ ID NO:5. In some embodiments, the antigen binding protein binds to ASGR-1 having an amino acid sequence that is at least 90% identical to SEQ ID NO:5. In some embodiments, the antigen binding protein is an antibody.

In some embodiments, an isolated antigen binding protein or an antibody that binds to human ASGR-1 and inhibits human ASGR-1 function is provided. In some embodiments, the isolated antigen binding protein or an antibody binds to human ASGR-1 and inhibits human ASGR-1 from binding to a ligand. In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, : H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, or R263 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR1 at an epitope comprising at least one of the following amino acid residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, or R263 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, or R263 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, : H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, or W264 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, or G252 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, or C269 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, or Q270 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, or D266 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, or Y273 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments, the antigen binding protein or antibody or a paratope in an antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5).

In some embodiments, an isolated antigen binding protein or an antibody or a paratope in an antibody that specifically binds to human ASGR-1 and inhibits human ASGR-1 function is provided. In some embodiments, the isolated antigen binding protein or an antibody or a paratope in an antibody specifically binds to human ASGR-1 and inhibits human ASGR-1 from binding to a ligand. In some embodiments, the antigen binding protein or antibody or a paratope in an antibody specifically binds to human ASGR-1 within residues 148-291 of SEQ ID NO:5. In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5).

In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273, R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, D267, R237, Q240, D242, W244, E253, N265, D266, D267, N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: Q240, D242, W244, E253, N265, D266, or D267 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R237, Q240, D242, W244, E253, N265, D266, D267, N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R237, Q240, D242, W244, E253, N265, D266, or D267 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, or R271 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, or C269 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, or Q270 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, or D266 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, or Y273 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues of human ASGR-1 (SEQ ID NO:5): D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274, R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263, V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues of human ASGR-1 (SEQ ID NO:5): H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, or R263 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275, P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, or T279 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274, N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, or R274 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263, E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, or R263 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263, R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, or R263 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252, : H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, or W264 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, or G252 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 8 angstroms or less from at least one of the following residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274, V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270 or W275 (SEQ ID NO:5). In some embodiments when the antigen binding protein or antibody or a paratope in an antibody is bound to human ASGR-1, the antigen binding protein or antibody or a paratope in an antibody is positioned 5 angstroms or less from at least one of the following residues: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273 or R274 (SEQ ID NO:5).

In some embodiments, an isolated antigen binding protein or antibody that specifically binds to human ASGR-1 and inhibits human ASGR-1 function is provided. In some embodiments, the isolated antigen binding protein or antibody that specifically binds to human ASGR-1 inhibits binding of human ASGR-1 binding to a ligand. In some embodiments, the antigen binding protein or antibody specifically binds to human ASGR-1 at a location that overlaps with a location where a ligand binds to human ASGR-1. In some embodiments, the location where a ligand binds to ASGR-1 includes at least one amino acid residue selected from the group consisting of: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273, P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, or R271 (SEQ ID NO:5). In some embodiments, an isolated antigen binding protein or an antibody specifically binds to human ASGR-1 at a location that overlaps with a location that a ligand binds to ASGR-1. In some embodiments, the location that a ligand binds to human ASGR-1 includes at least one amino acid residue selected from the group consisting of: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, and Y273 (SEQ ID NO:5).

In some embodiments, an isolated antigen binding protein that binds to human ASGR-1 and inhibits human ASGR, ASGR-1 and/or ASGR-2 function is provided, wherein the antigen binding protein does not bind to a variant ASGR-1 protein, and wherein said variant ASGR-1 protein comprises a single mutation of a residue selected the group consisting of: R170, S171, G172, R183, L184, W195, E196, K199, H203, H204, P207, V208, N209, H215, D216, P220, D225, D228, R237, P238, E239, P241, D242, D243, Y245, G246, H247, G248, L249, G251, E253, T259, D260, R263, N265, Q270, R271, P272, R274, and E280 as shown in SEQ ID NO:5. In some embodiments, an isolated antigen binding protein or an antibody is contemplated. An antigen binding protein “does not bind” to a variant ASGR-1 protein when the measured reduction in antibody binding signal to a variant ASGR-1 protein (compared to that determined for binding to wild type ASGR-1) is statistically significant as measured by any number of methods known to one skilled in the art, such as the method described in Example 7E below. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting of: W195, E196, K199, H203, H204, P207, P220, G251, and R263 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of H203, H204, P220, and G251. In some embodiments, the single mutation is selected from the group consisting of W195, E196 and K199. In some embodiments, the single mutation is selected from the group consisting of W195, E196 and H204. In some embodiments, the single mutation is selected from the group consisting W195, K199, and R263. In some embodiments, the single mutation is selected from the group consisting of W195 and E196. In some embodiments, the single mutation is selected from the group consisting of W195 and K199. In some embodiments, the single mutation is selected from the group consisting of W195 or P207. In some embodiments, the single mutation is selected from the group consisting of W195 and R263. In some embodiments, the single mutation is selected from the group consisting of H203 and H204. In some embodiments, the single mutation is selected from the group consisting of K199 and R263. In some embodiments, the single mutation is a mutation of residue W195. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue selected the group consisting of: R170, S171, R183, L184, H215, P220, P238, G246, H247, G248, G251, and N265 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R183, L184, H215, P220, G246, G248, G251, and N265. In some embodiments, the single mutation is selected from the group consisting of L184, P220, P238, H247, and G251. In some embodiments, the single mutation is selected from the group consisting of R170, S171, and L184. In some embodiments, the single mutation is a mutation of residue R183. In some embodiments, the single mutation is a mutation of residue L184. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting of: P241, D242, D243, Y245, G251, E253 and D260 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of P241, D243, Y245, G251, E253 and D260. In some embodiments, the single mutation is selected from the group consisting of P241, D243, and E253. In some embodiments, the single mutation is a mutation of residue D260. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, R237, E239, P241, T259, D260, R263, and N265 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R237, D260 and R263. In some embodiments, the single mutation is selected from the group consisting of R237, T259, D260 and R263. In some embodiments, the single mutation is selected from the group consisting of R170, R237, P241, T259, D260, R263 and N265. In some embodiments, the single mutation is selected from the group consisting of R237, E239, P241, T259, D260, R263 and N265. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, S171, G172, E196, H204, P207, V208, N209, H215, D216, D225, D228, P238, P241, D242, D243, H247, G248, L249, G251, D260, R263, N265, Q270, R271, P272, R274 and E280 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R170, S171, G172, E196, H204, P207, V208, N209, H215, D216, D225, D228, P238, P241, D242, D243, H247, G248, L249, G251, D260, R263, N265, Q270, R271, P272, R274 and E280 as shown in SEQ ID NO:5. In some embodiments, the single mutation is selected from the group consisting of R170, S171, G172, E196, H204, P207, H215, D216, D225, D228, D243, G248, L249, G251, D260, Q270, R271, P272, R274 and E280. In some embodiments, the single mutation is selected from the group consisting of G172, V208, R271, P272 and R274. In some embodiments, the single mutation is selected from the group consisting of G172, R271 and R274. In some embodiments, the single mutation is selected from the group consisting of G172, N209, and R271. In some embodiments, the single mutation is selected from the group consisting of R170, G172, V208, R271 and P272. In some embodiments, the single mutation is selected from the group consisting of G172, V208, P238, R271, P272 and R274. In some embodiments, the single mutation is selected from the group consisting of G172, P238, R271, P272 and R274. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: G172, P238, R271 and R274 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, G172, V208 and R274 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: R170, R183, H215 and Q270 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: P241, T259, and N265 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: P207 and R263 as shown in SEQ ID NO:5. In some embodiments, the variant ASGR-1 protein comprises a single mutation of a residue at a position selected from the group consisting or comprising: G172, P241, D242, H247, L249, N265, R271 and P272 as shown in SEQ ID NO:5. In some embodiments, the antigen binding protein or antibody does not bind to two or more variant ASGR-1 proteins, wherein the variant ASGR-1 proteins comprise the single mutations of the group individually.

A “CDR grafted antibody” is an antibody comprising one or more CDRs derived from an antibody of a particular species or isotype and the framework of another antibody of the same or different species or isotype.

A “multi-specific antibody” is an antibody that recognizes more than one epitope on one or more antigens. A subclass of this type of antibody is a “bi-specific antibody” which recognizes two distinct epitopes on the same or different antigens.

An antigen binding protein including an antibody “specifically binds” to an antigen, such as ASGR, ASGR-1 or ASGR-2, if it binds to the antigen with a tight binding affinity as determined by a equilibrium dissociation constant (K_D, or corresponding K_D, as defined below) value of 10⁻⁷ M or less. An antigen binding protein that specifically binds to human ASGR, ASGR-1 or ASGR-2 may be able to bind to ASGR, ASGR-1 or ASGR-2 from other species as well with the same or different affinities.

Affinity can be determined using a variety of techniques known in the art, for example but not limited to, equilibrium methods (e.g., enzyme-linked immunoabsorbent assay (ELISA); KinExA, Rathanaswami et al. Analytical Biochemistry, Vol. 373:52-60, 2008; or radioimmunoassay (RIA)), or by a surface plasmon resonance assay or other mechanism of kinetics-based assay (e.g., BIACORE® analysis or Octet® analysis (forteBIO)), and other methods such as indirect binding assays, competitive binding assays fluorescence resonance energy transfer (FRET), gel electrophoresis and chromatography (e.g., gel filtration). These and other methods may utilize a label on one or more of the components being examined and/or employ a variety of detection methods including but not limited to chromogenic, fluorescent, luminescent, or isotopic labels. A detailed description of binding affinities and kinetics can be found in Paul, W. E., ed., Fundamental Immunology, 4th Ed., Lippincott-Raven, Philadelphia (1999), which focuses on antibody-immunogen interactions. One example of a competitive binding assay is a radioimmunoas say comprising the incubation of labeled antigen with the antibody of interest in the presence of increasing amounts of unlabeled antigen, and the detection of the antibody bound to the labeled antigen. The affinity of the antibody of interest for a particular antigen and the binding off-rates can be determined from the data by scatchard plot analysis. Competition with a second antibody can also be determined using radioimmunoassays. In this case, the antigen is incubated with antibody of interest conjugated to a labeled compound in the presence of increasing amounts of an unlabeled second antibody.

Further embodiments of the invention provide antigen binding molecules (e.g., antibodies) that specifically bind ASGR, ASGR-1 and/or ASGR-2 with an equilibrium dissociation constant or K_D (k_off/k_on) of less than 10⁻⁷ M, or of less than 10⁻⁸ M, or of less than 10⁻⁹ M, or of less than 10⁻¹⁰ M, or of less than 10⁻¹¹ M, or of less than 10⁻¹² M, or of less than 10⁻¹³ M, or of less than 5×10⁻¹³ M (lower values indicating tighter binding affinity). Yet further embodiments of the invention are antigen binding molecules that specifically bind ASGR, ASGR-1 and/or ASGR-2 with an equilibrium dissociation constant or K_D (k_off/k_on) of less than about 10⁻⁷ M, or of less than about 10⁻⁸ M, or of less than about 10⁻⁹ M, or of less than about 10⁻¹⁰ M, or of less than about 10⁻¹¹ M, or of less than about 10⁻¹² M, or of less than about 10⁻¹³ M, or of less than about 5×10⁻¹³ M.

In still another embodiment, an antigen binding protein of the invention (e.g., an antibody) that specifically bind ASGR, ASGR-1 and/or ASGR-2 has an equilibrium dissociation constant or K_D (k_off/k_on) of between about 10⁻⁷ M and about 10⁻⁸ M, between about 10⁻⁸ M and about 10⁻⁹ M, between about 10⁻⁹ M and about 10⁻¹⁰ M, between about 10⁻¹⁰ M and about 10⁻¹¹ M, between about 10⁻¹¹ M and about 10⁻¹² M, between about 10⁻¹² M and about 10⁻¹³ M. In still another embodiment, an antibody of the invention that specifically bind ASGR, ASGR-1 and/or ASGR-2 has an equilibrium dissociation constant or K_D (k_off/k_on) of between 10⁻⁷ M and 10⁻⁸ M, between 10⁻⁸ M and 10⁻⁹ M, between 10⁻⁹ M and 10⁻¹⁰ M, between 10⁻¹⁰ M and 10⁻¹¹ M, between 10⁻¹¹ M and 10⁻¹² M, between 10⁻¹² M and 10⁻¹³ M.

It will be appreciated that an antigen binding protein of the present invention (e.g., an antibody or fragments thereof) may have at least one amino acid substitution, providing that the antigen binding protein retains the same or better desired binding specificity (e.g., binding to human ASGR, human ASGR-1, and/or human ASGR-2)(See Example 14). Therefore, modifications to the antigen binding protein structures are encompassed within the scope of the invention. In one embodiment, the antigen binding protein (e.g., but not limited to, an antibody) comprises sequences that each independently differ by 5, 4, 3, 2, 1, or 0 single amino acid additions, substitutions, and/or deletions from a CDR sequence of those set forth in Table 2 herein. As used herein, a CDR sequence that differs by no more than a total of, for example, four amino acid additions, substitutions and/or deletions from a CDR sequence shown in Table 2 below refers to a sequence with 4, 3, 2, 1 or 0 single amino acid additions, substitutions, and/or deletions compared with the sequences shown in Table 2. These may include amino acid substitutions, which may be conservative or non-conservative that do not destroy the desired binding capability of an antibody. Conservative amino acid substitutions may encompass non-naturally occurring amino acid residues, which are typically incorporated by chemical peptide synthesis rather than by synthesis in biological systems. These include peptidomimetics and other reversed or inverted forms of amino acid moieties. A conservative amino acid substitution may also involve a substitution of a native amino acid residue with a normative residue such that there is little or no effect on the polarity or charge of the amino acid residue at that position. In some embodiments, the one or more substitutions to one or more of the antibody sequences can be as follows for each noted section in the noted antibody: 1) VH1∥-08/D6|6-19|RF1/JH4, 25A4 H CDR2 sequence—WMYPN---SGNTGYAQKFQG, where N at 11 can be S or Q and T at 12 can be A or V, such that the sequence can be Trp Met Tyr Pro Asn Ser Gly X1 X2 Gly Tyr Ala Gln Lys Phe Gln Gly (SEQ ID NO: 50259) wherein X1=N or S or Q or a conservative substitution thereof, X2=T or A or V or a conservative substitution thereof. 2) VH111-08/D6|6-19|RF1/JH4, 4A2 H CDR2 sequence—WMHPN---SGNTGYAQKFQG, where N at 11 can be S or Q, and T at 12 can be A or E, such that the sequence can be Trp Met His Pro Asn Ser Gly X1 X2 Gly Tyr Ala Gln Lys Phe Gln Gly (SEQ ID NO: 50260) wherein X1=N or S or Q or a conservative substitution thereof, X2=T or A or E or a conservative substitution thereof. 3) VK4|B3/JK3, 4A2 L CDR3 sequence—QQYYN-----------------------TPVT, where N at 5 can be Q, and T at 29 can be A, such that the sequence can be Gln Gln Tyr Tyr X1 X2 Pro Val Thr (SEQ ID NO: 50261) wherein X1=N or Q or a conservative substitution thereof, X2=T or A or a conservative substitution thereof. 4) VH1∥-02/D1|1-1|RF1/JH4, 4H6 H CDR3 sequence—DGTS----------------------SFDY, where D at 1 can be S, G at 2 can be A, such that the sequence can be X1 X2 Thr Ser Ser Phe Asp Tyr (SEQ ID NO: 50262) wherein X1=D or S or a conservative substitution thereof, X2=or A or a conservative substitution thereof. 5) VH3|3-33/D4|4-11|RF2/JH6 and VH3|3-07/D4|4-11|RF2/JH6, 7E11 H CDR2 sequence—IIWHD---GSNKYYADSVKG, where D at 5 can be S or E, G at 9 can be A, D at 16 can be E, and S at 17 can be A, such that the sequence can be Ile Ile Trp His X1 X2 Ser Asn Lys Tyr Tyr Ala X3 X4 Val Lys Gly (SEQ ID NO: 50263) wherein X1=D or S or E or a conservative substitution thereof, X2=G or A or a conservative substitution thereof, X3=D or E or a conservative substitution thereof, X4=S or A or a conservative substitution thereof. 6) VH3|3-33/D6|6-6|RF1/JH6 and VH3|3-07/D6|6-6|RF1/JH6, 5E5 H CDR2 sequence VIWYD---GSNKYYADSVKG, where G at 9 can be A, D at 16 can be E or G, and S at 17 can be A, such that the sequence can be Val Be Trp Tyr Asp X1 Ser Asn Lys Tyr Tyr Ala X2 X3 Val Lys Gly (SEQ ID NO: 50264) wherein X1=G or A or a conservative substitution thereof X2=D or E or G or a conservative substitution thereof X3=S or A or a conservative substitution thereof. 7) VH3|3-33/D6|6-6|RF1/JH6 and VH3|3-07/D6|6-6|RF1/JH6, 5E5 H CDR3 sequence EVYSSGW----------------YDYGMDV, where W at 7 can be F, such that the sequence can be Glu Val Tyr Ser Ser Gly X1 Tyr Asp Tyr Gly Met Asp Val (SEQ ID NO: 50265) wherein X1=W or F or a conservative substitution thereof.

In some embodiments, any one or more of the above CDR sequences can be combined with any one or more of the CDR sequences provided herein (e.g., Table 2 in FIG. 49, and Tables 19A-C and Tables 20A-C in FIG. 55). In some embodiments, any one or more of the above CDR sequences can be combined with any one or more CDR sequences provided herein for the designated antibody to provide an antibody of 6 CDRs (LCDR1, LCDR2, LCDR3, HCDR1, HCDR2, and HCDR3). For example, any one or more of the above CDRs can be used as one of the CDRs for the antibodies provided in Table 2 in FIG. 49 and/or Tables 19A, 19B, 19C, 20A, 20B and/or 20C in FIG. 55. In some embodiments, the variant positions provided in the above consensus sequences can be further combined as optional variations with the variations of sequence provided in Table 2 in FIG. 49, and Tables 19A-C and Tables 20A-C in FIG. 55, such that any demonstrated combination of sequences in one consensus sequence (e.g., for an antibody, such as 4A2 H CDR2 above) can be combined with all permissible options outlined for the relevant antibody in Table 2 in FIG. 49, and Tables 19A-C and Tables 20A-C in FIG. 55 (e.g., the corresponding 4A2 H CDR2), which can further be combined with any of the other 4A2 sequences in Table 2 in FIG. 49, and Tables 19A-C and Tables 20A-C in FIG. 55 (e.g., HCDR1, HCDR3, LCDR1, LCDR2, and LCDR3). Of course, 4A2 L CDR3 noted above can similarly be combined, and/or combined with the immediate combination as well. Thus, such sequences are not disclosed herein as needing to be alternative sequences, but are contemplated as additional options for the noted sequences. In some embodiments, variants of such sequences are also contemplated. Such variants can retain or have superior desired activity. Examples of such aspects are provided in Example 14 and tables 6 and 7. In some embodiments, any one or more of the FR regions in tables 6 and 7 can be combined with any one or more of the CDR sequences provided herein. In some embodiments, any one or more of the FR regions provided in Table 6 or 7 can be combined with the corresponding CDR set for the corresponding antibody (as a set of 6 CDRs). Thus, variants of antibody 4A2 are provided that include 6 CDRs (HCDR1, HCDR2, HCDR3, LCDR1, LCDR2, and LCDR3) and 8 FRs HFR1, HFR2, HFR3, HFR4, LFR1, LFR2, LFR3, and LFR4), any particular sequence of which can be from any of the designated sequences for antibody 4A2 provided herein (the present paragraph, Tables 2, 6 and/or 7, tables 19A, 19B, and 19C, 20A, 20B and 20C, etc).

Non-conservative substitutions may involve the exchange of a member of one class of amino acids or amino acid mimetics for a member from another class with different physical properties (e.g. size, polarity, hydrophobicity, charge). In certain embodiments, such substituted residues may be introduced into regions of a human antibody that are homologous with non-human antibodies, or into the non-homologous regions of the molecule.

Moreover, one skilled in the art may generate test variants containing a single amino acid substitution at each desired amino acid residue. The variants can then be screened using activity assays known to those skilled in the art. Such variants could be used to gather information about suitable variants. For example, if one discovered that a change to a particular amino acid residue resulted in destroyed, undesirably reduced, or unsuitable activity, variants with such a change may be avoided. In other words, based on information gathered from such routine experiments, one skilled in the art can readily determine the amino acids where further substitutions should be avoided either alone or in combination with other mutations.

A skilled artisan will be able to determine suitable variants of the antigen binding protein as set forth herein using well-known techniques. In certain embodiments, one skilled in the art may identify suitable areas of the molecule that may be changed without destroying activity by targeting regions not believed to be important for activity. In certain embodiments, one can identify residues and portions of the molecules that are conserved among similar polypeptides as has been describe above. In certain embodiments, even areas that may be important for biological activity or for structure may be subject to conservative amino acid substitutions without destroying the biological activity or without adversely affecting the polypeptide structure.

Additionally, one skilled in the art can review structure-function studies identifying residues in similar polypeptides that are important for activity or structure. In view of such a comparison, one can predict the importance of amino acid residues in a protein that correspond to amino acid residues which are important for activity or structure in similar proteins. One skilled in the art may opt for chemically similar amino acid substitutions for such predicted important amino acid residues.

In some embodiments, one skilled in the art may identify residues that may be changed that result in enhanced properties as desired. For example, an amino acid substitution (conservative or non-conservative) may result in enhanced binding affinity to human ASGR, human ASGR-1, and/or human ASGR-2, or enhanced binding affinity to other species of ASGR, ASGR-1, and/or ASGR-2.

One skilled in the art can also analyze the three-dimensional structure and amino acid sequence in relation to that structure in similar polypeptides. In view of such information, one skilled in the art may predict the alignment of amino acid residues of an antibody with respect to its three dimensional structure. In certain embodiments, one skilled in the art may choose not to make radical changes to amino acid residues predicted to be on the surface of the protein, since such residues may be involved in important interactions with other molecules. A number of scientific publications have been devoted to the prediction of secondary structure. See Moult J., Curr. Op. in Biotech., 7(4):422-427 (1996), Chou et al., Biochemistry, 13(2):222-245 (1974); Chou et al., Biochemistry, 113(2):211-222 (1974); Chou et al., Adv. Enzymol. Relat. Areas Mol. Biol., 47:45-148 (1978); Chou et al., Ann. Rev. Biochem., 47:251-276 and Chou et al., Biophys. J., 26:367-384 (1979). Moreover, computer programs are currently available to assist with predicting secondary structure. One method of predicting secondary structure is based upon homology modeling. For example, two polypeptides or proteins which have a sequence identity of greater than 30%, or similarity greater than 40% often have similar structural topologies. The growth of the protein structural database (PDB) has provided enhanced predictability of secondary structure, including the potential number of folds within a polypeptide's or protein's structure. See Holm et al., Nucl. Acid. Res., 27(1):244-247 (1999). Additional methods of predicting secondary structure include “threading” (Jones, D., Curr. Opin. Struct. Biol., 7(3):377-87 (1997); Sippl et al., Structure, 4(1):15-19 (1996)), “profile analysis” (Bowie et al., Science, 253:164-170 (1991); Gribskov et al., Meth. Enzym., 183:146-159 (1990); Gribskov et al., Proc. Nat. Acad. Sci., 84(13):4355-4358 (1987)), and “evolutionary linkage” (See Holm, supra (1999), and Brenner, supra (1997)).

In certain embodiments, variants of the antigen binding protein include glycosylation variants wherein the number and/or type of glycosylation site has been altered compared to the amino acid sequences of a parent polypeptide. In certain embodiments, variants comprise a greater or a lesser number of N-linked glycosylation sites than the native protein. Alternatively, substitutions which eliminate this sequence will remove an existing N-linked carbohydrate chain. Also provided is a rearrangement of N-linked carbohydrate chains wherein one or more N-linked glycosylation sites (typically those that are naturally occurring) are eliminated and one or more new N-linked sites are created. Additional antibody variants include cysteine variants wherein one or more cysteine residues are deleted from or substituted for another amino acid (e.g., serine) as compared to the parent amino acid sequence. Cysteine variants may be useful when antibodies must be refolded into a biologically active conformation such as after the isolation of insoluble inclusion bodies. Cysteine variants generally have fewer cysteine residues than the native protein, and typically have an even number to minimize interactions resulting from unpaired cysteines.

Desired amino acid substitutions (whether conservative or non-conservative) can be determined by those skilled in the art at the time such substitutions are desired. In certain embodiments, amino acid substitutions can be used to identify important residues of antibodies to the target of interest, or to increase or decrease the affinity of the antibodies to the target of interest described herein.

According to certain embodiments, desired amino acid substitutions are those which: (1) reduce susceptibility to proteolysis, (2) reduce susceptibility to oxidation, (3) alter binding affinity for forming protein complexes, (4) alter binding affinities, and/or (4) confer or modify other physiochemical or functional properties on such polypeptides. According to certain embodiments, single or multiple amino acid substitutions (in certain embodiments, conservative amino acid substitutions) may be made in the naturally-occurring sequence (in certain embodiments, in the portion of the polypeptide outside the domain(s) forming intermolecular contacts). In certain embodiments, a conservative amino acid substitution typically may not substantially change the structural characteristics of the parent sequence (e.g., a replacement amino acid should not tend to break a helix that occurs in the parent sequence, or disrupt other types of secondary structure that characterizes the parent sequence). Examples of art-recognized polypeptide secondary and tertiary structures are described in Proteins, Structures and Molecular Principles (Creighton, Ed., W. H. Freeman and Company, New York (1984)); Introduction to Protein Structure (C. Branden and J. Tooze, eds., Garland Publishing, New York, N.Y. (1991)); and Thornton et al. Nature 354:105 (1991), which are each incorporated herein by reference.

Antigen Binding Protein Sequences

The amino acid sequences of the light chain CDRs of exemplary antigen binding proteins (antibodies) and the heavy chain CDRs of exemplary antigen binding proteins (antibodies) are shown in Tables 2-7, in addition to the exemplary antigen binding proteins described above as consensus light chain CDRs and/or consensus heavy chain CDRs (see Tables 19 B and C and Tables 20 B and C in FIG. 55). Also shown are polynucleotide sequences which encode the amino acid sequences of the CDRs (Table 2). Tables 3-7 and Tables A, B and C further provide the amino acid sequences of the VH and VL of exemplary antigen binding proteins (e.g., antibodies), in addition to the exemplary antigen binding proteins described above as consensus variable light chain sequences and/or consensus variable heavy chain sequences (see Table 19A and Table 20A in FIG. 55, as well as the Tables in FIGS. 56 and 57). Table 3 further provides the polynucleotide (DNA) sequences encoding the amino acid sequences of the variable light and variable heavy domains for exemplary antibodies.

Particular embodiments of antigen binding proteins of the present invention comprise one or more amino acid sequences that are identical to the amino acid sequences of one or more of the CDRs and/or FRs (framework regions) illustrated herein in Tables 2-7, and Tables A-C below. In one embodiment, the antigen binding protein comprises a light chain CDR1 sequence illustrated herein in Table 2 in FIG. 49 and Table C below. In another embodiment, the antigen binding protein comprises a light chain CDR2 sequence illustrated herein in Table 2 in FIG. 49 and Table C below. In another embodiment, the antigen binding protein comprises a light chain CDR3 sequence illustrated in herein in Table 2 in FIG. 49 and Table C below. In another embodiment, the antigen binding protein comprises a heavy chain CDR1 sequence illustrated in herein in Table 2 in FIG. 49 and Table C below. In another embodiment, the antigen binding protein comprises a heavy chain CDR2 sequence illustrated herein in Table 2 in FIG. 49 and Table C below. In another embodiment, the antigen binding protein comprises a heavy chain CDR3 sequence illustrated herein in Table 2 in FIG. 49 and Table C below. In another embodiment, the antigen binding protein comprises a light chain FR1 sequence illustrated herein in Tables 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a light chain FR2 sequence illustrated herein in Tables 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a light chain FR3 sequence illustrated herein in Tables 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a light chain FR4 sequence illustrated herein in Table 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a heavy chain FR1 sequence illustrated herein in Table 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a heavy chain FR2 sequence illustrated herein in Table 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a heavy chain FR3 sequence illustrated herein in Table 3-7 in FIGS. 50-54, respectively. In another embodiment, the antigen binding protein comprises a heavy chain FR4 sequence illustrated herein in Table 3-7 in FIGS. 50-54, respectively.

In another embodiment, at least one of the antigen binding protein's CDR3 sequences differs by no more than 6, 5, 4, 3, 2, 1 or 0 single amino acid addition, substitution, and/or deletion from a CDR3 sequence from the sequences as shown in Table 2 in FIG. 49 or Table C below. In another embodiment, the antigen binding protein's light chain CDR3 sequence differs by no more than 6, 5, 4, 3, 2, 1 or 0 single amino acid addition, substitution, and/or deletion from a light chain CDR3 sequence from the sequences as shown in Table 2 in FIG. 49 or Table C below and the antigen binding protein's heavy chain CDR3 sequence differs by no more than 6, 5, 4, 3, 2, 1 or 0 single amino acid addition, substitution, and/or deletion from a heavy chain CDR3 sequence from the sequences as shown in Table 2 in FIG. 49 or Table C below. In another embodiment, the antigen binding protein further comprises 1, 2, 3, 4, or 5 CDR sequences that each independently differs by 6, 5, 4, 3, 2, 1, or 0 single amino acid additions, substitutions, and/or deletions from a CDR sequence of the sequences shown in Table 2 in FIG. 49 or Table C below. In another embodiment, the antigen binding protein comprises the CDRs of the light chain variable region and the CDRs of the heavy chain variable region set forth in Table 2 in FIG. 49 or Table C below. In a further embodiment, the antigen binding protein comprises the CDRs of any one of the antibodies in Table 2 in FIG. 49 or Table C below. In one embodiment, the antigen binding protein is a human antibody. In another embodiment, the antigen binding protein is a humanized antibody. In certain embodiments, the VH CDRs and the VL CDRs are paired in a manner indicated in Tables 2-7 in FIGS. 49-54, respectively.

In one embodiment, the antigen binding protein (e.g., an antibody) comprises a light chain variable domain comprising a sequence of amino acids that differs from the sequence of a light chain variable domain listed in Table 3-7 in FIGS. 50-54, respectively at 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, 1 or 0 residues, wherein each such sequence difference is independently either a deletion, insertion, or substitution of one amino acid residue. In another embodiment, the antigen binding protein (e.g., an antibody) comprises a heavy chain variable domain comprising a sequence of amino acids that differs from the sequence of a heavy chain variable domain listed in Table 3-7 in FIGS. 50-54, respectively at 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, 1 or 0 residues, wherein each such sequence difference is independently either a deletion, insertion, or substitution of one amino acid residue. In certain embodiments, the antigen binding protein comprises a light chain variable domain and a heavy chain variable domain that are paired in a manner indicated in Tables 3-7 in FIGS. 50-54, respectively. In certain embodiments, the antigen binding protein comprises a light chain variable domain and a heavy chain variable domain that are paired in a manner indicated in Tables A-C below.

In a particular embodiment, the antigen binding protein (e.g., antibody) binds to human ASGR-1 and comprises a heavy chain variable domain containing one or more VH CDR1 (HCDR1), VH CDR2 (HCDR2) and/or VH CDR3 (HCDR3), wherein the VH CDR1 (HCDR1) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:5136, SEQ ID NO:50001, SEQ ID NO:50012 and SEQ ID NO:50468; the VH CDR2 (HCDR2) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:13148, SEQ ID NO:50002, SEQ ID NO:50014, and SEQ ID NO:50260; and the VH CDR3 (HCDR3) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:21160, SEQ ID NO:50003, and SEQ ID NO:50470.

In a particular embodiment, the antigen binding protein (e.g., antibody) binds to human ASGR-1 and comprises a light chain variable domain containing one or more VL CDR1 (LCDR1), VL CDR2 (LCDR2) and/or VL CDR3 (LCDR3), wherein the VL CDR1 (LCDR1) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:1130, SEQ ID NO:50133, SEQ ID NO:50156 and SEQ ID NO:50162; the VL CDR2 (LCDR2) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:9142, SEQ ID NO:50157, SEQ ID NO:50163, SEQ ID NO:50229, SEQ ID NO:50619, SEQ ID NO:50643 and SEQ ID NO:50649; and the VL CDR3 (LCDR3) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:17154, SEQ ID NO:50134, SEQ ID NO:50164, and SEQ ID NO:50261.

In a particular embodiment, the antigen binding protein (e.g., antibody) binds to human ASGR-1 and comprises A) a heavy chain variable domain containing one or more VH CDR1 (HCDR1), VH CDR2 (HCDR2) and/or VH CDR3 (HCDR3), wherein the VH CDR1 (HCDR1) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:5136, SEQ ID NO:50001, SEQ ID NO:50012 and SEQ ID NO:50468; the VH CDR2 (HCDR2) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:13148, SEQ ID NO:50002, SEQ ID NO:50014, and SEQ ID NO:50260; and the VH CDR3 (HCDR3) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:21160, SEQ ID NO:50003, and SEQ ID NO:50470; and B) a light chain variable domain containing one or more VL CDR1 (LCDR1), VL CDR2 (LCDR2) and/or VL CDR3 (LCDR3), wherein the VL CDR1 (LCDR1) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:1130, SEQ ID NO:50133, SEQ ID NO:50156 and SEQ ID NO:50162; the VL CDR2 (LCDR2) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:9142, SEQ ID NO:50157, SEQ ID NO:50163, SEQ ID NO:50229, SEQ ID NO:50619, SEQ ID NO:50643 and SEQ ID NO:50649; and the VL CDR3 (LCDR3) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:17154, SEQ ID NO:50134, SEQ ID NO:50164, and SEQ ID NO:50261. In one embodiment, the antigen binding protein (e.g., antibody) comprises A) a heavy chain variable domain containing a VH CDR1 (HCDR1), a VH CDR2 (HCDR2) and a VH CDR3 (HCDR3), wherein the VH CDR1 (HCDR1) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:5136, SEQ ID NO:50001, SEQ ID NO:50012 and SEQ ID NO:50468; the VH CDR2 (HCDR2) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:13148, SEQ ID NO:50002, SEQ ID NO:50014, and SEQ ID NO:50260; and the VH CDR3 (HCDR3) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:21160, SEQ ID NO:50003, and SEQ ID NO:50470; and B) a light chain variable domain containing a VL CDR1 (LCDR1), a VL CDR2 (LCDR2) and a VL CDR3 (LCDR3), wherein the VL CDR1 (LCDR1) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:1130, SEQ ID NO:50133, SEQ ID NO:50156 and SEQ ID NO:50162; the VL CDR2 (LCDR2) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:9142, SEQ ID NO:50157, SEQ ID NO:50163, SEQ ID NO:50229, SEQ ID NO:50619, SEQ ID NO:50643 and SEQ ID NO:50649; and the VL CDR3 (LCDR3) has an amino acid sequence identical to, or comprising not more than 3 amino acid additions/insertions, deletions or substitutions as compared to, the amino acid sequences selected from the group consisting of SEQ ID NO:17154, SEQ ID NO:50134, SEQ ID NO:50164, and SEQ ID NO:50261. In one embodiment, the antigen binding protein comprises A) a heavy chain variable domain containing a VH CDR1 (HCDR1), a VH CDR2 (HCDR2) and a VH CDR3 (HCDR3), wherein the VH CDR1 (HCDR1) amino acid sequence is selected from the group consisting of SEQ ID NO:5136, SEQ ID NO:50001, SEQ ID NO:50012 and SEQ ID NO:50468; the VH CDR2 (HCDR2) amino acid sequence is selected from the group consisting of SEQ ID NO:13148, SEQ ID NO:50002, SEQ ID NO:50014, and SEQ ID NO:50260; and the VH CDR3 (HCDR3) amino acid sequence is selected from the group consisting of SEQ ID NO:21160, SEQ ID NO:50003, and SEQ ID NO:50470; and B) a light chain variable domain containing a VL CDR1 (LCDR1), a VL CDR2 (LCDR2) and a VL CDR3 (LCDR3), wherein the VL CDR1 (LCDR1) amino acid sequence is selected from the group consisting of SEQ ID NO:1130, SEQ ID NO:50133, SEQ ID NO:50156 and SEQ ID NO:50162; the VL CDR2 (LCDR2) amino acid sequence is selected from the group consisting of SEQ ID NO:9142, SEQ ID NO:50157, SEQ ID NO:50163, SEQ ID NO:50229, SEQ ID NO:50619, SEQ ID NO:50643 and SEQ ID NO:50649; and the VL CDR3 (LCDR3) amino acid sequence is selected from the group consisting of SEQ ID NO:17154, SEQ ID NO:50134, SEQ ID NO:50164, and SEQ ID NO:50261. In one embodiment, the antigen binding protein comprises a heavy chain variable domain and a light chain variable domain containing a VH CDR1 having the amino acid sequence set forth in SEQ ID NO:5136; a VH CDR2 having the amino acid sequence set forth in SEQ ID NO:13148; a VH CDR3 having the amino acid sequence set forth in SEQ ID NO:21160; a VL CDR1 having the amino acid sequence set forth in SEQ ID NO:1130; a VL CDR2 having the amino acid sequence set forth in SEQ ID NO:9142; and a VL CDR3 having the amino acid sequence set forth in SEQ ID NO:17154.

In a particular embodiment, the antigen binding protein (e.g., antibody) comprises a) a light chain variable domain having no more than ten or no more than five amino acid additions/insertions, deletions or substitutions from the amino acid sequence set forth in SEQ ID NO:25164 or SEQ ID NO:50326; b) a heavy chain variable domain having no more than ten or no more than five amino acid additions/insertions, deletions or substitutions from the amino acid sequence set forth in SEQ ID NO:29170 or SEQ ID NO:50266; or c) the light chain variable domain of a) and the heavy chain variable domain of b). In one embodiment, the antigen binding protein comprises a light chain varable domain having the amino acid sequence set forth in SEQ ID NO:25164 or SEQ ID NO:50326; and a heavy chain variable domain having the amino acid sequence set forth in SEQ ID NO:29170 or SEQ ID NO:50266. In one embodiment, the antigen binding protein comprises a light chain varable domain having the amino acid sequence set forth in SEQ ID NO:50326; and a heavy chain variable domain having the amino acid sequence set forth in SEQ ID NO:50266. In one embodiment, the antigen binding protein comprises a light chain varable domain having the amino acid sequence set forth in SEQ ID NO:25164; and a heavy chain variable domain having the amino acid sequence set forth in SEQ ID NO:29170.

While specific embodiments relating to the antigen binding protein identified as 4A2 are set forth above with particularity, the embodiments of the present invention are not intended to be limited in scope to this individual embodiment. The embodiments directed to 4A2 are intended merely as single illustrations of individual embodiments. It is fully anticipated that the embodiments of the present invention include antigen binding proteins comprising heavy chain variable domains containing one or more VH CDR1 (HCDR1), VH CDR2 (HCDR2) and/or VH CDR3 (HCDR3) and/or light chain variable domains containing one or more VL CDR1 (LCDR1), VL CDR2 (LCDR2) and/or VL CDR3 (LCDR3) as set forth in Tables 2-7 in FIGS. 49-57, respectively, as well as Tables 19A-C and Tables 20A-C in FIG. 55, Tables 21-134 in FIGS. 56 and 57, and Tables A, B and C.

TABLE A
Exemplary Heavy and Light Chain Variable Regions
Ab	SEQ ID NOs:		SEQ ID NOs:	Ab	SEQ ID NOs:	Ab	SEQ ID NOs:
name	VH/VL	Ab name	VH/VL	name	VH/VL	name	VH/VL
10G6	29184/25178	59F2	31512/27506	147E9	30172/26166	191G10	30846/26840
11E2	29040/25034	5E5	29016/25010	184E7	30660/26654	191G12	30730/26724
11F5	29054/25048	60D2	31518/27512	194A4	30820/26814	192C10	30764/26758
12E9	29186/25180	60E8	29494/25488	208A2	28136/24130	192C8	30756/26750
12F11	29178/25172	63A10	31536/27530	210G10	31054/27048	192E4	30744/26738
12F12	29188/25182	63G7	31534/27528	4B1	28878/24872	192G6	30752/26746
13F6	28772/24766	64B12	29624/25618	60E12	29502/25496	192G8	30760/26754
148E10	28132/24126	65F10	28134/24128	61A1	29504/25498	192H10	30768/26762
154F4	31392/27386	68G6	28224/24218	62H10	31832/27826	193C7	30794/26788
159H8	31416/27410	6A6	28806/24800	63H8	29604/25598	194B7	30828/26822
160B12	31418/27412	6D4	28816/24810	72G9	32080/28074	194C1	30816/26810
175D10	30538/26532	6D9	29154/25148	8D8	29168/25162	196C7	30870/26864
177D2	31858/27852	6G6	29198/25192	12D2	29036/25030	197B6	30894/26888
25A4	28522/24516	70D1	29670/25664	148H10	30196/26190	197E11	30906/26900
25D12	28510/24504	7A10	29194/25188	173C11	30520/26514	197F2	30886/26880
26C4	28580/24574	7E11	28914/24908	179C2	30570/26564	197G3	30888/26882
27E7	28744/24738	7F4	28814/24808	47C1	29286/25280	198G3	30620/26614
28H2	29190/25184	7F8	28948/24942	49C1	29320/25314	213B3	31092/27086
29E2	29192/25186	7G4	28966/24960	60C12	29500/25494	219H1	31156/27150
29E6	28550/24544	8D12	29050/25044	60G2	29482/25476	74C8	29768/25762
29H8	28798/24792	9F12LC1	28216/24210	65D5	29632/25626	74G6	29894/25888
32D6	29196/25190	9F12LC2	28217/24211	66H11	28130/24124	75G3	29714/25708
3G7	28840/24834	9G9	28790/24784	71A6	28128/24122	89A11	30028/26022
45B4	29252/25246	65E9	31538/27532	73G1	31556/27550	74B2	29736/25730
49F10	29334/25328	72B4	31552/27546	49C5	32086/28080	74H7	29966/25960
4A2	29170/25164	7H7	28944/24938	49D10	32088/28082	85F7	29766/25760
4B3	28750/24744	9C11	28856/24850	51E3	30958/26952	198B9	30918/26912
4H6	28936/24930	12B12	28978/24972	51F4	31476/27470	199A7	30932/26926
50D4	29362/25356	147D10	30174/26168	53E8	32090/28084	218G4	31786/27780
50G9	32082/28076	149D11	30226/26220	54E9	31488/27482	146A8	31332/27326
51E9	29366/25360	149F8	30222/26216	56E3	31492/27486	146B6	31334/27328
52G11	28138/24132	151B9	31372/27366	56G1	31490/27484	149A1	31344/27338
52H1	31482/27476	175F4	31456/27450	190C11	30602/26596	172B12	31452/27446
53F2	28140/24134	22G5	28368/24362	190E6	30642/26636	172C3	31450/27444
53F7	29412/25406	48B12	31820/27814	190F12	30618/26612	193E7	30796/26790
55B1	29430/25424	52H2	29380/25374	190F8	30712/26706	199E3	30926/26920
56E5	29466/25460	6G7	28880/24874	190G11	30608/26602	226F9	31264/27258
65C12	32078/28072	7G2	28942/24936	190H9	30716/26710	227C1	31280/27274
	Ab	SEQ ID NOs:		SEQ ID NOs:	Ab	SEQ ID NOs:
	name	VH/VL	Ab name	VH/VL	name	VH/VL
	176H4	30542/26536	72F5	29700/25694	48D7	29306/25300
	194C10	30832/26826	191A10	30724/26718	52D10	29388/25382
	191E10	30726/26720	191G1	30628/26622	59E6	29590/25584
	196F4	30868/26862	227F2	31282/27276	64E2	31836/27830
	198D2	31604/27598	31D12LC1	29176/25170	57A7	29554/25548
	202A3	30972/26966	31D12LC2	29174/25168	58G11	31510/27504
	204G6	31004/26998	7C3LC1	28212/24206	64G12	29626/25620
	224G1	31196/27190	7C3LC2	28214/24208

TABLE B
	SEQ ID		SEQ ID		SEQ ID		SEQ ID
Ab	NOs:	Ab	NOs:	Ab	NOs:	Ab	NOs:
name	VH/VL	name	VH/VL	name	VH/VL	name	VH/VL
175D10	30538/26532	184E7	30660/26654	192E4	30744/26738	74B2	29736/25730
25A4	28522/24516	194A4	30820/26814	192G6	30752/26746	74H7	29966/25960
26C4	28580/24574	208A2	28136/24130	192G8	30760/26754	85F7	29766/25760
29H8	28798/24792	210G10	31054/27048	192H10	30768/26762	218G4	31786/27780
49F10	29334/25328	4B1	28878/24872	193C7	30794/26788	172B12	31452/27446
4A2	29170/25164	72G9	32080/28074	194B7	30828/26822	172C3	31450/27444
4H6	28936/24930	190C11	30602/26596	194C1	30816/26810	193E7	30796/26790
50D4	29362/25356	190E6	30642/26636	196C7	30870/26864	199E3	30926/26920
51E9	29366/25360	190F12	30618/26612	197B6	30894/26888	191E10	30726/26720
52H1	31482/27476	190F8	30712/26706	197E11	30906/26900	196F4	30868/26862
55B1	29430/25424	190G11	30608/26602	197F2	30886/26880	198D2	31604/27598
56E5	29466/25460	190H9	30716/26710	197G3	30888/26882	202A3	30972/26966
64B12	29624/25618	191A10	30724/26718	198G3	30620/26614	204G6	31004/26998
6G6	29198/25192	191G1	30628/26622	213B3	31092/27086	10G6	29184/25178
7F4	28814/24808	191G10	30846/26840	219H1	31156/27150	160B12	31418/27412
7G4	28966/24960	191G12	30730/26724	74C8	29768/25762	177D2	31858/27852
149F8	30222/26216	192C10	30764/26758	74G6	29894/25888	53F7	29412/25406
48B12	31820/27814	192C8	30756/26750	75G3	29714/25708	63A10	31536/24530
7E11	28914/24908	198B9	30918/26912	146B6	31334/27328	22G5	28368/24362
6G7	28880/24874	199A7	30932/26926	176H4	30542/26536	5E5	29016/25010
147E9	30172/26166	146A8	31332/27326	149A1	31344/27338	194C10	30832/26826
54E9	31488/27482	12D2	29036/25030

TABLE C
Exemplary Heavy and Light Chain Variable Regions and Heavy and
Light Chain CDR1/2/3
	VH	VL	HCDR1	HCDR2	HCDR3	LCDR1	LCDR2	LCDR3
Ab	SEQ ID	SEQ ID	SEQ ID	SEQ ID	SEQ ID	SEQ ID	SEQ ID	SEQ ID
name	NOs:	NOs:	NOs:	NOs:	NOs:	NOs:	NOs:	NOs:
25A4	28522	24516	4488,	12500,	20512,	480,	8492,	16504,
	or	or	50468,	50002,	50003 or	50133 or	50157,	50134,
	50266	50316	50001 or	50014 or	50470	50162	50229,	50164
			50013	50259			50619,	or
							50643 or	50620
							50649
26C4	28580	24574	4546,	12588 or	20570,	538,	8550,	16562,
	or	or	50001,	50002	50003 or	50133 or	50157,	50134,
	50266	50316	50013 or		50470	50156	50163,	50164
			50468				50229,	or
							50619,	50620
							50643 or
							50649
29H8	28798	24792	4764,	12776 or	20788 or	756 or	8768,	16780
	or	or	50001,	50002	50003 or	50133	50157,	or
	50266	50316	50013 or		50470		50163	50134
			50468				50229,
							50619,
							50643 or
							50649
4A2	29170	25164	5136,	13148,	21160,	1130,	9142,	17154,
	or	or	50001,	50002,	50003 or	50133,	50157,	50134,
	50266	50326	50013,	50014 or	50470	50156 or	50163	50164
			or 50468	50260		50162	50229,	or
							50619,	50261
							50643 or
							50649
4H6	28936	24930	4902 or	12914 or	20926 or	894,	8096,	16918
	or	or	50019	50020	50021 or	50147 or	50148 or	or
	50272	50321			50262	50159	50160	50149
56E5	29466	25460	5432,	13444 or	21456 or	1426 or	9438,	17450
	or	or	50019 or	50020	50021	50147	50123,	or
	50272	50321	50058				50131,	50149
							50136,
							50139,
							50142,
							50145,
							50148,
							50154,
							50160,
							50181,
							50184,
							50199,
							50202,
							50213 or
							50248
7F4	28814	24808	4780,	12792 or	20804 or	772,	8784,	16796
	or	or	50046 or	50047	50048	50122,	50123,	or
	50284	50312	50075			50130,	50131,	50124
						50135 or	50136,
						50198	50139,
							50142,
							50145,
							50148,
							50154,
							50160,
							50181,
							50199 or
							50213
7G4	28966	24960	4932,	12944,	20956 or	924,	8936,	16948
	or	or	50004,	50005,	50006	50122,	50123,
	50267	50315	50037 or	50008,		50130,	50131,
			50107	50017,		50135,	50136,
				50023,		50198, or	50139,
				50026,		50247	50142,
				50038,			50145,
				50053,			50148,
				50067,			50154,
				50073,			50160,
				50085,			50181,
				50088,			50184,
				50100,			50199,
				50108,			50202,
				50238 or			50213 or
				50254			50248
48B12	31820	27814	7784,	15796,	23808	3780	11792 or	19804
	or		50034,	50032,			50126
	50267		50055,	50035,
			50093,	50056,
			50113 or	50070,
			50116	50091,
				50105 or
				50117
184E7	30660	26654	6626,	14638 or	22650	2620,	10632,	18644
	or	or	50019 or	50020		50138,	50123,	or
	50272	50320	50237			50144,	50131,	50146
						50147,	50136,
						50183 or	50139,
						50212	50142,
							50145,
							50148,
							50154,
							50160,
							50181,
							50184,
							50199,
							50202,
							50213 or
							50248
194A4	30820	26814	6786	14798,	22810	2780 or	10792,	18804
		or		50020,		50206	50128 or	or
		50342		50050,			50207	50208
				50059 or
				50079
4B1	28878	24872	4844	12856	20868	836,	8848,	16860,
		or				50141 or	50123,	50143
		50323				50153	50131,	or
							50136,	50203
							50139,
							50142,
							50145,
							50148,
							50154,
							50160,
							50181,
							50184,
							50199,
							50202,
							50213 or
							50248
190F8	30712	26706	6678,	14690,	22702 or	2672,	10684 or	18696,
	or	or	50007,	50017,	50018	50138 or	50139	50140,
	50271	50318	50016,	50023,		50144		or
			50037,	50038 or				50146
			50066,	50088
			50072
			50084,
			50237 or
			50253
191G1	30628	26622	6594,	14606,	22618 or	2588,	10600,	18612
	or	or	50004,	50008 or	50018	50138,	50123,	or
	50271	50318	50007,	50017		50144,	50131,	50140
			50016,			50147,	50136,
			50022,			50183, or	50139,
			50025,			50212	50142,
			50037,				50145,
			50066,				50148,
			50072,				50154,
			50084,				50160,
			50087,				50181,
			50096,				50184,
			50099,				50199,
			50107,				50202,
			50237 or				50213 or
			50252				50214
191G10	30846	26840	6812,	14824,	22836 or	2806,	10818 or	18830
	or	or	50004,	50017,	50018	50138 or	50139	or
	50271	50318	50007,	50023,		50144		50140
			50016,	50038, or
			50022,	50088
			50025,
			50037,
			50066,
			50072,
			50084,
			50087,
			50096,
			50099,
			50107,
			50237 or
			50253
194C1	30816	26810	6782,	14794,	22806	2776,	10788,	18800
			50004,	50008, or		50138,	50123,	or
			50007,	50017		50144,	50131,	50140
			50016,			50147,	50136,
			50022,			50183 or	50139,
			50025,			50212	50142,
			50037,				50145,
			50066,				50148,
			50072,				50154,
			50084,				50160,
			50087,				50181,
			50096,				50184,
			50099,				50199,
			50107,				50202,
			50237 or				50213 or
			50253				50248
197G3	30888	26882	6854,	14866,	22878 or	2848,	10860,	18872
	or	or	50016 or	50017,	50024	50138 or	50123,	or
	50273	50320	50022	50023,		50144	50131,	50140
				50038, or			50136,
				50088			50139,
							50142,
							50145,
							50148,
							50154,
							50160,
							50181,
							50184,
							50199,
							50202,
							50213 or
							50248
198G3	30620	26614	6586,	14598,	22610 or	2580 or	10592 or	18604
	or	or	50007,	50017, or	50018	50138	50139	or
	50271	50318	50016,	50038				50140
			50037,
			50066,
			50072,
			50084,
			50237 or
			50253
75G3	29714	25708	5680,	13692	21704 or	1674 or	9686 or	17698
	or	or	50010 or		50235	50127	50128	or
	50283	50314	50233					50129
218G4	31786	27780	7750,	15762,	23774	3746 or	11758 or	19770
	or	or	50004,	50005,		50189	50190	or
	50298	50335	50025,	50008,				50191
			50037,	50017,
			50087,	50023,
			50096 or	50026,
			50253	50038,
				50053,
				50067,
				50073,
				50085,
				50088,
				50100,
				50108,
				50238 or
				50254
193E7	30796	26790	6762	14774,	22786	2756,	10768,	18780
		or		50011, or		50122,	50123 or	or
		50312		50234		50130,	50142	50124
						50135,
						50198, or
						50247
198D2	31604	27598	7568,	15580 or	23592	3564 or	11576 or	19588
	or	or	50004,	50023		50189	50190	or
	50273	50335	50007,					50191
			50016,
			50022,
			50025,
			50037,
			50066,
			50072,
			50084,
			50087,
			50096,
			50099,
			50107,
			50237 or
			50253
202A3	30972	26966	6938	14950	22962	2932,	10944,	18956
		or				50122,	50123,	or
		50317				50130,	50131,	50137
						50135,	50136,
						50198, or	50139,
						50247	50142,
							50148, or
							50213
7E11	28914	24908	4880,	12892 or	20904 or	872 or	8884,	16896,
	or	or	50004,	50263 or	50024	50141 or	50123,	or
	50273	50319	50007,	50023		50153	50131,	50143
			50022,				50136,
			50025 or				50139,
			50037				50142,
							50145,
							50148,
							50154,
							50160,
							50181,
							50199 or
							50213
22G5	28368	24362	4334,	12346 or	20358 or	326,	8338,	16350
		or	50031,	50032	50033	50141,	50123,
		50323	50034,			50153,	50131,
			50055,			50180 or	50136,
			50093,			50201	50139,
			50113 or				50142,
			50116				50148,
							50154 or
							50160
5E5	29016	25010	4982	12994,	21006,	974	8986,	16998
	or	or	50004,	50005,	50006 or	50122,	50123,	or
	50267	50315	50037 or	50008,	50265	50130,	50131,	50132
			50107	50017,		50135,	50136,
				50023,		50198, or	50139,
				50026,		50247	50142,
				50038,			50145,
				50053,			50148,
				50067,			50154,
				50073,			50160,
				50085,			50181,
				50088,			50184,
				50100,			50199,
				50108,			50202,
				50238,			50213 or
				50254 or			50248
				50264,
54E9	31488	27482	7452 or	15464 or	23476 or	3448 or	11460 or	19472
	or	or	50102	50103	50227	50195	50196	or
	50303	50338						50197
6G7	28880	24874	4846,	12858	20870 or	838 or	8850 or	16862
		or	50004,		50098	50186	50187	or
		50334	50007,					50188
			50016,
			50022,
			50025,
			50037,
			50066,
			50072,
			50084,
			50087,
			50096,
			50099,
			50107,
			50237 or
			50253
176H4	30542	26536	6508,	14520,	22532,	2502,	10514,	18526
	or	or	50004,	50023,	or 50255	50150, or	50151,	or
	50282	50322	50007,	50053,		50174	50175 or	50152
			50016,	50085 or			50205
			50022,	50254
			50025,
			50037,
			50066,
			50072,
			50084,
			50087,
			50096,
			50099,
			50107,
			50237 or
			50253
194C10	30832	26826	6798 or	14810,	22822	2792 or	10804 or	18816
		or	50233	50011 or		50146	50128	or
		50314		50234				50129

In the exemplary embodiments described above, the antigen binding proteins maintain desired binding to the various desired species of ASGR, ASGR-1 and/or ASGR-2.

In another embodiment, the light-chain variable domain comprises a sequence of amino acids that is at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of a light chain variable domain listed above.

In another embodiment, the light chain variable domain comprises a sequence of amino acids that is encoded by a nucleotide sequence that is at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the polynucleotide sequence listed above. In another embodiment, the light chain variable domain comprises a sequence of amino acids that is encoded by a polynucleotide that hybridizes under moderately stringent conditions to the complement of a polynucleotide that encodes a light chain variable domain selected from the sequences listed above. In another embodiment, the light chain variable domain comprises a sequence of amino acids that is encoded by a polynucleotide that hybridizes under stringent conditions to the complement of a polynucleotide that encodes a light chain variable domain selected from the group consisting of the sequences listed above.

In another embodiment, the heavy chain variable domain comprises a sequence of amino acids that is at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of a heavy chain variable domain selected from the sequences listed above. In another embodiment, the heavy chain variable domain comprises a sequence of amino acids that is encoded by a nucleotide sequence that is at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to a nucleotide sequence that encodes a heavy chain variable domain selected from the sequences listed above. In another embodiment, the heavy chain variable domain comprises a sequence of amino acids that is encoded by a polynucleotide that hybridizes under moderately stringent conditions to the complement of a polynucleotide that encodes a heavy chain variable domain selected from the sequences listed above. In another embodiment, the heavy chain variable domain comprises a sequence of amino acids that is encoded by a polynucleotide that hybridizes under stringent conditions to the complement of a polynucleotide that encodes a heavy chain variable domain selected from the sequences listed above.

In the exemplary embodiments described above, the antigen binding proteins maintain desired binding to the various desired species of ASGR, ASGR-1 and/or ASGR-2.

Antigen binding proteins of the invention (e.g., antibodies) can comprise any constant region known in the art. The light chain constant region can be, for example, a kappa- or lambda-type light chain constant region, e.g., a human kappa- or lambda-type light chain constant region. The heavy chain constant region can be, for example, an alpha-, delta-, epsilon-, gamma-, or mu-type heavy chain constant regions, e.g., a human alpha-, delta-, epsilon-, gamma-, or mu-type heavy chain constant region.

Techniques are known for deriving an antibody of a different subclass or isotype from an antibody of interest, i.e., subclass switching. Thus, IgG antibodies may be derived from an IgM antibody, for example, and vice versa. Such techniques allow the preparation of new antibodies that possess the antigen-binding properties of a given antibody (the parent antibody), but also exhibit biological properties associated with an antibody isotype or subclass different from that of the parent antibody. Recombinant DNA techniques may be employed. Cloned DNA encoding particular antibody polypeptides may be employed in such procedures, e.g., DNA encoding the constant domain of an antibody of the desired isotype. See also Lanitto et al., Methods Mol. Biol. 178:303-16 (2002).

In one embodiment, an antigen binding protein of the invention further comprises the constant light chain kappa or lambda domains or a fragment of these. Exemplary sequences of the light chain constant regions and polynucleotides encoding them are provided in Table 15 below, and are generally well known in the art. In another embodiment, an antigen binding protein of the invention further comprises a heavy chain constant domain, or a fragment thereof, such as the IgG1 or IgG2 heavy chain constant region provided in Table 15.

The antigen binding proteins (for example, antibodies) of the present invention include those having a desired isotype (for example, IgA, IgG1, IgG2, IgG3, IgG4, IgM, IgE, and IgD) as well as Fab or F(ab′)₂ fragments thereof. Moreover, if an IgG4 is desired, it may also be desired to introduce a point mutation in the hinge region as described in Bloom et al., 1997, Protein Science 6:407, (incorporated by reference herein) to alleviate a tendency to form intra-H chain disulfide bonds that can lead to heterogeneity in the IgG4 antibodies.

Generation of Antibodies

Antibodies of the invention may be prepared by techniques that are well known to those skilled in the art. For example, by immunizing an animal (e.g., a mouse or rat or rabbit) and then by immortalizing spleen cells harvested from the animal after completion of the immunization schedule. The spleen cells can be immortalized using any technique known in the art, e.g., by fusing them with myeloma cells to produce hybridomas. See, for example, Antibodies; Harlow and Lane, Cold Spring Harbor Laboratory Press, 1^st Edition, e.g. from 1988, or 2^nd Edition, e.g. from 2014).

In one embodiment, a humanized monoclonal antibody comprises the variable domain of a murine antibody (or all or part of the antigen binding site thereof) and a constant domain derived from a human antibody. Alternatively, a humanized antibody fragment may comprise the antigen binding site of a murine monoclonal antibody and a variable domain fragment (lacking the antigen-binding site) derived from a human antibody. Procedures for the production of engineered monoclonal antibodies include those described in Riechmann et al., 1988, Nature 332:323, Liu et al., 1987, Proc. Nat. Acad. Sci. USA 84:3439, Larrick et al., 1989, Bio/Technology 7:934, and Winter et al., 1993, TIPS 14:139. In one embodiment, the chimeric antibody is a CDR grafted antibody. Techniques for humanizing antibodies are discussed in, e.g., U.S. Pat. Nos. 5,869,619; 5,225,539; 5,821,337; 5,859,205; 6,881,557, Padlan et al., 1995, FASEB J. 9:133-39, Tamura et al., 2000, J. Immunol. 164:1432-41, Zhang, W., et al., Molecular Immunology. 42(12):1445-1451, 2005; Hwang W. et al., Methods. 36(1):35-42, 2005; Dall'Acqua W F, et al., Methods 36(1):43-60, 2005; and Clark, M., Immunology Today. 21(8):397-402, 2000.

An antibody of the present invention may also be a fully human monoclonal antibody. Fully human monoclonal antibodies may be generated by any number of techniques with which those having ordinary skill in the art will be familiar. Such methods include, but are not limited to, Epstein Barr Virus (EBV) transformation of human peripheral blood cells (e.g., containing B lymphocytes), in vitro immunization of human B-cells, fusion of spleen cells from immunized transgenic mice carrying inserted human immunoglobulin genes, isolation from human immunoglobulin V region phage libraries, or other procedures as known in the art and based on the disclosure herein.

Procedures have been developed for generating human monoclonal antibodies in non-human animals. For example, mice in which one or more endogenous immunoglobulin genes have been inactivated by various means have been prepared. Human immunoglobulin genes have been introduced into the mice to replace the inactivated mouse genes. In this technique, elements of the human heavy and light chain locus are introduced into strains of mice derived from embryonic stem cell lines that contain targeted disruptions of the endogenous heavy chain and light chain loci (see also Bruggemann et al., Curr. Opin. Biotechnol. 8:455-58 (1997)). For example, human immunoglobulin transgenes may be mini-gene constructs, or transloci on yeast artificial chromosomes, which undergo B-cell-specific DNA rearrangement and hypermutation in the mouse lymphoid tissue.

Antibodies produced in the animal incorporate human immunoglobulin polypeptide chains encoded by the human genetic material introduced into the animal. In one embodiment, a non-human animal, such as a transgenic mouse, is immunized with a suitable immunogen.

Examples of techniques for production and use of transgenic animals for the production of human or partially human antibodies are described in U.S. Pat. Nos. 5,814,318, 5,569,825, and 5,545,806, Davis et al., Production of human antibodies from transgenic mice in Lo, ed. Antibody Engineering: Methods and Protocols, Humana Press, NJ:191-200 (2003), Kellermann et al., 2002, Curr Opin Biotechnol. 13:593-97, Russel et al., 2000, Infect Immun. 68:1820-26, Gallo et al., 2000, Eur J Immun. 30:534-40, Davis et al., 1999, Cancer Metastasis Rev. 18:421-25, Green, 1999, J Immunol Methods. 231:11-23, Jakobovits, 1998, Advanced Drug Delivery Reviews 31:33-42, Green et al., 1998, J Exp Med. 188:483-95, Jakobovits A, 1998, Exp. Opin. Invest. Drugs. 7:607-14, Tsuda et al., 1997, Genomics. 42:413-21, Mendez et al., 1997, Nat Genet. 15:146-56, Jakobovits, 1994, Curr Biol. 4:761-63, Arbones et al., 1994, Immunity. 1:247-60, Green et al., 1994, Nat Genet. 7:13-21, Jakobovits et al., 1993, Nature. 362:255-58, Jakobovits et al., 1993, Proc Natl Acad Sci USA. 90:2551-55. Chen, J., M. Trounstine, F. W. Alt, F. Young, C. Kurahara, J. Loring, D. Huszar. “Immunoglobulin gene rearrangement in B-cell deficient mice generated by targeted deletion of the JH locus.” International Immunology 5 (1993): 647-656, Choi et al., 1993, Nature Genetics 4: 117-23, Fishwild et al., 1996, Nature Biotechnology 14: 845-51, Harding et al., 1995, Annals of the New York Academy of Sciences, Lonberg et al., 1994, Nature 368: 856-59, Lonberg, 1994, Transgenic Approaches to Human Monoclonal Antibodies in Handbook of Experimental Pharmacology 113: 49-101, Lonberg et al., 1995, Internal Review of Immunology 13: 65-93, Neuberger, 1996, Nature Biotechnology 14: 826, Taylor et al., 1992, Nucleic Acids Research 20: 6287-95, Taylor et al., 1994, International Immunology 6: 579-91, Tomizuka et al., 1997, Nature Genetics 16: 133-43, Tomizuka et al., 2000, Proceedings of the National Academy of Sciences USA 97: 722-27, Tuaillon et al., 1993, Proceedings of the National Academy of Sciences USA 90: 3720-24, and Tuaillon et al., 1994, Journal of Immunology 152: 2912-20.; Lonberg et al., Nature 368:856, 1994; Taylor et al., Int. Immun. 6:579, 1994; U.S. Pat. No. 5,877,397; Bruggemann et al., 1997 Curr. Opin. Biotechnol. 8:455-58; Jakobovits et al., 1995 Ann. N. Y. Acad. Sci. 764:525-35. In addition, protocols involving the XenoMouse® (Abgenix, now Amgen, Inc.) are described, for example in U.S. Ser. No. 05/011,8643 and WO 05/694879, WO 98/24838, WO 00/76310, and U.S. Pat. No. 7,064,244.

Lymphoid cells from the immunized transgenic mice are fused with myeloma cells for example to produce hybridomas. Myeloma cells for use in hybridoma-producing fusion procedures preferably are non-antibody-producing, have high fusion efficiency, and enzyme deficiencies that render them incapable of growing in certain selective media which support the growth of only the desired fused cells (hybridomas). Examples of suitable cell lines for use in such fusions include Sp-20, P3-X63/Ag8, P3-X63-Ag8.653, NS1/1.Ag 4 1, Sp210-Ag14, FO, NSO/U, MPC-11, MPC11-X45-GTG 1.7 and S194/5XX0 Bul; examples of cell lines used in rat fusions include R210.RCY3, Y3-Ag 1.2.3, IR983F and 4B210. Other cell lines useful for cell fusions are U-266, GM1500-GRG2, LICR-LON-HMy2 and UC729-6.

The lymphoid (e.g., spleen) cells and the myeloma cells may be combined for a few minutes with a membrane fusion-promoting agent, such as polyethylene glycol or a nonionic detergent, and then plated at low density on a selective medium that supports the growth of hybridoma cells but not unfused myeloma cells. One selection media is HAT (hypoxanthine, aminopterin, thymidine). After a sufficient time, usually about one to two weeks, colonies of cells are observed. Single colonies are isolated, and antibodies produced by the cells may be tested for binding activity to, for example, human ASGR-1, using any one of a variety of immunoassays known in the art and described herein. The hybridomas are cloned (e.g., by limited dilution cloning or by soft agar plaque isolation) and positive clones that produce an antibody specific to, for example, human ASGR-1, are selected and cultured. The monoclonal antibodies from the hybridoma cultures may be isolated from the supernatants of hybridoma cultures. Thus the present invention provides hybridomas that comprise polynucleotides encoding the antigen binding proteins of the invention in the chromosomes of the cell. These hybridomas can be cultured according to methods described herein and known in the art.

Another method for generating human antibodies of the invention includes immortalizing human peripheral blood cells by EBV transformation. See, e.g., U.S. Pat. No. 4,464,456. Such an immortalized B-cell line (or lymphoblastoid cell line) producing a monoclonal antibody that specifically binds to, for example, human ASGR-1, can be identified by immunodetection methods as provided herein, for example, an ELISA, and then isolated by standard cloning techniques. The stability of the lymphoblastoid cell line producing an antibody may be improved by fusing the transformed cell line with a murine myeloma to produce a mouse-human hybrid cell line according to methods known in the art (see, e.g., Glasky et al., Hybridoma 8:377-89 (1989)). Still another method to generate human monoclonal antibodies is in vitro immunization, which includes priming human splenic B-cells with antigen, followed by fusion of primed B-cells with a heterohybrid fusion partner. See, e.g., Boerner et al., 1991 J. Immunol. 147:86-95.

In certain embodiments, a B-cell that is producing a desired antibody is selected and the light chain and heavy chain variable regions are cloned from the B-cell according to molecular biology techniques known in the art (WO 92/02551; U.S. Pat. No. 5,627,052; Babcook et al., Proc. Natl. Acad. Sci. USA 93:7843-48 (1996)) and described herein. B-cells from an immunized animal may be isolated from the spleen, lymph node, or peripheral blood sample by selecting a cell that is producing a desired antibody. B-cells may also be isolated from humans, for example, from a peripheral blood sample. Methods for detecting single B-cells that are producing an antibody with the desired specificity are well known in the art, for example, by plaque formation, fluorescence-activated cell sorting, in vitro stimulation followed by detection of specific antibody, and the like. Methods for selection of specific antibody-producing B-cells include, for example, preparing a single cell suspension of B-cells in soft agar that contains antigen. Binding of the specific antibody produced by the B-cell to the antigen results in the formation of a complex, which may be visible as an immunoprecipitate. After the B-cells producing the desired antibody are selected, the specific antibody genes may be cloned by isolating and amplifying DNA or mRNA according to methods known in the art and described herein.

An additional method for obtaining antibodies of the invention is by phage display. See, e.g., Winter et al., 1994 Annu. Rev. Immunol. 12:433-55; Burton et al., 1994 Adv. Immunol. 57:191-280. Human or murine immunoglobulin variable region gene combinatorial libraries may be created in phage vectors that can be screened to select Ig fragments (Fab, Fv, sFv, or multimers thereof) that bind specifically to TGF-beta binding protein or variant or fragment thereof. See, e.g., U.S. Pat. No. 5,223,409; Huse et al., 1989 Science 246:1275-81; Sastry et al., Proc. Natl. Acad. Sci. USA 86:5728-32 (1989); Alting-Mees et al., Strategies in Molecular Biology 3:1-9 (1990); Kang et al., 1991 Proc. Natl. Acad. Sci. USA 88:4363-66; Hoogenboom et al., 1992 J. Molec. Biol. 227:381-388; Schlebusch et al., 1997 Hybridoma 16:47-52 and references cited therein. For example, a library containing a plurality of polynucleotide sequences encoding Ig variable region fragments may be inserted into the genome of a filamentous bacteriophage, such as M13 or a variant thereof, in frame with the sequence encoding a phage coat protein. A fusion protein may be a fusion of the coat protein with the light chain variable region domain and/or with the heavy chain variable region domain. According to certain embodiments, immunoglobulin Fab fragments may also be displayed on a phage particle (see, e.g., U.S. Pat. No. 5,698,426).

Heavy and light chain immunoglobulin cDNA expression libraries may also be prepared in lambda phage, for example, using λlmmunoZap™(H) and λImmunoZap™(L) vectors (Stratagene, La Jolla, Calif.). Briefly, mRNA is isolated from a B-cell population, and used to create heavy and light chain immunoglobulin cDNA expression libraries in the λImmunoZap(H) and λImmunoZap(L) vectors. These vectors may be screened individually or co-expressed to form Fab fragments or antibodies (see Huse et al., supra; see also Sastry et al., supra). Positive plaques may subsequently be converted to a non-lytic plasmid that allows high level expression of monoclonal antibody fragments from E. coli.

In one embodiment, in a hybridoma the variable regions of a gene expressing a monoclonal antibody of interest are amplified using nucleotide primers. These primers may be synthesized by one of ordinary skill in the art, or may be purchased from commercially available sources. (See, e.g., Stratagene (La Jolla, Calif.), which sells primers for mouse and human variable regions including, among others, primers for V_Ha, V_Hb, V_Hc, V_Hd, C_H1, V_L and C_L regions.) These primers may be used to amplify heavy or light chain variable regions, which may then be inserted into vectors such as ImmunoZAP™H or ImmunoZAP™L (Stratagene), respectively. These vectors may then be introduced into E. coli, yeast, or mammalian-based systems for expression. Large amounts of a single-chain protein containing a fusion of the V_H and V_L domains may be produced using these methods (see Bird et al., Science 242:423-426, 1988).

In certain embodiments, the antigen binding proteins of the invention are obtained from transgenic animals (e.g., mice) that produce “heavy chain only” antibodies or “HCAbs.” HCAbs are analogous to naturally occurring camel and llama single-chain VHH antibodies.

See, for example, U.S. Pat. Nos. 8,507,748 and 8,502,014, and U.S. Patent Application Publication Nos. US2009/0285805A1, US2009/0169548A1, US2009/0307787A1, US2011/0314563A1, US2012/0151610A1, WO2008/122886A2, and WO2009/013620A2.

Once cells producing antibodies according to the invention have been obtained using any of the above-described immunization and other techniques, the specific antibody genes may be cloned by isolating and amplifying DNA or mRNA therefrom according to standard procedures as described herein. The antibodies produced therefrom may be sequenced and the CDRs identified and the DNA coding for the CDRs may be manipulated as described previously to generate other antibodies according to the invention.

In certain embodiments, antibodies are generated by first identifying antibodies that bind to cells expressing, for example, human ASGR, human ASGR-1 and/or human ASGR-2, and/or compete for binding with the antibodies described in this application.

It will be understood by one skilled in the art that some proteins, such as antibodies, may undergo a variety of posttranslational modifications. The type and extent of these modifications often depends on the host cell line used to express the protein as well as the culture conditions. Such modifications may include variations in glycosylation, methionine oxidation, diketopiperizine formation, aspartate isomerization and asparagine deamidation. A frequent modification is the loss of a carboxy-terminal basic residue (such as lysine or arginine) due to the action of carboxypeptidases (as described in Harris, R. J. Journal of Chromatography 705:129-134, 1995).

An alternative method for production of a murine monoclonal antibody is to inject the hybridoma cells into the peritoneal cavity of a syngeneic mouse, for example, a mouse that has been treated (e.g., pristane-primed) to promote formation of ascites fluid containing the monoclonal antibody. Monoclonal antibodies can be isolated and purified by a variety of well-established techniques. Such isolation techniques include affinity chromatography with Protein-A Sepharose, size-exclusion chromatography, and ion-exchange chromatography (see, for example, Coligan at pages 2.7.1-2.7.12 and pages 2.9.1-2.9.3; Baines et al., “Purification of Immunoglobulin G (IgG),” in Methods in Molecular Biology, Vol. 10, pages 79-104 (The Humana Press, Inc. 1992)). Monoclonal antibodies may be purified by affinity chromatography using an appropriate ligand selected based on particular properties of the antibody (e.g., heavy or light chain isotype, binding specificity, etc.). Examples of a suitable ligand, immobilized on a solid support, include Protein A, Protein G, an anticonstant region (light chain or heavy chain) antibody, an anti-idiotype antibody, and a TGF-beta binding protein, or fragment or variant thereof.

Molecular evolution of the complementarity determining regions (CDRs) in the center of the antibody binding site also has been used to isolate antibodies with increased affinity, for example, those as described by Schier et al., 1996, J. Mol. Biol. 263:551. Accordingly, such techniques are useful in preparing antibodies of the invention.

Although human, partially human, or humanized antibodies will be suitable for many applications, particularly those involving administration of the antibody to a human subject, other types of antigen binding proteins will be suitable for certain applications. The non-human antibodies of the invention can be, for example, derived from any antibody-producing animal, such as mouse, rat, rabbit, goat, donkey, or non-human primate (for example, monkey such as cynomologous or rhesus monkey) or ape (e.g., chimpanzee)). Non-human antibodies of the invention can be used, for example, in in vitro and cell-culture based applications, or any other application where an immune response to the antibody of the invention does not occur, is insignificant, can be prevented, is not a concern, or is desired. An antibody from a particular species can be made by, for example, immunizing an animal of that species with the desired immunogen or using an artificial system for generating antibodies of that species (e.g., a bacterial or phage display-based system for generating antibodies of a particular species), or by converting an antibody from one species into an antibody from another species by replacing, e.g., the constant region of the antibody with a constant region from the other species, or by replacing one or more amino acid residues of the antibody so that it more closely resembles the sequence of an antibody from the other species. In one embodiment, the antibody is a chimeric antibody comprising amino acid sequences derived from antibodies from two or more different species.

Antibodies also may be prepared by any of a number of other conventional techniques. For example, they may be purified from cells that naturally express them (e.g., an antibody can be purified from a hybridoma that produces it), or produced in recombinant expression systems, using any technique known in the art. See, for example, Monoclonal Antibodies, Hybridomas: A New Dimension in Biological Analyses, Kenneth et al. (eds.), Plenum Press, New York (1980); and Antibodies: A Laboratory Manual, Harlow and Land (eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., (1988).

Where it is desired to improve the affinity of antibodies according to the invention containing one or more of the above-mentioned CDRs can be obtained by a number of affinity maturation protocols including maintaining the CDRs (Yang et al., J. Mol. Biol., 254, 392-403, 1995), chain shuffling (Marks et al., Bio/Technology, 10, 779-783, 1992), use of mutation strains of E. coli. (Low et al., J. Mol. Biol., 250, 350-368, 1996), DNA shuffling (Patten et al., Curr. Opin. Biotechnol., 8, 724-733, 1997), phage display (Thompson et al., J. Mol. Biol., 256, 7-88, 1996) and additional PCR techniques (Crameri, et al., Nature, 391, 288-291, 1998). All of these methods of affinity maturation are discussed by Vaughan et al. (Nature Biotechnology, 16, 535-539, 1998).

Single chain antibodies may be formed by linking heavy and light chain variable domain (Fv region) fragments via an amino acid bridge (short peptide linker), resulting in a single polypeptide chain. Such single-chain Fvs (scFvs) have been prepared by fusing DNA encoding a peptide linker between DNAs encoding the two variable domain polypeptides (V_L and V_H). The resulting polypeptides can fold back on themselves to form antigen-binding monomers, or they can form multimers (e.g., dimers, trimers, or tetramers), depending on the length of a flexible linker between the two variable domains (Kortt et al., 1997, Prot. Eng. 10:423; Kortt et al., 2001, Biomol. Eng. 18:95-108). By combining different V_L and V_H-comprising polypeptides, one can form multimeric scFvs that bind to different epitopes (Kriangkum et al., 2001, Biomol. Eng. 18:31-40). Techniques developed for the production of single chain antibodies include those described in U.S. Pat. No. 4,946,778; Bird, 1988, Science 242:423; Huston et al., 1988, Proc. Natl. Acad. Sci. USA 85:5879; Ward et al., 1989, Nature 334:544, de Graaf et al., 2002, Methods Mol Biol. 178:379-87.

Antigen binding fragments derived from an antibody can also be obtained, for example, by proteolytic hydrolysis of the antibody, for example, pepsin or papain digestion of whole antibodies according to conventional methods. By way of example, antibody fragments can be produced by enzymatic cleavage of antibodies with pepsin to provide a 5S fragment termed F(ab′)₂. This fragment can be further cleaved using a thiol reducing agent to produce 3.5S Fab′ monovalent fragments. Optionally, the cleavage reaction can be performed using a blocking group for the sulfhydryl groups that result from cleavage of disulfide linkages. As an alternative, an enzymatic cleavage using papain produces two monovalent Fab fragments and an Fc fragment directly. These methods are described, for example, by Goldenberg, U.S. Pat. No. 4,331,647, Nisonoff et al., Arch. Biochem. Biophys. 89:230, 1960; Porter, Biochem. J. 73:119, 1959; Edelman et al., in Methods in Enzymology 1:422 (Academic Press 1967); and by Andrews, S. M. and Titus, J. A. in Current Protocols in Immunology (Coligan J. E., et al., eds), John Wiley & Sons, New York (2003), pages 2.8.1-2.8.10 and 2.10A. 1-2.10A. 5. Other methods for cleaving antibodies, such as separating heavy chains to form monovalent light-heavy chain fragments (Fd), further cleaving of fragments, or other enzymatic, chemical, or genetic techniques may also be used, so long as the fragments bind to the antigen that is recognized by the intact antibody.

Another exemplary form of an antigen binding protein is a peptide comprising one or more complementarity determining regions (CDRs) of an antibody. CDRs can be obtained by constructing polynucleotides that encode the CDR of interest. Such polynucleotides are prepared, for example, by using the polymerase chain reaction to synthesize the variable region using mRNA of antibody-producing cells as a template (see, for example, Larrick et al., Methods: A Companion to Methods in Enzymology 2:106, 1991; Courtenay-Luck, “Genetic Manipulation of Monoclonal Antibodies,” in Monoclonal Antibodies: Production, Engineering and Clinical Application, Ritter et al. (eds.), page 166 (Cambridge University Press 1995); and Ward et al., “Genetic Manipulation and Expression of Antibodies,” in Monoclonal Antibodies: Principles and Applications, Birch et al., (eds.), page 137 (Wiley-Liss, Inc. 1995)). The antibody fragment further may comprise at least one variable region domain of an antibody described herein. Thus, for example, the V region domain may be monomeric and be a V_H or V_L domain, which is capable of independently binding a desired target (e.g., human ASGR-1) with an affinity at least equal to 10⁻⁷M or less as described herein.

The variable region may be any naturally occurring variable domain or an engineered version thereof. By engineered version is meant a variable region that has been created using recombinant DNA engineering techniques. Such engineered versions include those created, for example, from a specific antibody variable region by insertions, deletions, or changes in or to the amino acid sequences of the specific antibody. One of ordinary skill in the art can use any known methods for identifying amino acid residues appropriate for engineering, such as the amino acid residues depicted with shading in Tables 21-48 of FIG. 56. Additional examples include engineered variable regions containing at least one CDR and optionally one or more framework amino acids from a first antibody and the remainder of the variable region domain from a second antibody. Engineered versions of antibody variable domains may be generated by any number of techniques with which those having ordinary skill in the art will be familiar, including but not limited to the methods outlined in Example 14 below.

The variable region may be covalently attached at a C-terminal amino acid to at least one other antibody domain or a fragment thereof. Thus, for example, a VH that is present in the variable region may be linked to an immunoglobulin CH1 domain. Similarly a V_L domain may be linked to a C_K domain. In this way, for example, the antibody may be a Fab fragment wherein the antigen binding domain contains associated V_H and V_L domains covalently linked at their C-termini to a CH1 and C_K domain, respectively. The CH1 domain may be extended with further amino acids, for example to provide a hinge region or a portion of a hinge region domain as found in a Fab′ fragment, or to provide further domains, such as antibody CH2 and CH3 domains.

Derivatives and Variants

The nucleotide sequences of the antigen binding proteins of the present invention, encoding the corresponding amino acid sequences of the antibodies of the present invention, can be altered, for example, by random mutagenesis or by site-directed mutagenesis (e.g., oligonucleotide-directed site-specific mutagenesis) to create an altered polynucleotide comprising one or more particular nucleotide substitutions, deletions, or insertions as compared to the non-mutated polynucleotide. Examples of techniques for making such alterations are described in Walder et al., 1986, Gene 42:133; Bauer et al. 1985, Gene 37:73; Craik, BioTechniques, January 1985, 12-19; Smith et al., 1981, Genetic Engineering: Principles and Methods, Plenum Press; and U.S. Pat. Nos. 4,518,584 and 4,737,462. These and other methods can be used to make, for example, derivatives of the antigen binding proteins that have a desired property, for example, increased affinity, avidity, or specificity for a desired target, increased activity or stability in vivo or in vitro, or reduced in vivo side-effects as compared to the underivatized antibody.

Other derivatives of the antigen binding proteins within the scope of this invention include covalent or aggregative conjugates of the antigen binding proteins, with other proteins or polypeptides, such as by expression of recombinant fusion proteins comprising heterologous polypeptides fused to the N-terminus or C-terminus of a polypeptide. For example, the conjugated peptide may be a heterologous signal (or leader) polypeptide, e.g., the yeast alpha-factor leader, or a peptide such as an epitope tag. Antigen binding protein-containing fusion proteins can comprise peptides added to facilitate purification or identification of antigen binding protein (e.g., poly-His). An antigen binding protein also can be linked to the FLAG peptide as described in Hopp et al., Bio/Technology 6:1204, 1988, and U.S. Pat. No. 5,011,912. The FLAG peptide is highly antigenic and provides an epitope reversibly bound by a specific monoclonal antibody (mAb), enabling rapid assay and facile purification of expressed recombinant protein. Reagents useful for preparing fusion proteins in which the FLAG peptide is fused to a given polypeptide are commercially available (Sigma, St. Louis, Mo.).

In another embodiment, the antigen binding proteins within the scope of this invention include antibody conjugates where antibody is conjugated to a non-proteinaceous chemical (drug) to form an antibody drug conjugate (ADC). Generally the ADC comprises an antibody conjugated to a chemotherapeutic agent, e.g., a cytotoxic agent, a cytostatic agent, a toxin, or a radioactive agent. A linker molecule can be used to conjugate the drug to the antibody. A wide variety of linkers and drugs useful in ADC technology are known in the art and may be used in embodiments of the present invention. (See US20090028856; US2009/0274713; US2007/0031402; WO2005/084390; WO2009/099728; U.S. Pat. No. 5,208,020; U.S. Pat. No. 5,416,064; U.S. Pat. Nos. 5,475,092; 5,585,499; 6,436,931; 6,372,738; and 6,340,701, all incorporated herein by reference).

In another embodiment, oligomers that contain one or more antigen binding proteins may be employed in certain embodiments of the present invention. Oligomers may be in the form of covalently-linked or non-covalently-linked dimers, trimers, or higher oligomers. Oligomers comprising two or more antigen binding protein are contemplated for use, with one example being a homodimer. Other oligomers include heterodimers, homotrimers, heterotrimers, homotetramers, heterotetramers, etc.

One embodiment is directed to oligomers comprising multiple antigen binding proteins joined via covalent or non-covalent interactions between peptide moieties fused to the antigen binding proteins. Such peptides may be peptide linkers (spacers), or peptides that have the property of promoting oligomerization. Leucine zippers and certain polypeptides derived from antibodies are among the peptides that can promote oligomerization of antigen binding proteins attached thereto, as described in more detail below.

In particular embodiments, the oligomers comprise from two to four antigen binding proteins. The antigen binding proteins of the oligomer may be in any form, such as any of the forms described above, e.g., variants.

In one embodiment, an oligomer is prepared using polypeptides derived from immunoglobulins. Preparation of fusion proteins comprising certain heterologous polypeptides fused to various portions of antibody-derived polypeptides (including the Fc domain) has been described, e.g., by Ashkenazi et al., 1991, PNAS USA 88:10535; Byrn et al., 1990, Nature 344:677; and Hollenbaugh et al., 1992 “Construction of Immunoglobulin Fusion Proteins”, in Current Protocols in Immunology, Suppl. 4, pages 10.19.1-10.19.11.

One embodiment of the present invention is directed to a dimer comprising two fusion proteins created by fusing an antigen binding fragment of an anti-ASGR, ASGR-1, and/or ASGR-2 antibody to the Fc region of an antibody. The dimer can be made by, for example, inserting a gene fusion encoding the fusion protein into an appropriate expression vector, expressing the gene fusion in host cells transformed with the recombinant expression vector, and allowing the expressed fusion protein to assemble much like antibody molecules, whereupon interchain disulfide bonds form between the Fc moieties to yield the dimer.

The term “Fc polypeptide” as used herein includes native and mutein forms of polypeptides derived from the Fc region of an antibody. Truncated forms of such polypeptides containing the hinge region that promotes dimerization also are included. Fusion proteins comprising Fc moieties (and oligomers formed therefrom) offer the advantage of facile purification by affinity chromatography over Protein A or Protein G columns.

One suitable Fc polypeptide, described in PCT application WO 93/10151 (hereby incorporated by reference), is a single chain polypeptide extending from the N-terminal hinge region to the native C-terminus of the Fc region of a human IgG1 antibody. Another useful Fc polypeptide is the Fc mutein described in U.S. Pat. No. 5,457,035 and in Baum et al., 1994, EMBO J. 13:3992-4001. The amino acid sequence of this mutein is identical to that of the native Fc sequence presented in WO 93/10151, except that amino acid 19 has been changed from Leu to Ala, amino acid 20 has been changed from Leu to Glu, and amino acid 22 has been changed from Gly to Ala. The mutein exhibits reduced affinity for Fc receptors.

In some embodiments, the variable portion of the heavy and/or light chains of a desired antibody may be substituted for the variable portion of an antibody heavy and/or light chain.

Alternatively, the oligomer is a fusion protein comprising multiple antigen binding proteins, with or without peptide linkers (spacer peptides). Among the suitable peptide linkers are those described in U.S. Pat. Nos. 4,751,180 and 4,935,233.

Another method for preparing oligomeric antigen binding proteins involves use of a leucine zipper. Leucine zipper domains are peptides that promote oligomerization of the proteins in which they are found. Leucine zippers were originally identified in several DNA-binding proteins (Landschulz et al., 1988, Science 240:1759), and have since been found in a variety of different proteins. Among the known leucine zippers are naturally occurring peptides and derivatives thereof that dimerize or trimerize. Examples of leucine zipper domains suitable for producing soluble oligomeric proteins are described in PCT application WO 94/10308, and the leucine zipper derived from lung surfactant protein D (SPD) described in Hoppe et al., 1994, FEBS Letters 344:191, hereby incorporated by reference. The use of a modified leucine zipper that allows for stable trimerization of a heterologous protein fused thereto is described in Fanslow et al., 1994, Semin. Immunol. 6:267-78. In one approach, recombinant fusion proteins comprising a desired antibody fragment or derivative fused to a leucine zipper peptide are expressed in suitable host cells, and the soluble oligomeric antibody fragments or derivatives that form are recovered from the culture supernatant.

In another embodiment, the antigen binding proteins (e.g., antibodies) can be conjugated to a suitable vehicle to enhance the half-life thereof. Suitable vehicles include, but are not limited to Fc, albumin, transferrin, and the like. These and other suitable vehicles are known in the art. Such conjugated CDR peptides may be in monomeric, dimeric, tetrameric, or other form. In one embodiment, one or more water-soluble polymer is bonded at one or more specific position, for example at the amino terminus, of a binding agent. In an example, an antibody derivative comprises one or more water soluble polymer attachments, including, but not limited to, polyethylene glycol, polyoxyethylene glycol, or polypropylene glycol. See, e.g., U.S. Pat. Nos. 4,640,835, 4,496,689, 4,301,144, 4,670,417, 4,791,192 and 4,179,337. In certain embodiments, a derivative comprises one or more of monomethoxy-polyethylene glycol, dextran, cellulose, or other carbohydrate based polymers, poly-(N-vinyl pyrrolidone)-polyethylene glycol, propylene glycol homopolymers, a polypropylene oxide/ethylene oxide co-polymer, polyoxyethylated polyols (e.g., glycerol) and polyvinyl alcohol, as well as mixtures of such polymers. In certain embodiments, one or more water-soluble polymer is randomly attached to one or more side chains. In certain embodiments, PEG can act to improve the therapeutic capacity for a binding agent, such as an antibody. Certain such methods are discussed, for example, in U.S. Pat. No. 6,133,426, which is hereby incorporated by reference for any purpose. In certain embodiments, antibodies of the invention may be chemically bonded with polymers, lipids, or other moieties.

Nucleic Acids Encoding Antigen Binding Proteins

In another embodiment, the present invention provides isolated nucleic acid molecules that encode the antigen binding proteins of the present invention. In addition, provided are vectors comprising the nucleic acids, cell comprising the nucleic acids, and methods of making the antigen binding proteins of the invention. The nucleic acids comprise, for example, polynucleotides that encode all or part of an antigen binding protein, for example, one or both chains of an antibody of the invention, or a fragment, derivative, mutein, or variant thereof, polynucleotides sufficient for use as hybridization probes, PCR primers or sequencing primers for identifying, analyzing, mutating or amplifying a polynucleotide encoding a polypeptide, anti-sense nucleic acids for inhibiting expression of a polynucleotide, and complementary sequences of the foregoing. The nucleic acids can be any length as appropriate for the desired use or function, and can comprise one or more additional sequences, for example, regulatory sequences, and/or be part of a larger nucleic acid, for example, a vector. The nucleic acids can be single-stranded or double-stranded and can comprise RNA and/or DNA nucleotides, and artificial variants thereof (e.g., peptide nucleic acids).

Nucleic acids encoding antibody polypeptides (e.g., heavy or light chain, variable domain only, or full length) may be isolated from B-cells of mice that have been immunized with antigen. The nucleic acid may be isolated by conventional procedures such as polymerase chain reaction (PCR).

Nucleic acid sequences encoding the variable regions of the heavy and light chain variable regions are included herein. The skilled artisan will appreciate that, due to the degeneracy of the genetic code, each of the polypeptide sequences disclosed herein is encoded by a large number of other nucleic acid sequences. The present invention provides each degenerate nucleotide sequence encoding each antigen binding protein of the invention.

The invention further provides nucleic acids that hybridize to other nucleic acids under particular hybridization conditions. Methods for hybridizing nucleic acids are well-known in the art. See, e.g., Current Protocols in Molecular Biology, John Wiley & Sons, N.Y. (1989), 6.3.1-6.3.6. As defined herein, for example, a moderately stringent hybridization condition uses a prewashing solution containing 5× sodium chloride/sodium citrate (SSC), 0.5% SDS, 1.0 mM EDTA (pH 8.0), hybridization buffer of about 50% formamide, 6×SSC, and a hybridization temperature of 55° C. (or other similar hybridization solutions, such as one containing about 50% formamide, with a hybridization temperature of 42° C.), and washing conditions of 60° C., in 0.5×SSC, 0.1% SDS. A stringent hybridization condition hybridizes in 6×SSC at 45° C., followed by one or more washes in 0.1×SSC, 0.2% SDS at 68° C. Furthermore, one of skill in the art can manipulate the hybridization and/or washing conditions to increase or decrease the stringency of hybridization such that nucleic acids comprising nucleotide sequences that are at least 65, 70, 75, 80, 85, 90, 95, 98 or 99% identical to each other typically remain hybridized to each other. The basic parameters affecting the choice of hybridization conditions and guidance for devising suitable conditions are set forth by, for example, Sambrook, Fritsch, and Maniatis (1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., chapters 9 and 11; and Current Protocols in Molecular Biology, 1995, Ausubel et al., eds., John Wiley & Sons, Inc., sections 2.10 and 6.3-6.4), and can be readily determined by those having ordinary skill in the art based on, for example, the length and/or base composition of the DNA. Changes can be introduced by mutation into a nucleic acid, thereby leading to changes in the amino acid sequence of a polypeptide (e.g., an antigen binding protein) that it encodes. Mutations can be introduced using any technique known in the art. In one embodiment, one or more particular amino acid residues are changed using, for example, a site-directed mutagenesis protocol. In another embodiment, one or more randomly selected residues is changed using, for example, a random mutagenesis protocol. However it is made, a mutant polypeptide can be expressed and screened for a desired property.

Mutations can be introduced into a nucleic acid without significantly altering the biological activity of a polypeptide that it encodes. For example, one can make nucleotide substitutions leading to amino acid substitutions at non-essential amino acid residues. In one embodiment, a nucleotide sequence provided herein for of the antibodies of the present invention, or a desired fragment, variant, or derivative thereof, is mutated such that it encodes an amino acid sequence comprising one or more deletions or substitutions of amino acid residues that are shown herein for the light chains of the antibodies of the present invention or the heavy chains of the antibodies of the present invention to be residues where two or more sequences differ. In another embodiment, the mutagenesis inserts an amino acid adjacent to one or more amino acid residues shown herein for the light chains of the antibodies of the present invention or the heavy chains of the antibodies of the present invention to be residues where two or more sequences differ. Alternatively, one or more mutations can be introduced into a nucleic acid that selectively change the biological activity of a polypeptide that it encodes.

In another embodiment, the present invention provides vectors comprising a nucleic acid encoding a polypeptide of the invention or a portion thereof. Examples of vectors include, but are not limited to, plasmids, viral vectors, non-episomal mammalian vectors and expression vectors, for example, recombinant expression vectors.

The recombinant expression vectors of the invention can comprise a nucleic acid of the invention in a form suitable for expression of the nucleic acid in a host cell. The recombinant expression vectors include one or more regulatory sequences, selected on the basis of the host cells to be used for expression, which is operably linked to the nucleic acid sequence to be expressed. Regulatory sequences include those that direct constitutive expression of a nucleotide sequence in many types of host cells (e.g., SV40 early gene enhancer, Rous sarcoma virus promoter and cytomegalovirus promoter), those that direct expression of the nucleotide sequence only in certain host cells (e.g., tissue-specific regulatory sequences, see Voss et al., 1986, Trends Biochem. Sci. 11:287, Maniatis et al., 1987, Science 236:1237, incorporated by reference herein in their entireties), and those that direct inducible expression of a nucleotide sequence in response to particular treatment or condition (e.g., the metallothionin promoter in mammalian cells and the tet-responsive and/or streptomycin responsive promoter in both prokaryotic and eukaryotic systems (see id.). It will be appreciated by those skilled in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expression of protein desired, etc. The expression vectors of the invention can be introduced into host cells to thereby produce proteins or peptides, including fusion proteins or peptides, encoded by nucleic acids as described herein.

In another embodiment, the present invention provides host cells into which a recombinant expression vector of the invention has been introduced. A host cell can be any prokaryotic cell or eukaryotic cell. Prokaryotic host cells include gram negative or gram positive organisms, for example E. coli or bacilli. Higher eukaryotic cells include insect cells, yeast cells, and established cell lines of mammalian origin. Examples of suitable mammalian host cell lines include Chinese hamster ovary (CHO) cells or their derivatives such as Veggie CHO and related cell lines which grow in serum-free media (see Rasmussen et al., 1998, Cytotechnology 28:31) or CHO strain DXB-11, which is deficient in DHFR (see Urlaub et al., 1980, Proc. Natl. Acad. Sci. USA 77:4216-20). Additional CHO cell lines include CHO-K1 (ATCC#CCL-61), EM9 (ATCC# CRL-1861), and UV20 (ATCC# CRL-1862). Additional host cells include the COS-7 line of monkey kidney cells (ATCC CRL 1651) (see Gluzman et al., 1981, Cell 23:175), L cells, C127 cells, 3T3 cells (ATCC CCL 163), AM-1/D cells (described in U.S. Pat. No. 6,210,924), HeLa cells, BHK (ATCC CRL 10) cell lines, the CV1/EBNA cell line derived from the African green monkey kidney cell line CV1 (ATCC CCL 70) (see McMahan et al., 1991, EMBO J. 10:2821), human embryonic kidney cells such as 293, 293 EBNA or MSR 293, human epidermal A431 cells, human Colo205 cells, other transformed primate cell lines, normal diploid cells, cell strains derived from in vitro culture of primary tissue, primary explants, HL-60, U937, HaK or Jurkat cells. Appropriate cloning and expression vectors for use with bacterial, fungal, yeast, and mammalian cellular hosts are described by Pouwels et al. (Cloning Vectors: A Laboratory Manual, Elsevier, New York, 1985).

Vector DNA can be introduced into prokaryotic or eukaryotic cells via conventional transformation or transfection techniques. For stable transfection of mammalian cells, it is known that, depending upon the expression vector and transfection technique used, only a small fraction of cells may integrate the foreign DNA into their genome. In order to identify and select these integrants, a gene that encodes a selectable marker (e.g., for resistance to antibiotics) is generally introduced into the host cells along with the gene of interest. Additional selectable markers include those which confer resistance to drugs, such as G418, hygromycin and methotrexate. Cells stably transfected with the introduced nucleic acid can be identified by drug selection (e.g., cells that have incorporated the selectable marker gene will survive, while the other cells die), among other methods.

The transformed cells can be cultured under conditions that promote expression of the polypeptide, and the polypeptide recovered by conventional protein purification procedures. Polypeptides contemplated for use herein include substantially homogeneous recombinant mammalian antibody polypeptides substantially free of contaminating endogenous materials.

Cells containing the nucleic acid encoding the antigen binding proteins of the present invention also include hybridomas. The production and culturing of hybridomas are discussed in the antibody section above.

In some emobodiments, a vector comprising a nucleic acid molecule as described herein is provided. In some embodiments, the invention comprises a host cell comprising a nucleic acid molecule as described herein.

In some emobodiments, a nucleic acid molecule encoding the antigen binding protein as described herein is provided.

In some emobodiments, a pharmaceutical composition comprising at least one antigen binding protein described herein is provided.

Antigen Binding Protein Production

The antigen binding proteins of the invention can be produced by any method known in the art for the synthesis of proteins (e.g., antibodies), in particular, by chemical synthesis or preferably, by recombinant expression techniques.

Recombinant expression of the antigen binding proteins requires construction of an expression vector containing a polynucleotide that encodes the antigen binding proteins. Once a polynucleotide encoding the antigen binding proteins molecule has been obtained, the vector for the production of the antigen binding proteins may be produced by recombinant DNA technology. An expression vector is constructed containing the antigen binding proteins coding sequences and appropriate transcriptional and translational control signals. These methods include, for example, in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination.

The expression vector is transferred to a host cell by conventional techniques and the transfected cells are then cultured by conventional techniques to produce an antigen binding proteins of the invention. In one embodiment of the invention, vectors encoding both the heavy and light chains of an antibody may be co-expressed in the host cell for expression of the entire immunoglobulin molecule, as detailed below.

A variety of host-expression vector systems may be utilized to express the antigen binding proteins of the invention. Such host-expression systems represent vehicles by which the coding sequences of interest may be produced and subsequently purified, but also represent cells which may, when transformed or transfected with the appropriate nucleotide coding sequences, express an antibody molecule of the invention in situ. Bacterial cells such as E. coli, and eukaryotic cells are commonly used for the expression of a recombinant antibody molecule, especially for the expression of whole recombinant antibody molecule. For example, mammalian cells such as Chinese hamster ovary cells (CHO), in conjunction with a vector such as the major intermediate early gene promoter element from human cytomegalovirus is an effective expression system for antibodies (Foecking et al., Gene 45:101 (1986); Cockett et al., Bio/Technology 8:2 (1990)).

In addition, a host cell strain may be chosen which modulates the expression of the inserted sequences, or modifies and processes the gene product in the specific fashion desired. Such modifications (e.g., glycosylation) and processing (e.g., cleavage) of protein products may be important for the function of the protein. Different host cells have characteristic and specific mechanisms for the post-translational processing and modification of proteins and gene products. Appropriate cell lines or host systems can be chosen to ensure the correct modification and processing of the foreign protein expressed. To this end, eukaryotic host cells which possess the cellular machinery for proper processing of the primary transcript, glycosylation, and phosphorylation of the gene product may be used. Such mammalian host cells include, but are not limited to, CHO, COS, 293, 3T3, or myeloma cells.

For long-term, high-yield production of recombinant proteins, stable expression is preferred. For example, cell lines which stably express the antibody molecule may be engineered. Rather than using expression vectors which contain viral origins of replication, host cells can be transformed with DNA controlled by appropriate expression control elements (e.g., promoter, enhancer, sequences, transcription terminators, polyadenylation sites, etc.), and a selectable marker. Following the introduction of the foreign DNA, engineered cells may be allowed to grow for 1-2 days in an enriched media, and then are switched to a selective media. The selectable marker in the recombinant plasmid confers resistance to the selection and allows cells to stably integrate the plasmid into their chromosomes and grow to form foci which in turn can be cloned and expanded into cell lines. This method may advantageously be used to engineer cell lines which express the antibody molecule. Such engineered cell lines may be particularly useful in screening and evaluation of compounds that interact directly or indirectly with the antibody molecule.

A number of selection systems may be used, including but not limited to the herpes simplex virus thymidine kinase (Wigler et al., Cell 11:223 (1977)), hypoxanthine-guanine phosphoribosyltransferase (Szybalska & Szybalski, Proc. Natl. Acad. Sci. USA 48:202 (1992)), and adenine phosphoribosyltransferase (Lowy et al., Cell 22:817 (1980)) genes can be employed in tk, hgprt or aprt-cells, respectively. Also, antimetabolite resistance can be used as the basis of selection for the following genes: dhfr, which confers resistance to methotrexate (Wigler et al., Proc. Natl. Acad. Sci. USA 77:357 (1980); O'Hare et al., Proc. Natl. Acad. Sci. USA 78:1527 (1981)); gpt, which confers resistance to mycophenolic acid (Mulligan & Berg, Proc. Natl. Acad. Sci. USA 78:2072 (1981)); neo, which confers resistance to the aminoglycoside G-418 (Wu and Wu, Biotherapy 3:87-95 (1991)); and hygro, which confers resistance to hygromycin (Santerre et al., Gene 30:147 (1984)). Methods commonly known in the art of recombinant DNA technology may be routinely applied to select the desired recombinant clone, and such methods are described, for example, in Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley & Sons, N Y (1993); Kriegler, Gene Transfer and Expression, A Laboratory Manual, Stockton Press, N Y (1990); and in Chapters 12 and 13, Dracopoli et al. (eds), Current Protocols in Human Genetics, John Wiley & Sons, N Y (1994); Colberre-Garapin et al., J. Mol. Biol. 150:1 (1981), which are incorporated by reference herein in their entireties.

The expression levels of an antibody molecule can be increased by vector amplification (for a review, see Bebbington and Hentschel, “The use of vectors based on gene amplification for the expression of cloned genes in mammalian cells” (DNA Cloning, Vol. 3. Academic Press, New York, 1987)). When a marker in the vector system expressing antibody is amplifiable, increase in the level of inhibitor present in culture of host cell will increase the number of copies of the marker gene. Since the amplified region is associated with the antibody gene, production of the antibody will also increase (Crouse et al., Mol. Cell. Biol. 3:257 (1983)).

The host cell may be co-transfected with two expression vectors of the invention, for example, the first vector encoding an antibody heavy chain derived polypeptide and the second vector encoding an antibody light chain derived polypeptide. The two vectors may contain identical selectable markers which enable equal expression of heavy and light chain polypeptides. Alternatively, a single vector may be used which encodes, and is capable of expressing, for example, both antibody heavy and light chain polypeptides. In such situations, the light chain should be placed before the heavy chain to avoid an excess of toxic free heavy chain (Proudfoot, Nature 322:52 (1986); Kohler, Proc. Natl. Acad. Sci. USA 77:2197 (1980)). The coding sequences for the heavy and light chains may comprise cDNA or genomic DNA.

Once an antibody molecule of the invention has been produced by an animal, chemically synthesized, or recombinantly expressed, it may be purified by any method known in the art for purification of an immunoglobulin molecule, for example, by chromatography (e.g., ion exchange, affinity, particularly by affinity for the specific antigen after Protein A, and size-exclusion chromatography), centrifugation, differential solubility, or by any other standard technique for the purification of proteins. In addition, the antibodies of the present invention or fragments thereof can be fused to heterologous polypeptide sequences described herein or otherwise known in the art, to facilitate purification.

In some embodiments, the present invention encompasses antibodies recombinantly fused or chemically conjugated (including both covalently and non-covalently conjugations) to a polypeptide. Fused or conjugated antibodies of the present invention may be used for ease in purification. See e.g., Harbor et al., supra, and PCT publication WO 93/21232; EP 439,095; Naramura et al., Immunol. Lett. 39:91-99 (1994); U.S. Pat. No. 5,474,981; Gillies et al., Proc. Natl. Acad. Sci. 89:1428-1432 (1992); Fell et al., J. Immunol. 146:2446-2452 (1991).

Moreover, the antibodies or fragments thereof of the present invention can be fused to marker sequences, such as a peptide to facilitate purification. In preferred embodiments, the marker amino acid sequence is a hexa-histidine peptide, such as the tag provided in a pQE vector (QIAGEN, Inc., 9259 Eton Avenue, Chatsworth, Calif., 91311), among others, many of which are commercially available. As described in Gentz et al., Proc. Natl. Acad. Sci. USA 86:821-824 (1989), for instance, hexa-histidine provides for convenient purification of the fusion protein. Other peptide tags useful for purification include, but are not limited to, the “HA” tag, which corresponds to an epitope derived from the influenza hemagglutinin protein (Wilson et al., Cell 37:767 (1984)) and the “flag” tag.

Antibody Effector Function

In some embodiments, the present invention provides antigen binding proteins (e.g., antibodies) with altered effector function (e.g., decreasing or increasing effector function). Nonlimiting examples of methods for increasing effector function can be found in U.S. Pat. Nos. 5,624,821, 6,602,684, 7,029,872, U.S. Patent Application Publication Nos. 2006/0067930A1, 2005/0272128A1, 2005/0079605A1, 2005/0123546A1, 2004/0072290A1, 2006/0257399A1, 2004/0261148A1, 2007/0092521, 2006/0040325A1, and 2006/0039904A1, and International Patent Application Publication Nos. WO 04/029207, WO03011878, WO05044859, WO 06071856, and WO 06071280.

Methods of engineering Fc regions of antibodies so as to alter effector functions are known in the art (e.g., U.S. Patent Publication No. 20040185045 and PCT Publication No. WO 2004/016750, both to Koenig et al., which describe altering the Fc region to enhance the binding affinity for Fc gamma RIIB as compared with the binding affinity for FC gamma RIIA; see, also, PCT Publication Nos. WO 99/58572 to Armour et al., WO 99/51642 to Idusogie et al., and U.S. Pat. No. 6,395,272 to Deo et al.). Methods of modifying the Fc region to decrease binding affinity to Fc gamma RIIB are also known in the art (e.g., U.S. Patent Publication No. 20010036459 and PCT Publication No. WO 01/79299, both to Ravetch et al.). Modified antibodies having variant Fc regions with enhanced binding affinity for Fc gamma RIIIA and/or Fc gamma RIIA as compared with a wildtype Fc region have also been described (e.g., PCT Publication Nos. WO 2004/063351, to Stavenhagen et al., the disclosure of which is incorporated herein in its entirety).

Antibody effector function may also be modified through the generation of antibodies with altered glycosylation patterns. Such altered glycosylation patterns have been demonstrated to increase or decrease the ADCC ability of antibodies, as desired. Such carbohydrate modifications can be accomplished by, for example, expressing the antibody in a host cell with altered glycosylation machinery. Cells with altered glycosylation machinery have been described in the art and can be used as host cells in which to express recombinant antibodies of the invention to thereby produce an antibody with altered glycosylation.

Half-Life Alteration

In some embodiments, the present invention provides for antigen binding proteins (e.g., antibodies) which have an extended half-life in vivo. In particular, the present invention provides antigen binding proteins which have a half-life in a mammal (for example, but not limited to, a human), of greater than 3 days, greater than 7 days, greater than 10 days, greater than 15 days, greater than 25 days, greater than 30 days, greater than 35 days, greater than 40 days, greater than 45 days, greater than 2 months, greater than 3 months, greater than 4 months, or greater than 5 months.

To prolong the serum circulation of antigen binding proteins (for example, monoclonal antibodies) or antibody fragments (for example, Fab fragments) in vivo, for example, inert polymer molecules such as high molecular weight polyethyleneglycol (PEG) can be attached to the antibodies (including antibody fragments thereof) with or without a multifunctional linker either through site-specific conjugation of the PEG to the N- or C-terminus of the antibodies or via epsilon-amino groups present on lysine residues. Linear or branched polymer derivatization that results in minimal loss of biological activity will be used. The degree of conjugation can be closely monitored by SDS-PAGE and mass spectrometry to ensure proper conjugation of PEG molecules to the antigen binding proteins. Unreacted PEG can be separated from antigen binding proteins-PEG conjugates by size-exclusion or by ion-exchange chromatography. PEG-derivatized antigen binding proteins can be tested for binding activity as well as for in vivo efficacy using methods known to those of skill in the art, for example, by immunoassays described herein.

In certain embodiments, antibodies having an increased half-life in vivo can also be generated by introducing one or more amino acid modifications (i.e., substitutions, insertions or deletions) into an IgG constant domain, or FcRn binding fragment thereof (e.g., Fc or hinge Fc domain fragment). See, e.g., International Publication No. WO 98/23289; International Publication No. WO 97/34631; and U.S. Pat. No. 6,277,375, each of which is incorporated herein by reference in its entirety.

Conjugates

In some embodiments, covalent modifications of the antigen binding proteins of the invention are included within the scope of this invention. They may be made by chemical synthesis or by enzymatic or chemical cleavage of the antigen binding proteins, if applicable. Other types of covalent modifications of the antigen binding proteins are introduced into the molecule by reacting targeted amino acid residues of the antibody with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C-terminal residues.

Cysteinyl residues most commonly are reacted with alpha-haloacetates (and corresponding amines), such as chloroacetic acid or chloroacetamide, to give carboxymethyl or carboxyamidomethyl derivatives. Similarly, iodo-reagents may also be used. Cysteinyl residues also are derivatized by reaction with bromotrifluoroacetone, alpha-bromo-beta-(5-imidozoyl)propionic acid, chloroacetyl phosphate, N-alkylmaleimides, 3-nitro-2-pyridyl disulfide, methyl 2-pyridyl disulfide, p-chloromercuribenzoate, 2-chloromercuri-4-nitrophenol, or chloro-7-nitrobenzo-2-oxa-1,3-diazole.

Histidyl residues are derivatized by reaction with diethylpyrocarbonate at pH 5.5-7.0 because this agent is relatively specific for the histidyl side chain. Para-bromophenacyl bromide also is useful; the reaction is preferably performed in 0.1 M sodium cacodylate at pH 6.0.

Lysyl and amino-terminal residues are reacted with succinic or other carboxylic acid anhydrides. Derivatization with these agents has the effect of reversing the charge of the lysinyl residues. Other suitable reagents for derivatizing .alpha.-amino-containing residues and/or e-amino-containing residues include imidoesters such as methyl picolinimidate, pyridoxal phosphate, pyridoxal, chloroborohydride, trinitrobenzenesulfonic acid, 0-methylisourea, 2,4-pentanedione, and transaminase-catalyzed reaction with glyoxylate.

Arginyl residues are modified by reaction with one or several conventional reagents, among them phenylglyoxal, 2,3-butanedione, 1,2-cyclohexanedione, and ninhydrin. Derivatization of arginyl residues generally requires that the reaction be performed in alkaline conditions because of the high pKa of the guanidine functional group. Furthermore, these reagents may react with the epsilon-amino groups of lysine as well as the arginine epsilon-amino group.

The specific modification of tyrosyl residues may be made, with particular interest in introducing spectral labels into tyrosyl residues by reaction with aromatic diazonium compounds or tetranitromethane. Most commonly, N-acetylimidizole and tetranitromethane are used to form O-acetyl tyrosyl species and 3-nitro derivatives, respectively. Tyrosyl residues are iodinated using I¹²⁵ or I¹³¹ to prepare labeled proteins for use in radioimmunoassay.

Carboxyl side groups (aspartyl or glutamyl) are selectively modified by reaction with carbodiimides (R—N══C══N—R′), where R and R′ are different alkyl groups, such as 1-cyclohexyl-3-(2-morpholinyl-4-ethyl)carbodiimide or 1-ethyl-3-(4-azonia-4,4-dimethylpentyl)carbodiimide. Furthermore, aspartyl and glutamyl residues are converted to asparaginyl and glutaminyl residues by reaction with ammonium ions.

Glutaminyl and asparaginyl residues are frequently deamidated to the corresponding glutamyl and aspartyl residues, respectively. These residues are deamidated under neutral or basic conditions. The deamidated form of these residues falls within the scope of this invention.

Other modifications include hydroxylation of proline and lysine, phosphorylation of hydroxyl groups of seryl or threonyl residues, methylation of the .alpha.-amino groups of lysine, arginine, and histidine side chains (T. E. Creighton, Proteins: Structure and Molecular Properties, W.H. Freeman & Co., San Francisco, pp. 79-86 (1983)), acetylation of the N-terminal amine, and amidation of any C-terminal carboxyl group.

Another type of covalent modification involves chemically or enzymatically coupling glycosides to the antibody. These procedures are advantageous in that they do not require production of the antibody in a host cell that has glycosylation capabilities for N- or O-linked glycosylation. Depending on the coupling mode used, the sugar(s) may be attached to (a) arginine and histidine, (b) free carboxyl groups, (c) free sulfhydryl groups such as those of cysteine, (d) free hydroxyl groups such as those of serine, threonine, or hydroxyproline, (e) aromatic residues such as those of phenylalanine, tyrosine, or tryptophan, or (f) the amide group of glutamine. These methods are described in WO 87/05330 published 11 Sep. 1987, and in Aplin and Wriston, CRC Crit. Rev. Biochem., pp. 259-306 (1981).

Interfering RNA

In some embodiments, the present invention provides polynucleotide compositions that target ASGR-1 and/or ASGR-2 and are useful for methods for treatment, therapy, and prophylaxis in disease related to ASGR, ASGR-1 and/or ASGR-2 expression, where reduction or inhibition of the expression or function of a selected target polynucleotide sequence is desired. Examples of polynucleotides that can be used to target ASGR-1 and/or ASGR-2 sequences and reduce ASGR-1 and/or ASGR-2 expression include, but are not limited to, antisense oligonucleotides, and RNA interference (RNAi) agents, including short or small interfering RNA (siRNA), short hairpin RNA (shRNA), and microRNA (miRNA). See, for example, U.S. Pat. Nos. 6,506,559; 8,394,628; 7,056,704; 7,078,196; 6,107,094; 5,898,031; 6,573,099; and European Patent No. 1,144,623. See also, for example, U.S. patent application publication nos. 2015/0259689; 2015/0197746; 2011/0092565; U.S. Pat. Nos. 8,877,917; 8,507,455; and 7,579,451.

In certain embodiments, a composition for inhibiting the function or expression of a target polynucleotide sequence (e.g. ASGR-1 mRNA sequence, ASGR-2 mRNA sequence) in a mammalian cell, according to this invention, comprises an agent that provides to a mammalian cell an at least partially double-stranded RNA molecule (e.g., an interfering RNA molecule). A double-stranded RNA molecule may include chemical modifications to ribonucleotides, including modifications to the ribose sugar, base, or backbone components of the ribonucleotides, such as those described herein or known in the art. Any such modifications, as used in a double-stranded RNA molecule (e.g. siRNA, shRNA, or the like), are encompassed by the term “double-stranded RNA” for the purposes of this disclosure. Thus, in general, the term “RNA” may also include RNA-DNA hybrids and polynucleotides comprising one or more modified nucleotides (e.g. nucleotides with modifications at the 2′ position of the ribose ring), except where specified otherwise, e.g., where a 2′-OH group of ribose is required for a particular linkage.

In some embodiments at least 10% of a partially double-stranded RNA molecule is double-stranded. Alternatively, the double stranded portion of these RNA molecules can be at least 30% of the length of the molecule. In another embodiment, the double stranded portion of these molecules can be at least 50% of the length of the molecule. In still another embodiment, the double stranded portion of these molecules can be at least 70% of the length of the molecule. In another embodiment, the double stranded portion of these molecules can be at least 90% of the length of the molecule. In another embodiment, the molecule can be double stranded over its entire length. Alternatively, the double-stranded portion of these molecules can occur at either or both termini, or in some middle portion of the molecule, if the molecule is linear. Similarly, the double-stranded portion can be in any location if the molecule is circular. In certain embodiments of the present invention, the double-stranded portion of the RNA molecule becomes double-stranded only when the molecule is in the mammalian cell. In still other embodiment of this invention, the partially double-stranded molecule is an RNA/DNA hybrid, for example, a single strand containing RNA and DNA, prepared in vitro; or a duplex of two such single strands or portions thereof. In yet another embodiment, the RNA molecule, made in vivo or in vitro, is a duplex comprised of an RNA single strand and a DNA single strand. In some embodiments, the partially double-stranded RNA molecule comprises a polynucleotide sequence that is substantially homologous to the target polynucleotide sequence in order to effectively reduce or inhibit the function or expression thereof. The necessary homology may be suitably defined by use of a computer algorithm. As known in the art and discussed herein, “homology” or “identity” means the degree of sequence relatedness between two polypeptide or two polynucleotide sequences as determined by the identity of the match between two lengths of such sequences. Both identity and homology can be readily calculated by methods in the prior art [See also, e.g., COMPUTATIONAL MOLECULAR BIOLOGY, Lesk, A. M., ed., Oxford University Press, New York, (1988); BIOCOMPUTING: INFORMATICS AND GENOME PROJECTS, Smith, D. W., ed., Academic Press, New York, (1993); COMPUTER ANALYSIS OF SEQUENCE DATA, PART I, Griffin, A. M., and Griffin, H. G., eds., Humana Press, New Jersey, (1994); SEQUENCE ANALYSIS IN MOLECULAR BIOLOGY, von Heinje, G., Academic Press, (1987); and SEQUENCE ANALYSIS PRIMER, Gribskov, M. and Devereux, J., eds., M Stockton Press, New York, (1991)]. While there exist a number of methods to measure identity and homology between two polynucleotide sequences, the terms “identity”, “similarity” and homology are well known to skilled artisans [H. Carillo and D. Lipton, SIAM J. Applied Math., 48:1073 (1988)]. Methods commonly employed to determine identity or homology between two sequences include, but are not limited to, those disclosed in Guide to Huge Computers, Martin J. Bishop, ed., Academic Press, San Diego, 1994, and H. Carillo and D. Lipton, SIAM J. Applied Math., 48:1073 (1988). Preferred methods to determine identity or homology are designed to give the largest match between the two sequences tested. Methods to determine identity and similarity are codified in computer programs. Preferred computer program to determine identity and homology between two sequences include, but are not limited to, the algorithm BESTFIT from the GCG program package [J. Devereux et al., Nucl. Acids Res., 12(1):387 (1984)], the related MACVECTOR program (Oxford), and the FASTA (Pearson) programs. For instance, searches for sequence similarities in databases between significant naturally occurring mammalian polynucleotide sequences and target polynucleotide sequences enable the design of suitable RNA molecules desired for use in the invention. The algorithm and/or the degree of homology necessary for any particular RNA molecule may be selected by one of skill in the art, depending on the identity of the target, and/or the closeness of homology of the target sequence to any naturally occurring mammalian sequence, which is desired to be left functioning normally after use of the methods of this invention.

In some embodiments, a polynucleotide composition for reducing the expression or function of ASGR-1 and/or ASGR-2 sequences is an RNAi agent comprising a double-stranded RNA molecule which comprises two antiparallel strands of contiguous nucleotides that are sufficiently complementary to each other to hybridize to form a duplex region. “Hybridize” or “hybridization” refers to the pairing of complementary polynucleotides, typically via hydrogen bonding (e.g. Watson-Crick, Hoogsteen or reversed Hoogsteen hydrogen bonding) between complementary bases in the two polynucleotides. The strand comprising a region having a sequence that is substantially complementary to a target sequence (e.g. target mRNA) is referred to as the “antisense strand.” The “sense strand” refers to the strand that includes a region that is substantially complementary to a region of the antisense strand. In some embodiments, the sense strand may comprise a region that has a sequence that is substantially identical to the target sequence.

As used herein, a first sequence is “complementary” to a second sequence if a polynucleotide comprising the first sequence can hybridize to a polynucleotide comprising the second sequence to form a duplex region under certain conditions, such as physiological conditions. Other such conditions can include moderate or stringent hybridization conditions, which are known to those of skill in the art. A first sequence is considered to be fully complementary (100% complementary) to a second sequence if a polynucleotide comprising the first sequence base pairs with a polynucleotide comprising the second sequence over the entire length of one or both nucleotide sequences without any mismatches. A sequence is “substantially complementary” to a target sequence if the sequence is at least about 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% complementary to a target sequence. Percent complementarity can be calculated by dividing the number of bases in a first sequence that are complementary to bases at corresponding positions in a second or target sequence by the total length of the first sequence. A sequence may also be said to be substantially complementary to another sequence if there are no more than 5, 4, 3, or 2 mismatches over a 30 base pair duplex region when the two sequences are hybridized. Generally, if any nucleotide overhangs, as defined herein, are present, the sequence of such overhangs is not considered in determining the degree of complementarity between two sequences. By way of example, a sense strand of 21 nucleotides in length and an antisense strand of 21 nucleotides in length that hybridize to form a 19 base pair duplex region with a 2 nucleotide overhang at the 3′ end of each strand would be considered to be fully complementary as the term is used herein.

In some embodiments, a region of the antisense strand comprises a sequence that is fully complementary to a region of the target RNA sequence (e.g. ASGR-1 and/or ASGR-2 mRNA). In such embodiments, the sense strand may comprise a sequence that is fully complementary to the sequence of the antisense strand. In other such embodiments, the sense strand may comprise a sequence that is substantially complementary to the sequence of the antisense strand, e.g. having 1, 2, 3, 4, or 5 mismatches in the duplex region formed by the sense and antisense strands. In certain embodiments, it is preferred that any mismatches occur within the terminal regions (e.g. within 6, 5, 4, 3, or 2 nucleotides of the 5′ and/or 3′ ends of the strands). In one embodiment, any mismatches in the duplex region formed from the sense and antisense strands occur within 6, 5, 4, 3, or 2 nucleotides of the 5′ end of the antisense strand.

In certain embodiments, the sense strand and antisense strand of the double-stranded RNA may be two separate molecules that hybridize to form a duplex region, but are otherwise unconnected. Such double-stranded RNA molecules formed from two separate strands are referred to as “small interfering RNAs” or “short interfering RNAs” (siRNAs).

In other embodiments, the sense strand and the antisense strand that hybridize to form a duplex region may be part of a single RNA molecule, i.e. the sense and antisense strands are part of a self-complementary region of a single RNA molecule. In such cases, a single RNA molecule comprises a duplex region (also referred to as a stem region) and a loop region. The 3′ end of the sense strand is connected to the 5′ end of the antisense strand by a contiguous sequence of unpaired nucleotides, which will form the loop region. The loop region is typically of a sufficient length to allow the RNA molecule to fold back on itself such that the antisense strand can base pair with the sense strand to form the duplex or stem region. The loop region can comprise from about 3 to about 25, from about 5 to about 15, or from about 8 to about 12 unpaired nucleotides. Such RNA molecules with at least partially self-complementary regions are referred to as “short hairpin RNAs” (shRNAs). The length of a single, at least partially self-complementary RNA molecule can be from about 35 nucleotides to about 100 nucleotides, from about 45 nucleotides to about 85 nucleotides, or from about 50 to about 60 nucleotides and comprise a duplex region and loop region each having the lengths recited herein.

In some embodiments, the double-stranded RNA molecule comprises a sense strand and an antisense strand, wherein the antisense strand comprises a region having a sequence that is substantially or fully complementary to an ASGR-1 messenger RNA (mRNA) sequence and/or ASGR-2 mRNA sequence. As used herein, an “ASGR-1 mRNA sequence” or “ASGR-2 mRNA sequence” refers to any messenger RNA sequence, including splice variants, encoding an ASGR-1 protein or ASGR-2 protein, including ASGR-1 or ASGR-2 protein variants or isoforms from any species (e.g. mouse, rat, non-human primate, human).

The sense strand of the double-stranded RNA molecule typically comprises a sequence that is sufficiently complementary to the sequence of the antisense strand such that the two strands hybridize under physiological conditions to form a duplex region. A “duplex region” refers to the region in two complementary or substantially complementary polynucleotides that form base pairs with one another, either by Watson-Crick base pairing or other hydrogen bonding interaction, to create a duplex between the two polynucleotides. The duplex region of the RNA molecule should be of sufficient length to allow the RNA molecule to enter the RNA interference pathway, e.g. by engaging the Dicer enzyme and/or the RISC complex. For instance, in some embodiments, the duplex region is about 15 to about 30 base pairs in length. Other lengths for the duplex region within this range are also suitable, such as about 15 to about 28 base pairs, about 15 to about 26 base pairs, about 15 to about 24 base pairs, about 15 to about 22 base pairs, about 17 to about 28 base pairs, about 17 to about 26 base pairs, about 17 to about 24 base pairs, about 17 to about 23 base pairs, about 17 to about 21 base pairs, about 19 to about 25 base pairs, about 19 to about 23 base pairs, or about 19 to about 21 base pairs. In one embodiment, the duplex region is about 17 to about 24 base pairs in length. In another embodiment, the duplex region is about 19 to about 21 base pairs in length.

For embodiments in which the sense strand and antisense strand are two separate molecules (e.g. RNAi agent is a siRNA), the sense strand and antisense strand need not be the same length as the length of the duplex region. For instance, one or both strands may be longer than the duplex region and have one or more unpaired nucleotides or mismatches flanking the duplex region. Thus, in some embodiments, the double-stranded RNA molecule comprises at least one nucleotide overhang. As used herein, a “nucleotide overhang” refers to the unpaired nucleotide or nucleotides that extend beyond the duplex region at the terminal ends of the strands. Nucleotide overhangs are typically created when the 3′ end of one strand extends beyond the 5′ end of the other strand or when the 5′ end of one strand extends beyond the 3′ end of the other strand. The length of a nucleotide overhang is generally between 1 and 6 nucleotides, 1 and 5 nucleotides, 1 and 4 nucleotides, 1 and 3 nucleotides, 2 and 6 nucleotides, 2 and 5 nucleotides, or 2 and 4 nucleotides. In some embodiments, the nucleotide overhang comprises 1, 2, 3, 4, 5, or 6 nucleotides. In one particular embodiment, the nucleotide overhang comprises 1 to 4 nucleotides. In certain embodiments, the nucleotide overhang comprises 2 nucleotides. The nucleotides in the overhang can be ribonucleotides, deoxyribonucleotides, or modified nucleotides as described herein.

The nucleotide overhang can be at the 5′ end or 3′ end of one or both strands. For example, in one embodiment, the double-stranded RNA molecule comprises a nucleotide overhang at the 5′ end and the 3′ end of the antisense strand. In another embodiment, the double-stranded RNA molecule comprises a nucleotide overhang at the 5′ end and the 3′ end of the sense strand. In some embodiments, the double-stranded RNA molecule comprises a nucleotide overhang at the 5′ end of the sense strand and the 5′ end of the antisense strand. In other embodiments, the double-stranded RNA molecule comprises a nucleotide overhang at the 3′ end of the sense strand and the 3′ end of the antisense strand.

The double-stranded RNA molecules may comprise a single nucleotide overhang at one end of the molecule and a blunt end at the other. A “blunt end” means that the sense strand and antisense strand are fully base-paired at the end of the molecule and there are no unpaired nucleotides that extend beyond the duplex region. In some embodiments, the double-stranded RNA molecule comprises a nucleotide overhang at the 3′ end of the sense strand and a blunt end at the 5′ end of the sense strand and 3′ end of the antisense strand. In other embodiments, the double-stranded RNA molecule comprises a nucleotide overhang at the 3′ end of the antisense strand and a blunt end at the 5′ end of the antisense strand and the 3′ end of the sense strand. In certain embodiments, the double-stranded RNA molecule comprises a blunt end at both ends of the double-stranded RNA molecule. In such embodiments, the sense strand and antisense strand have the same length and the duplex region is the same length as the sense and antisense strands (i.e. the molecule is double-stranded over its entire length).

The sense strand and antisense strand can each independently be about 15 to about 30 nucleotides in length, about 18 to about 28 nucleotides in length, about 19 to about 27 nucleotides in length, about 19 to about 25 nucleotides in length, about 19 to about 23 nucleotides in length, about 21 to about 25 nucleotides in length, or about 21 to about 23 nucleotides in length. In certain embodiments, the sense strand and antisense strand are each about 18, about 19, about 20, about 21, about 22, about 23, about 24, or about 25 nucleotides in length. In some embodiments, the sense strand and antisense strand have the same length but form a duplex region that is shorter than the strands such that the double-stranded RNA molecule has two nucleotide overhangs. For instance, in one embodiment, the double-stranded RNA molecule comprises (i) a sense strand and an antisense strand that are each 21 nucleotides in length, (ii) a duplex region that is 19 base pairs in length, and (iii) nucleotide overhangs of 2 unpaired nucleotides at both the 3′ end of the sense strand and the 3′ end of the antisense strand. In another embodiment, the double-stranded RNA molecule comprises (i) a sense strand and an antisense strand that are each 23 nucleotides in length, (ii) a duplex region that is 21 base pairs in length, and (iii) nucleotide overhangs of 2 unpaired nucleotides at both the 3′ end of the sense strand and the 3′ end of the antisense strand. In other embodiments, the sense strand and antisense strand have the same length and form a duplex region over their entire length such that there are no nucleotide overhangs on either end of the double-stranded molecule. In one such embodiment, the double-stranded RNA molecule is blunt ended and comprises (i) a sense strand and an antisense strand, each of which is 21 nucleotides in length, and (ii) a duplex region that is 21 base pairs in length. In another such embodiment, the double-stranded RNA molecule is blunt ended and comprises (i) a sense strand and an antisense strand, each of which is 23 nucleotides in length, and (ii) a duplex region that is 23 base pairs in length.

In other embodiments, the sense strand or the antisense strand is longer than the other strand and the two strands form a duplex region having a length equal to that of the shorter strand such that the double-stranded RNA molecule comprises at least one nucleotide overhang. For example, in one embodiment, the double-stranded RNA molecule comprises (i) a sense strand that is 19 nucleotides in length, (ii) an antisense strand that is 21 nucleotides in length, (iii) a duplex region of 19 base pairs in length, and (iv) a single nucleotide overhang of 2 unpaired nucleotides at the 3′ end of the antisense strand. In another embodiment, the double-stranded RNA molecule comprises (i) a sense strand that is 21 nucleotides in length, (ii) an antisense strand that is 23 nucleotides in length, (iii) a duplex region of 21 base pairs in length, and (iv) a single nucleotide overhang of 2 unpaired nucleotides at the 3′ end of the antisense strand.

Off-target toxicity is a constant concern in the development of pharmaceutical products. With interfering RNA agents, the potential exists for homology with certain endogenous polynucleotide sequences that could lead to unintended toxic effects in the patient receiving the interfering RNA. Accordingly, in some embodiments, the RNA molecule comprises a polynucleotide sequence that is also substantially non-homologous to any naturally occurring, normally functioning, and essential mammalian polynucleotide sequence, so that the RNA molecule does not adversely affect the function of any essential naturally occurring mammalian polynucleotide sequence, when used in the methods of this invention. Such naturally occurring functional mammalian polynucleotide sequences include mammalian sequences that encode desired proteins, as well as mammalian sequences that are non-coding, but that provide for essential regulatory sequences in a healthy mammal. Preferably, the RNA molecule useful in the methods of the invention must be sufficiently distinct in sequence from any mammalian polynucleotide sequence expressed in the target cells (e.g. liver cells) for which the function is intended to be undisturbed after any of the methods of this invention are performed. As described for determining the homology to the target sequence above, one of skill in the art may resort to the above-identified computer algorithms to define the essential lack of homology between the RNA molecule polynucleotide sequence and the normal mammalian sequences expressed in the target cells. For example, in a specific embodiment, the homology between the sequence of an RNAi agent and the selected normal sequence expressed in the target cells is less than the homologies of the formulae described above. In some embodiments, there is almost no homology at all between the sequence of an RNAi agent and any normal mammalian sequence.

The double-stranded RNA molecules used in the methods of the invention may comprise one or more modified nucleotides. A “modified nucleotide” refers to a nucleotide that has one or more chemical modifications to the nucleoside, nucleobase, pentose ring, or phosphate group. The double-stranded RNA molecules may comprise combinations of modified nucleotides, ribonucleotides, and deoxyribonucleotides. Incorporation of modified nucleotides into one or both strands of double-stranded RNA molecules can improve the in vivo stability of the RNA molecules, e.g., by reducing the molecules' susceptibility to nucleases and other degradation processes. The potency of double-stranded RNA molecules for reducing expression of the target gene can also be enhanced by incorporation of modified nucleotides.

In certain embodiments, the modified nucleotides have a modification of the ribose sugar. These sugar modifications can include modifications at the 2′ and/or 5′ position of the pentose ring. A 2′-modified nucleotide refers to a nucleotide having a pentose ring with a substituent at the 2′ position other than H or OH. Such 2′-modifications include, but are not limited to, 2′-O-alkyl (e.g. O—C₁-C₁₀ or O—C₁-C₁₀ substituted alkyl), 2′-O-allyl (O—CH₂CH═CH₂), 2′-C-allyl, 2′-fluoro, 2′-O-methyl (OCH₃), 2′-O-methoxyethyl (O—(CH₂)₂OCH₃), 2′-OCF₃, 2′-O(CH₂)₂SCH₃, 2′-O-aminoalkyl, 2′-amino (e.g. NH₂), 2′-O-ethylamine, and 2′-azido. Modifications at the 5′ position of the pentose ring include, but are not limited to, 5′-methyl (R or S); 5′-vinyl, and 5′-methoxy.

The double-stranded RNA molecules employed in the methods of the invention may also comprise one or more modified internucleotide linkages. As used herein, the term “modified internucleotide linkage” refers to an internucleotide linkage other than the natural 3′ to 5′ phosphodiester linkage. In some embodiments, the modified internucleotide linkage is a phosphorous-containing internucleotide linkage, such as a phosphotriester, aminoalkylphosphotriester, an alkylphosphonate (e.g. methylphosphonate, 3′-alkylene phosphonate), a phosphinate, a phosphoramidate (e.g. 3′-amino phosphoramidate and aminoalkylphosphoramidate), a phosphorothioate (P═S), a chiral phosphorothioate, a phosphorodithioate, a thionophosphoramidate, a thionoalkylphosphonate, a thionoalkylphosphotriester, and a boranophosphate. In one embodiment, a modified internucleotide linkage is a 2′ to 5′ phosphodiester linkage. In other embodiments, the modified internucleotide linkage is a non-phosphorous-containing internucleotide linkage and thus can be referred to as a modified internucleoside linkage. Such non-phosphorous-containing linkages include, but are not limited to, morpholino linkages (formed in part from the sugar portion of a nucleoside); siloxane linkages (—O—Si(H)₂—O—); sulfide, sulfoxide and sulfone linkages; formacetyl and thioformacetyl linkages; alkene containing backbones; sulfamate backbones; methylenemethylimino (—CH₂—N(CH₃)—O—CH₂—) and methylenehydrazino linkages; sulfonate and sulfonamide linkages; amide linkages; and others having mixed N, O, S and CH₂ component parts. In one embodiment, the modified internucleoside linkage is a peptide-based linkage (e.g. aminoethylglycine) to create a peptide nucleic acid or PNA, such as those described in U.S. Pat. Nos. 5,539,082; 5,714,331; and 5,719,262. Other suitable modified internucleotide and internucleoside linkages that may be employed in the double-stranded RNA molecules are described in U.S. Pat. No. 6,693,187, U.S. Pat. No. 9,181,551, U.S. Patent Publication No. 2016/0122761, and Deleavey and Damha, Chemistry and Biology, Vol. 19: 937-954, 2012, all of which are hereby incorporated by reference in their entireties.

Interfering RNA Delivery

The interfering RNA compounds can be administered by any method suitable for administration of nucleic acid agents, such as a DNA vaccine or gene therapy vectors. These methods include gene guns, bio injectors, and skin patches as well as needle-free methods such as the micro-particle DNA vaccine technology disclosed in U.S. Pat. No. 6,194,389, and the mammalian transdermal needle-free vaccination with powder-form vaccine as disclosed in U.S. Pat. No. 6,168,587. Additionally, intranasal delivery is possible, as described in, inter alia, Hamajima et al. (1998), Clin. Immunol. Immunopathol., 88(2), 205-10. Liposomes (e.g., as described in U.S. Pat. No. 6,472,375) and microencapsulation can also be used. Biodegradable targetable microparticle delivery systems can also be used (e.g., as described in U.S. Pat. No. 6,471,996).

In one embodiment, the active compounds are prepared with carriers that will protect the compound against rapid elimination from the body, such as a controlled release formulation, including implants and microencapsulated delivery systems. Biodegradable, biocompatible polymers can be used, such as ethylene vinyl acetate, polyanhydrides, polyglycolic acid, collagen, polyorthoesters, and polylactic acid. Such formulations can be prepared using standard techniques. The materials can also be obtained commercially from, for example, Alza Corporation and Nova Pharmaceuticals, Inc. Liposomal suspensions can also be used as pharmaceutically acceptable carriers. These can be prepared according to methods known to those skilled in the art, for example, as described in U.S. Pat. No. 4,522,811.

The interfering RNA molecule may be conjugated to one or more carbohydrate moieties to optimize one or more properties of the interfering RNA molecule. In many cases, the carbohydrate moiety will be attached to a modified subunit of the interfering RNA molecule or at the 5′ or 3′ end of one of strands of the interfering RNA molecule. E.g., the ribose sugar of one or more ribonucleotide subunits of an interfering RNA molecule can be replaced with another moiety, e.g., a non-carbohydrate (preferably cyclic) carrier to which is attached a carbohydrate moiety. A cyclic carrier may be a carbocyclic ring system, i.e., all ring atoms are carbon atoms, or a heterocyclic ring system, i.e., one or more ring atoms may be a heteroatom, e.g., nitrogen, oxygen, sulfur. The cyclic carrier may be a monocyclic ring system, or may contain two or more rings, e.g. fused rings. The cyclic carrier may be a fully saturated ring system, or it may contain one or more double bonds.

The carbohydrate moiety may be attached to the polynucleotide via a carrier. The carriers include (i) at least one “backbone attachment point,” preferably two “backbone attachment points” and (ii) at least one “tethering attachment point.” A “backbone attachment point” as used herein refers to a functional group, e.g. a hydroxyl group, or generally, a bond available for, and that is suitable for incorporation of the carrier into the backbone, e.g., the phosphate, or modified phosphate, e.g., sulfur containing, backbone, of a ribonucleic acid. A “tethering attachment point” (TAP) in some embodiments refers to a constituent ring atom of the cyclic carrier, e.g., a carbon atom or a heteroatom (distinct from an atom which provides a backbone attachment point), that connects a selected moiety. The moiety can be, e.g., a carbohydrate, e.g. monosaccharide, disaccharide, trisaccharide, tetrasaccharide, oligosaccharide and polysaccharide. Optionally, the selected moiety is connected by an intervening tether to the cyclic carrier. Thus, the cyclic carrier will often include a functional group, e.g., an amino group, or generally, provide a bond, that is suitable for incorporation or tethering of another chemical entity, e.g., a ligand to the constituent ring.

In some embodiments the interfering RNA molecule of the invention is conjugated to a carbohydrate moiety via a carrier, wherein the carrier can be cyclic group or acyclic group; in specific embodiments, the cyclic group is selected from pyrrolidinyl, pyrazolinyl, pyrazolidinyl, imidazolinyl, imidazolidinyl, piperidinyl, piperazinyl, [1,3]dioxolane, oxazolidinyl, isoxazolidinyl, morpholinyl, thiazolidinyl, isothiazolidinyl, quinoxalinyl, pyridazinonyl, tetrahydrofuryl and decalin; preferably, the acyclic group is selected from serinol backbone or diethanolamine backbone.

Targeting the Interfering RNA

Given that ASGR, ASGR-1 and/or ASGR-2 is expressed on the surface of liver cells (e.g. hepatocytes), in certain embodiments, it is desirable to deliver the interfering RNA molecules to those liver cells so that the interfering effect can be exerted specifically within liver cells. Accordingly, in certain embodiments, the interfering RNA molecules are specifically targeted to liver cells using various methodologies known in the art and described herein. For example, in certain embodiments, antigen binding proteins (e.g. antibodies) or other targeting moieties disclosed herein below can be used to specifically target the interfering RNA molecules to the hepatocytes using various different receptors expressed on the surface of hepatocytes. In certain embodiments, the interfering RNA molecules are targeted to liver cells using the surface expressed ASGR, ASGR-1 and/or ASGR-2. In these embodiments, it is envisioned that this can result in a self-regulating system that reduces the amount of RNAi agent delivered to the liver cells as expression of ASGR, ASGR-1, and/or ASGR-2 is reduced due to the effect of the targeted interfering RNA.

A wide variety of targeting moieties can be coupled to the oligonucleotides of the present invention. In some embodiments, the targeting moieties are coupled, e.g., covalently, either directly or indirectly via an intervening tether.

In some embodiments, a targeting moiety alters the distribution, targeting or lifetime of the molecule into which it is incorporated. In preferred embodiments a targeting moiety provides an enhanced affinity for a selected target, e.g., molecule, cell or cell type, compartment, receptor e.g., a cellular or organ compartment, tissue, organ or region of the body, as, e.g., compared to a species absent such a targeting moiety. Targeting moieties providing enhanced affinity for a selected target are also termed targeting moieties.

Some targeting moieties can have endosomolytic properties. The endosomolytic targeting moieties promote the lysis of the endosome and/or transport of the composition of the invention, or its components, from the endosome to the cytoplasm of the cell. The endosomolytic targeting moietymay be a polyanionic peptide or peptidomimetic which shows pH-dependent membrane activity and fusogenicity. In one embodiment, the endosomolytic targeting moiety assumes its active conformation at endosomal pH. The “active” conformation is that conformation in which the endosomolytic targeting moietypromotes lysis of the endosome and/or transport of the composition of the invention, or its components, from the endosome to the cytoplasm of the cell. Exemplary endosomolytic targeting moietiesinclude the GALA peptide (Subbarao et al., Biochemistry, 1987, 26: 2964-2972), the EALA peptide (Vogel et al., J. Am. Chem. Soc., 1996, 118: 1581-1586), and their derivatives (Turk et al., Biochem. Biophys. Acta, 2002, 1559: 56-68). In one embodiment, the endosomolytic component may contain a chemical group (e.g., an amino acid) which will undergo a change in charge or protonation in response to a change in pH. The endosomolytic component may be linear or branched.

In certain embodiments, targeting moieties can improve transport, hybridization, and specificity properties and may also improve nuclease resistance of the resultant natural or modified oligoribonucleotide, or a polymeric molecule comprising any combination of monomers described herein and/or natural or modified ribonucleotides.

In some embodiments, targeting moieties in general can include therapeutic modifiers, e.g., for enhancing uptake; diagnostic compounds or reporter groups e.g., for monitoring distribution; cross-linking agents; and nuclease-resistance conferring moieties. General examples include lipids, steroids, vitamins, sugars, proteins, peptides, polyamines, and peptide mimics.

Targeting moieties can include a naturally occurring substance, such as a protein (e.g., human serum albumin (I), low-density lipoprotein (LDL), high-density lipoprotein (HDL), or globulin); a carbohydrate (e.g., a dextran, pullulan, chitin, chitosan, inulin, cyclodextrin or hyaluronic acid); or a lipid. The targeting moiety may also be a recombinant or synthetic molecule, such as a synthetic polymer, e.g., a synthetic polyamino acid, an oligonucleotide (e.g. an aptamer). Examples of polyamino acids include polyamino acid is a polylysine (PLL), poly L-aspartic acid, poly L-glutamic acid, styrene-maleic acid anhydride copolymer, poly(L-lactide-co-glycolied) copolymer, divinyl ether-maleic anhydride copolymer, N-(2-hydroxypropyl)methacrylamide copolymer (HMPA), polyethylene glycol (PEG), polyvinyl alcohol (PVA), polyurethane, poly(2-ethylacryllic acid), N-isopropylacrylamide polymers, or polyphosphazine. Example of polyamines include: polyethylenimine, polylysine (PLL), spermine, spermidine, polyamine, pseudopeptide-polyamine, peptidomimetic polyamine, dendrimer polyamine, arginine, amidine, protamine, cationic lipid, cationic porphyrin, quaternary salt of a polyamine, or an alpha helical peptide.

Targeting moieties can also include other targeting groups, e.g., a cell or tissue targeting agent, e.g., a lectin, glycoprotein, lipid or protein, e.g., an antibody, that binds to a specified cell type such as a kidney cell. A targeting group can be a thyrotropin, melanotropin, lectin, glycoprotein, surfactant protein A, Mucin carbohydrate, multivalent lactose, multivalent galactose, N-acetyl-galactosamine, N-acetyl-gulucosamine multivalent mannose, multivalent fucose, glycosylated polyaminoacids, multivalent galactose, transferrin, bisphosphonate, polyglutamate, polyaspartate, a lipid, cholesterol, a steroid, bile acid, folate, vitamin B12, biotin, an RGD peptide, an RGD peptide mimetic or an aptamer.

Other examples of targeting moieties include dyes, intercalating agents (e.g. acridines), cross-linkers (e.g. psoralene, mitomycin C), porphyrins (TPPC4, texaphyrin, Sapphyrin), polycyclic aromatic hydrocarbons (e.g., phenazine, dihydrophenazine), artificial endonucleases or a chelator (e.g. EDTA), lipophilic molecules, e.g, cholesterol, cholic acid, 206 ligonucle acetic acid, 1-pyrene butyric acid, dihydrotestosterone, 1,3-Bis-O(hexadecyl)glycerol, geranyloxyhexyl group, hexadecylglycerol, borneol, menthol, 1,3-propanediol, heptadecyl group, palmitic acid, myristic acid, O3-(oleoyl)lithocholic acid, O3-(oleoyl)cholenic acid, dimethoxytrityl, or phenoxazine) and peptide conjugates (e.g., antennapedia peptide, Tat peptide), alkylating agents, phosphate, amino, mercapto, PEG (e.g., PEG-40K), MPEG, [MPEG]₂, polyamino, alkyl, substituted alkyl, radiolabeled markers, enzymes, haptens (e.g. biotin), transport/absorption facilitators (e.g., aspirin, vitamin E, folic acid), synthetic ribonucleases (e.g., imidazole, bisimidazole, histamine, imidazole clusters, acridine-imidazole conjugates, Eu3+ complexes of tetraazamacrocycles), dinitrophenyl, HRP, or AP.

Targeting moieties can be proteins, e.g., glycoproteins, or peptides, e.g., molecules having a specific affinity for a co-moiety, or antigen binding proteins, such as antibodies; e.g., an antibody, that binds to a specified cell type such as a liver hepatocyte. Targeting moieties may also include hormones and hormone receptors. They can also include non-peptidic species, such as lipids, lectins, carbohydrates, vitamins, cofactors, multivalent lactose, multivalent galactose, N-acetyl-galactosamine, N-acetyl-gulucosamine multivalent mannose, multivalent fucose, or aptamers. The targeting moiety can be, for example, a lipopolysaccharide.

The targeting moiety can be a substance, e.g, a drug, which can increase the uptake of the interfering RNA molecule into the cell, for example, by disrupting the cell's cytoskeleton, e.g., by disrupting the cell's microtubules, microfilaments, and/or intermediate filaments. The drug can be, for example, taxon, vincristine, vinblastine, cytochalasin, nocodazole, japlakinolide, latrunculin A, phalloidin, swinholide A, indanocine, or myoservin.

The targeting moiety can increase the uptake of the interfering RNA molecule into the cell by activating an inflammatory response, for example. Exemplary targeting moieties that would have such an effect include tumor necrosis factor alpha (TNFalpha), interleukin-1 beta, or gamma interferon.

In one embodiment, the targeting moiety is a lipid or lipid-based molecule. Such a lipid or lipid-based molecule preferably binds a serum protein, e.g., human serum albumin (I). A serum protein binding targeting moiety, in certain embodiments, allows for distribution of the conjugate to a target tissue, e.g., a non-kidney target tissue of the body. For example, the target tissue can be the liver, including hepatocytes or parenchymal cells of the liver. Other molecules that can bind serum proteins can also be used as targeting moieties. For example, naproxen or aspirin can be used. A lipid or lipid-based targeting moiety can (a) increase resistance to degradation of the conjugate, (b) increase targeting or transport into a target cell or cell membrane, and/or (c) can be used to adjust binding to a serum protein.

A lipid based targeting moiety can be used to modulate, e.g., control the binding of the conjugate to a target tissue. For example, a lipid or lipid-based targeting moiety that binds to a serum protein more strongly will be less likely to be targeted to the kidney and therefore less likely to be cleared from the body. A lipid or lipid-based targeting moiety that binds to a serum protein less strongly can be used to target the conjugate to the kidney, if so desired.

In one embodiment, the lipid based targeting moiety binds human serum albumin. In a specific embodiment, it binds human serum albumin with a sufficient affinity such that the conjugate will be preferably distributed to a non-kidney tissue. In certain embodiments, it is preferred that the affinity not be so strong that the human serum albumin targeting moiety binding cannot be reversed.

In another preferred embodiment, the lipid based targeting moiety binds human serum albumin weakly or not at all, such that the conjugate will be preferably distributed to the kidney. Other moieties that target to kidney cells can also be used in place of or in addition to the lipid-based targeting moiety.

In another embodiment, the targeting moiety is for example a vitamin, e.g., a vitamin, which is taken up by a target cell, e.g., a proliferating cell. Exemplary vitamins include vitamin A, E, and K. Other exemplary vitamins include B vitamins, e.g., folic acid, B12, riboflavin, biotin, pyridoxal or other vitamins or nutrients taken up by cells. Also included are low density lipoprotein (LDL) and high-density lipoprotein (HDL).

In another embodiment, the targeting moiety is a cell-permeation agent, preferably a helical cell-permeation agent. In some embodiments, the agent is amphipathic. An exemplary agent is a peptide such as tat or antennopedia. If the agent is a peptide, it can be modified, including a peptidylmimetic, invertomers, non-peptide or pseudo-peptide linkages, and use of D-amino acids. The helical agent is preferably an alpha-helical agent, which preferably has a lipophilic and a lipophobic phase.

The targeting moiety can be a peptide or peptidomimetic. A peptidomimetic (also referred to herein as an oligopeptidomimetic) is a molecule capable of folding into a defined three-dimensional structure similar to a natural peptide. The peptide or peptidomimetic moiety can be about 5-50 amino acids long, e.g., about 5, 10, 15, 20, 25, 30, 35, 40, 45, or 50 amino acids long. A peptide or peptidomimetic can be, for example, a cell permeation peptide, cationic peptide, amphipathic peptide, or hydrophobic peptide (e.g., consisting primarily of Tyr, Trp or Phe). The peptide moiety can be a dendrimer peptide, constrained peptide or crosslinked peptide. In another alternative, the peptide moiety can include a hydrophobic membrane translocation sequence (MTS). An exemplary hydrophobic MTS-containing peptide is RFGF having the amino acid sequence AAVALLPAVLLALLAP. An RFGF analogue (e.g., amino acid sequence AALLPVLLAAP) containing a hydrophobic MTS can also be a targeting moiety. The peptide moiety can be a “delivery” peptide, which can carry large polar molecules including peptides, oligonucleotides, and protein across cell membranes. For example, sequences from the HIV Tat protein (GRKKRRQRRRPPQ) and the Drosophila Antennapedia protein (RQIKIWFQNRRMKWKK) have been found to be capable of functioning as delivery peptides. A peptide or peptidomimetic can be encoded by a random sequence of DNA, such as a peptide identified from a phage-display library, or one-bead-one-compound (OBOC) combinatorial library (Lam et al., Nature, 354:82-84, 1991). In some embodiments, the peptide or peptidomimetic tethered to an interfering RNA molecule via an incorporated monomer unit is a cell targeting peptide such as an arginine-glycine-aspartic acid (RGD)-peptide, or RGD mimic. A peptide moiety can range in length from about 5 amino acids to about 40 amino acids. The peptide moieties can have a structural modification, such as to increase stability or direct conformational properties. Any of the structural modifications described below can be utilized. An RGD peptide can facilitate targeting of an interfering RNA molecule to cells of a variety of other tissues, including the lung, kidney, spleen, or liver (Aoki et al., Cancer Gene Therapy 8:783-787, 2001). The RGD peptide can be linear or cyclic, and can be modified, e.g., glycosylated or methylated to facilitate targeting to specific tissues. For example, a glycosylated RGD peptide can deliver an interfering RNA molecule to a cell expressing αVβ₃ (Haubner et al., Jour. Nucl. Med., 42:326-336, 2001). Peptides that target markers enriched in proliferating cells can be used. E.g., RGD containing peptides and peptidomimetics can target cells, in particular cells that exhibit an integrin. Thus, one could use RGD peptides, cyclic peptides containing RGD, RGD peptides that include D-amino acids, as well as synthetic RGD mimics. In addition to RGD, one can use other moieties that target the integrin ligand.

A “cell permeation peptide” is capable of permeating a cell, e.g., a microbial cell, such as a bacterial or fungal cell, or a mammalian cell, such as a human cell. A microbial cell-permeating peptide can be, for example, an α-helical linear peptide (e.g., LL-37 or Ceropin P1), a disulfide bond-containing peptide (e.g., α-defensin, β-defensin or bactenecin), or a peptide containing only one or two dominating amino acids (e.g., PR-39 or indolicidin). A cell permeation peptide can also include a nuclear localization signal (NLS). For example, a cell permeation peptide can be a bipartite amphipathic peptide, such as MPG, which is derived from the fusion peptide domain of HIV-1 gp41 and the NLS of SV40 large T antigen (Simeoni et al., Nucl. Acids Res. 31:2717-2724, 2003).

In one embodiment, a targeting peptide can be an amphipathic α-helical peptide. Exemplary amphipathic α-helical peptides include, but are not limited to, cecropins, lycotoxins, paradaxins, buforin, CPF, bombinin-like peptide (BLP), cathelicidins, ceratotoxins, S. clava peptides, hagfish intestinal antimicrobial peptides (HFIAPs), magainines, brevinins-2, dermaseptins, melittins, pleurocidin, H.sub. 2A peptides, Xenopus peptides, esculentinis-1, and caerins.

Peptide and peptidomimetic targeting moietiesinclude those having naturally occurring or modified peptides, e.g., D or L peptides; α, β, or γ peptides; N-methyl peptides; azapeptides; peptides having one or more amide, i.e., peptide, linkages replaced with one or more urea, thiourea, carbamate, or sulfonyl urea linkages; or cyclic peptides.

The targeting moiety can be any moiety that is capable of targeting a specific receptor. Examples are: folate, GalNAc, galactose, mannose, mannose-6P, clusters of sugars such as GalNAc cluster, mannose cluster, galactose cluster, or an apatamer. A cluster is a combination of two or more sugar units. The targeting moieties also include integrin receptor moieties, chemokine receptor moieties, transferrin, biotin, serotonin receptor moieties, PSMA, endothelin, GCPII, somatostatin, LDL and HDL moieties. The targeting moieties can also be based on nucleic acid, e.g., an aptamer. The aptamer can be unmodified or have any combination of modifications disclosed herein.

Other exemplary endosomal release agents include imidazoles, poly or oligoimidazoles, PEIs, peptides, fusogenic peptides, polycaboxylates, polyacations, masked oligo or poly cations or anions, acetals, polyacetals, ketals/polyketyals, orthoesters, polymers with masked or unmasked cationic or anionic charges, dendrimers with masked or unmasked cationic or anionic charges.

Pharmacokinetic (“PK”) modulators include lipophiles, bile acids, steroids, phospholipid analogues, peptides, protein binding agents, PEG, vitamins etc. Examplary PK modulators include, but are not limited to, cholesterol, fatty acids, cholic acid, lithocholic acid, dialkylglycerides, diacylglyceride, phospholipids, sphingolipids, naproxen, ibuprofen, vitamin E, biotin etc. Oligonucleotides that comprise a number of phosphorothioate linkages are also known to bind to serum protein, thus short oligonucleotides, e.g. oligonucleotides of about 5 bases, 10 bases, 15 bases or 20 bases, comprising multiple of phosphorothioate linkages in the backbaone are also amenable to the present invention as targeting moieties (e.g. as PK modulating moieties). In addition, aptamers that bind serum components (e.g. serum proteins) are also amenable to the present invention as PK modulating moieties.

When two or more targeting moieties are present, the targeting moieties can all have same properties, all have different properties or some targeting moieties have the same properties while others have different properties. For example, a targeting moiety can have targeting properties, have endosomolytic activity and/or have PK modulating properties. In certain embodiments, all the have different properties.

In some embodiments, a targeting moiety can be conjugated to nucleobases, sugar moieties, or internucleosidic linkages of nucleic acid molecules. Conjugation to purine nucleobases or derivatives thereof can occur at any position including, endocyclic and exocyclic atoms. In some embodiments, the 2-, 6-, 7-, or 8-positions of a purine nucleobase are attached to a conjugate moiety. Conjugation to pyrimidine nucleobases or derivatives thereof can also occur at any position. In some embodiments, the 2-, 5-, and 6-positions of a pyrimidine nucleobase can be substituted with a conjugate moiety. Conjugation to sugar moieties of nucleosides can occur at any carbon atom. Example carbon atoms of a sugar moiety that can be attached to a conjugate moiety include the 2′, 3′, and 5′ carbon atoms. The 1′ position can also be attached to a conjugate moiety, such as in an abasic residue. Internucleosidic linkages can also bear conjugate moieties. For phosphorus-containing linkages (e.g., phosphodiester, phosphorothioate, phosphorodithiotate, phosphoroamidate, and the like), the conjugate moiety can be attached directly to the phosphorus atom or to an O, N, or S atom bound to the phosphorus atom. For amine- or amide-containing internucleosidic linkages (e.g., PNA), the conjugate moiety can be attached to the nitrogen atom of the amine or amide or to an adjacent carbon atom.

It is envisioned that any suitable targeting moiety in the field of RNA interference may be used, although the targeting moiety is typically a carbohydrate e.g. monosaccharide (such as GalNAc), disaccharide, trisaccharide, tetrasaccharide, polysaccharide. Linkers that conjugate the targeting moiety to the nucleic acid include those discussed herein. For example, the targeting moiety can be one or more GalNAc derivatives attached through a bivalent or trivalent branched linker.

In certain embodiments, cleavable linking groups are utilized. A cleavable linking group is one which is sufficiently stable outside the cell, but which upon entry into a target cell is cleaved to release the two parts the linker is holding together. In one embodiment, the cleavable linking group is cleaved at least 10 times or more, and in some embodiments, at least 100 times faster in the target cell or under a first reference condition (which can, e.g., be selected to mimic or represent intracellular conditions) than in the blood of a subject, or under a second reference condition (which can, e.g., be selected to mimic or represent conditions found in the blood or serum).

Cleavable linking groups are susceptible to cleavage agents, e.g., pH, redox potential or the presence of degradative molecules. Generally, cleavage agents are more prevalent or found at higher levels or activities inside cells than in serum or blood. Examples of such degradative agents include: redox agents which are selected for particular substrates or which have no substrate specificity, including, e.g., oxidative or reductive enzymes or reductive agents such as mercaptans, present in cells, that can degrade a redox cleavable linking group by reduction; esterases; endosomes or agents that can create an acidic environment, e.g., those that result in a pH of five or lower; enzymes that can hydrolyze or degrade an acid cleavable linking group by acting as a general acid, peptidases (which can be substrate specific), and phosphatases.

A cleavable linkage group, such as a disulfide bond can be susceptible to pH. The pH of human serum is 7.4, while the average intracellular pH is slightly lower, ranging from about 7.1-7.3. Endosomes have a more acidic pH, in the range of 5.5-6.0, and lysosomes have an even more acidic pH at around 5.0. Some linkers will have a cleavable linking group that is cleaved at a preferred pH, thereby releasing the cationic lipid from the moiety inside the cell, or into the desired compartment of the cell.

A linker can include a cleavable linking group that is cleavable by a particular enzyme. The type of cleavable linking group incorporated into a linker can depend on the cell to be targeted. For example, liver targeting targeting moieties can be linked to the cationic lipids through a linker that includes an ester group. Liver cells are rich in esterases, and therefore the linker will be cleaved more efficiently in liver cells than in cell types that are not esterase-rich. Other cell-types rich in esterases include cells of the lung, renal cortex, and testis. Linkers that contain peptide bonds can be used when targeting cell types rich in peptidases, such as liver cells and synoviocytes.

In general, the suitability of a candidate cleavable linking group can be evaluated by testing the ability of a degradative agent (or condition) to cleave the candidate linking group. It will also be desirable to also test the candidate cleavable linking group for the ability to resist cleavage in the blood or when in contact with other non-target tissue. Thus one can determine the relative susceptibility to cleavage between a first and a second condition, where the first is selected to be indicative of cleavage in a target cell and the second is selected to be indicative of cleavage in other tissues or biological fluids, e.g., blood or serum. The evaluations can be carried out in cell free systems, in cells, in cell culture, in organ or tissue culture, or in whole animals. It may be useful to make initial evaluations in cell-free or culture conditions and to confirm by further evaluations in whole animals. In some embodiments, useful candidate compounds are cleaved at least 2, 4, 10 or 100 times faster in the cell (or under in vitro conditions selected to mimic intracellular conditions) as compared to blood or serum (or under in vitro conditions selected to mimic extracellular conditions).

In some embodiments, redox cleavable linking groups are utilized. Redox cleavable linking groups are cleaved upon reduction or oxidation. An example of reductively cleavable linking group is a disulphide linking group (—S—S—). To determine if a candidate cleavable linking group is a suitable “reductively cleavable linking group,” or for example is suitable for use with a particular interfering RNA molecule and particular targeting agent one can look to methods described herein. For example, a candidate can be evaluated by incubation with dithiothreitol (DTT), or other reducing agent using reagents know in the art, which mimic the rate of cleavage which would be observed in a cell, e.g., a target cell. The candidates can also be evaluated under conditions which are selected to mimic blood or serum conditions. In a specific embodiment, candidate compounds are cleaved by at most 10% in the blood. In some embodiments, useful candidate compounds are degraded at least 2, 4, 10 or 100 times faster in the cell (or under in vitro conditions selected to mimic intracellular conditions) as compared to blood (or under in vitro conditions selected to mimic extracellular conditions). The rate of cleavage of candidate compounds can be determined using standard enzyme kinetics assays under conditions chosen to mimic intracellular media and compared to conditions chosen to mimic extracellular media.

In yet some embodiments, phosphate-based cleavable linking groups are cleaved by agents that degrade or hydrolyze the phosphate group. An example of an agent that cleaves phosphate groups in cells are enzymes such as phosphatases in cells. Examples of phosphate-based linking groups are —O—P(O)(Ork)-O—, —O—P(S)(Ork)-O—, —O—P(S)(SRk)-O—, —S—P(O) (Ork)-O—, —O—P(O)(Ork)-S—, —S—P(O)(Ork)-S—, —O—P(S)(Ork)-S—, —S—P(S)(Ork)-O—, —O—P(O)(Rk)-O—, —O—P(S)(Rk)-O—, —S—P(O)(Rk)-O—, —S—P(S)(Rk)-O—, —S—P(O)(Rk)-S—, —O—P(S)(Rk)-S—. Specific embodiments include —O—P(O)(OH)—O—, —O—P(S)(OH)—O—, —O—P(S)(SH)—O—, —S—P(O)(OH)—O—, —O—P(O)(OH)—S—, —S—P(O)(OH)—S—, —O—P(S)(OH)—S—, —S—P(S)(OH)—O—, —O—P(O)(H)—O—, —O—P(S)(H)—O—, —S—P(O)(H)—O—, —S—P(S)(H)—O—, —S—P(O)(H)—S—, —O—P(S)(H)—S—. Another specific embodiment is —O—P(O)(OH)—O—. These candidates can be evaluated using methods analogous to those described above.

In some embodiments, acid cleavable linking groups, which are linking groups that are cleaved under acidic conditions, are envisioned. In some embodiments acid cleavable linking groups are cleaved in an acidic environment with a pH of about 6.5 or lower (e.g., about 6.0, 5.5, 5.0, or lower), or by agents such as enzymes that can act as a general acid. In a cell, specific low pH organelles, such as endosomes and lysosomes can provide a cleaving environment for acid cleavable linking groups. Examples of acid cleavable linking groups include but are not limited to hydrazones, esters, and esters of amino acids. Acid cleavable groups can have the general formula —C══NN—, C(O)O, or —OC(O). A specific embodiment is when the carbon attached to the oxygen of the ester (the alkoxy group) is an aryl group, substituted alkyl group, or tertiary alkyl group such as dimethyl pentyl or t-butyl. These candidates can be evaluated using methods analogous to those described above.

In some embodiments, ester-based cleavable linking groups, which are cleaved by enzymes such as esterases and amidases in cells, are envisioned. Examples of ester-based cleavable linking groups include but are not limited to esters of alkylene, alkenylene and alkynylene groups. Ester cleavable linking groups have the general formula —C(O)O—, or —OC(O)—. These candidates can be evaluated using methods analogous to those described above.

In yet further embodiments, peptide-based cleavable linking groups, which are cleaved by enzymes such as peptidases and proteases in cells, are envisioned. Peptide-based cleavable linking groups are peptide bonds formed between amino acids to yield oligopeptides (e.g., dipeptides, tripeptides etc.) and polypeptides. Peptide-based cleavable groups do not include the amide group (—C(O)NH—). The amide group can be formed between any alkylene, alkenylene or alkynelene. A peptide bond is a special type of amide bond formed between amino acids to yield peptides and proteins. The peptide based cleavage group is generally limited to the peptide bond (i.e., the amide bond) formed between amino acids yielding peptides and proteins and does not include the entire amide functional group. Peptide-based cleavable linking groups have the general formula —NHCHR^AC(O)NHCHR^BC(O)—, where R^A and R^B are the R groups of the two adjacent amino acids. These candidates can be evaluated using methods analogous to those described above. As used herein, “carbohydrate” refers to a compound which is either a carbohydrate per se made up of one or more monosaccharide units having at least 6 carbon atoms (which may be linear, branched or cyclic) with an oxygen, nitrogen or sulfur atom bonded to each carbon atom; or a compound having as a part thereof a carbohydrate moiety made up of one or more monosaccharide units each having at least six carbon atoms (which may be linear, branched or cyclic), with an oxygen, nitrogen or sulfur atom bonded to each carbon atom. Representative carbohydrates include the sugars (mono-, di-, tri- and oligosaccharides containing from about 4-9 monosaccharide units), and polysaccharides such as starches, glycogen, cellulose and polysaccharide gums.

Synthesis of Interfering RNA

The interfering RNA molecules that can be employed in the methods of the present invention can readily be made using techniques known in the art, for example, using conventional RNA solid phase synthesis. See, for example, U.S. Pat. No. 8,877,917. The polynucleotides of the double-stranded RNA molecules can be assembled on a suitable nucleic acid synthesizer utilizing standard nucleotide or nucleoside precursors (e.g. phosphoramidites). Automated nucleic acid synthesizers are sold commercially by several vendors, including DNA/RNA synthesizers from Applied Biosystems (Foster City, Calif.), MerMade synthesizers from BioAutomation (Irving, Tex.), and OligoPilot synthesizers from GE Healthcare Life Sciences (Pittsburgh, Pa.).

The 2′ silyl protecting group can be used in conjunction with acid labile dimethoxytrityl (DMT) at the 5′ position of ribonucleosides to synthesize oligonucleotides via phosphoramidite chemistry. Final deprotection conditions are known not to significantly degrade RNA products. All syntheses can be conducted in any automated or manual synthesizer on large, medium, or small scale. The syntheses may also be carried out in multiple well plates or glass slides.

The 2′-O-silyl group can be removed via exposure to fluoride ions, which can include any source of fluoride ion, e.g., those salts containing fluoride ion paired with inorganic counterions e.g., cesium fluoride and potassium fluoride or those salts containing fluoride ion paired with an organic counterion, e.g., a tetraalkylammonium fluoride. A crown ether catalyst can be utilized in combination with the inorganic fluoride in the deprotection reaction. Preferred fluoride ion source are tetrabutylammonium fluoride or aminehydrofluorides (e.g., combining aqueous HF with triethylamine in a dipolar aprotic solvent, e.g., dimethylformamide).

The choice of protecting groups for use on the phosphite triesters and phosphotriesters can alter the stability of the triesters towards fluoride. Methyl protection of the phosphotriester or phosphitetriester can stabilize the linkage against fluoride ions and improve process yields.

Since ribonucleosides have a reactive 2′ hydroxyl substituent, it can be desirable to protect the reactive 2′ position in RNA with a protecting group that is orthogonal to a 5′-O-dimethoxytrityl protecting group, e.g., one stable to treatment with acid. Silyl protecting groups meet this criterion and can be readily removed in a final fluroide deprotection step that can result in minimal RNA degradation.

Tetrazole catalysts can be used in the standard phosphoramidite coupling reaction. Preferred catalysts include e.g., tetrazole, S-ethyl-tetrazole, p-nitrophenyltetrazole.

See also, for example, Trufert et al., Tetrahedron, 52:3005, 1996; and Manoharan, “Oligonucleotide Conjugates in Antisense Technology,” in Antisense Drug Technology, ed. S. T. Crooke, Marcel Dekker, Inc., 2001. The protected monomer compounds can be separated from a reaction mixture and further purified by a method such as column chromatography, high pressure liquid chromatography, or recrystallization. As can be appreciated by the skilled artisan, further methods of synthesizing the compounds of the formulae herein will be evident to those of ordinary skill in the art. Additionally, the various synthetic steps may be performed in an alternate sequence or order to give the desired compounds. Other synthetic chemistry transformations, protecting groups (e.g., for hydroxyl, amino, etc. present on the bases) and protecting group methodologies (protection and deprotection) useful in synthesizing the compounds described herein are known in the art and include, for example, those such as described in R. Larock, Comprehensive Organic Transformations, VCH Publishers (1989); T. W. Greene and P. G. M. Wuts, Protective Groups in Organic Synthesis, 2d. Ed., John Wiley and Sons (1991); L. Fieser and M. Fieser, Fieser and Fieser's Reagents for Organic Synthesis, John Wiley and Sons (1994); and L. Paquette, ed., Encyclopedia of Reagents for Organic Synthesis, John Wiley and Sons (1995), and subsequent editions thereof.

Methods of Treatment

In further embodiments of the present invention, a method of treating a human subject, comprising administering a therapeutic dosage of the antigen binding proteins or antibodies or interfering RNA (e.g., siRNA or shRNA) of the present invention is provided. In one embodiment, the antigen binding proteins are monoclonal antibodies. In one embodiment, the antigen binding proteins are human antibodies. In another embodiment, the antigen binding proteins or antibodies are humanized antibodies. In another embodiment, interfering RNA (e.g., siRNA or shRNA) is administered. As used herein the term “subject” refers to a mammal, including humans, and can be used interchangeably with the term “patient”.

Given the results of the Icelandic study presented in the examples below, there need not be any particular further manipulation downstream in a host receiving a therapy involving administering the ASGR inhibitor (e.g., antigen binding proteins or antibodies or RNAi) to the host. That is, in some embodiments, the antibody (or RNAi) need simply be one or more of the antibodies (or RNAi) described herein, which binds to (and inhibits) ASGR (such as ASGR1), and be administered in an amount, and at a frequency sufficient to reduce the risk of cardiovascular disease, myocardial infarction, or other disorders provided herein. In some embodiments, the antibody (or RNAi) is administered in an amount sufficient to result in a lowering of non-HDL cholesterol. In some embodiments, the antibody (or RNAi) is administered in an amount sufficient to result in lowering LDL cholesterol. While not intended to be limiting unless expressed otherwise, below is a description of various embodiments through which ASGR can have an impact on various disorders, and thus, how the various antibodies (or RNAi) provided herein (which can inhibit (e.g., reduce) ASGR function) can have an impact on the various disorders provided herein.

In some embodiments, the ASGR inhibitor (e.g., antigen binding proteins or antibodies or RNAi) operates through ASGR's role in platelet clearance. Inhibiting (e.g., reducing) the receptor results in a reduction in clearance of old platelets. Such older platelets do not coagulate as well as new platelets and as a result, the blood is thinner. As a result, plaques can lessen and there can be a positive impact (e.g., stroke is lessened) for the subject.

In some embodiments, the ASGR inhibitor (e.g., antigen binding proteins or antibodies or RNAi) binds to ASGR to alter inflammation. For example, reducing the ASGR-1 receptor results in a modification of the immune response. Normally, there can be an increase in proinflammatory cytokines. These proinflammatory cytokines are circulating in the native state (one where the ASGR1 receptor is not reduced). However, ALP (alkaline phosphatase) can have an anti-inflammatory role thereby reducing inflammation and coagulopathy systemically. In some embodiments, the mechanism of action involves reducing ASGR1 which increases ALP and therefore reduces inflammation.

In some embodiments, and without intending to be limited by theory (unless expressed otherwise), the ASGR inhibitor (e.g., antigen binding proteins or antibodies or RNAi) can reduce an activity due to ASGR interacting with one or more other molecules, either directly or indirectly. For example, various embodiments for various proteins are provided herein in Examples 18 and 19. As noted above, this selection of proteins can also be useful for determining the effectiveness of the ASGR inhibitor (e.g., antigen binding proteins or antibodies or RNAi) (and/or the amount of the antibody and/or identification of a subject who can respond to the therapy (or RNAi)) by monitoring one or more of these proteins as a Cardiovascular Disease marker. Thus, these markers are useful as markers and, without intending to be limited by theory, in some embodiments, one or more of the proteins disclosed below is the protein through which (directly or indirectly) ASGR1 modulation achieves its benefit for one or more of the disorders provided herein, including cardiovascular disease.

In addition to the marker proteins described in Examples 18 and 19 herein (which also allow for various mechanisms of action and monitoring the effectiveness of various ASGR inhibitors (e.g., antigen binding proteins or antibodies or RNAi) and dosage regimes), the following proteins of interest are those that interact with ASGR, and ASGR-1 in particular, directly by binding to them. Thus, these are additional interactions that can be inhibited (e.g., reduced) for various embodiments provided herein, by various ASGR inhibitors (e.g., antigen binding proteins or antibodies or RNAi). While not intending to be limited by theory (unless explicitly stated otherwise), ASGR-1's binding to one or more of the following proteins can be inhibited (e.g., reduced) by using an ASGR-1 inhibitor (e.g., antigen binding protein or antibody or RNAi) provided herein that inhibits (e.g., reduces) the noted binding. While in some embodiments, the protein interactions are contemplated as resulting mechanisms of action that occur downstream from when ASGR levels are effectively reduced by an ASGR inhibitor (e.g., antigen binding protein or antibody binding or via RNAi), the following list is a list of proteins that directly bind to ASGR1, and thus whose direct binding to ASGR-1 can be inhibited (e.g., reduced) by one or more of the antigen binding proteins or antibodies provided herein (or RNAi). In some embodiments, the ASGR-1 inhbiitor (e.g., antigen bindng protein or antibody or RNAi) inhibits (e.g., reduces) ASGR-1's binding to one or more of: Alpha-2-HS-glycoprotein (aka Fetuin A) (see Tozawa et al, J Biol Chem (2001) 276:12624-12628); Asialoglycoprotein receptor 1 (see Stockert et al (1977) Science 197:667-668), Orosomucoid (aka alpha-1-acid glycoprotein) (see Tozawa et al, J Biol Chem (2001) 276:12624-12628), Alkaline phosphatase, (see Hardonk M J, Scholtens H B. Histochemistry. 1980; 69(3):289-97 and Scholtens H B, Meijer D K, Hardonk M J. Liver. 1982 March; 2(1):14-21), LDL and chylomicrons (Windler et al Biochem J (1991) 276:79-87), Fibronectin (see Rotundo et al Hepatology (1998) 28:475-485), and IgA (see Stockert et al PNAS (1982) 79:6229-6231). In some embodiments, the ASGR inhibitor (e.g., antigen binding protein or antibody or RNAi) antibody binds to ASGR and inhibits (e.g., reduces) ASGR's interaction with a molecule that has a terminal gal or galNAc, including, but not limited to protein ligands, synthetic polysaccharides, solid substrates, etc. In some embodiments, the ASGR inhibitor (e.g., antigen binding proteins or antibodies or RNAi) inhibits (e.g., reduces) ASGR1's ability to bind to an asialylated molecule. In some embodiments, the invention provides a method of treating or preventing a cardiovascular disease comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the cardiovascular disease is coronary artery disease or myocardial infarction. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described hereinn. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the relative risk reduction of a cardiovascular event is at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60% in the patient. Some non-limiting examples of cardiovascular disease include atherosclerotic diseases, such as, for example, coronary heart disease, coronary artery disease, peripheral arterial disease, stroke (ischaemic and hemorrhagic), angina pectoris, cerebrovascular disease, acute coronary syndrome, and myocardial infarction. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitors of the present invention are useful in reducing the risk of: nonfatal heart attacks, fatal and non-fatal strokes, certain types of heart surgery, hospitalization for heart failure, chest pain in patients with heart disease, and/or cardiovascular events because of established heart disease such as prior heart attack, prior heart surgery, and/or chest pain with evidence of clogged arteries. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitors of the present invention and methods can be used to reduce the risk of recurrent cardiovascular events.

In some embodiments, the invention provides a method of decreasing the risk of acquiring coronary artery disease or having an MI comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described hereinn. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the relative risk reduction of coronary artery disease or MI is at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60% in the patient.

In some embodiments, the invention provides a method of reducing blood LDL cholesterol levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described hereinn. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the blood LDL cholesterol level in the patient is reduced by at least about 15%, as compared to a predose level of blood LDL cholesterol in the patient. In some embodiments of this aspect of the invention, the blood LDL cholesterol level of said patient is lowered by at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, or at least about 90% as compared to a predose level of blood LDL cholesterol in the patient.

In some embodiments, the invention provides a method of reducing non-HDL cholesterol levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described hereinn. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the non-HDL cholesterol level in the patient is reduced by at least about 5%, as compared to a predose level of non-HDL cholesterol in the patient. In some embodiments of this aspect of the invention, the non-HDL cholesterol level of said patient is lowered by at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, or at least about 90% as compared to a predose level of non-HDL cholesterol in the patient.

In some embodiments, the invention provides a method of increasing ALP levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described hereinn. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the ALP level in the patient is increased by at least about 30%, as compared to a predose level of ALP in the patient. In some embodiments of this aspect of the invention, the ALP level of said patient is increased by at least about at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, or at least about 90% as compared to a predose ALP level in the patient. In some embodiments, ALP levels are increased at least about 1.25×1.5×, 2×, 2.5×, 3×, 3.5×, 4×, 4.5×, and 5× over pretreatment.

In some embodiments, the invention provides a method of antagonizing ASGR, ASGR-1 and/or ASGR-2 in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described hereinn. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein.

In some embodiments, a method of treating or preventing a cardiovascular disease is provided and comprises administering to a patient in need thereof a therapeutically effective dose of an ASGR inhibitor as described herein. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-2. In some embodiments, the ASGR inhibitor is an inhibitor of ASGR-1 and ASGR-2. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is one or more of the antigen binding proteins described herein. In some embodiments, the ASGR, ASGR-1 and/or ASGR-2 inhibitor is an interfering RNA (e.g., siRNA or shRNA) as described herein. In some embodiments, the relative risk reduction of a cardiovascular event is at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60% in the patient.

The term “treatment” encompasses alleviation of at least one symptom or other embodiment of a disorder, or reduction of disease severity, and the like. An antigen binding protein, in particular a human antibody according to the present invention, need not effect a complete cure, or eradicate every symptom or manifestation of a disease, to constitute a viable therapeutic agent. As is recognized in the pertinent field, drugs employed as therapeutic agents may reduce the severity of a given disease state, but need not abolish every manifestation of the disease to be regarded as useful therapeutic agents. Simply reducing the impact of a disease (for example, by reducing the number or severity of its symptoms, or by increasing the effectiveness of another treatment, or by producing another beneficial effect), or reducing the likelihood that the disease will occur or worsen in a subject, is sufficient. One embodiment of the invention is directed to a method comprising administering to a patient an antigen binding protein or interfering RNA in an amount and for a time sufficient to induce a sustained improvement over baseline of an indicator that reflects the severity of the particular disorder.

The term “prevention” encompasses prevention of at least one symptom or other embodiment of a disorder, and the like. A prophylactically administered treatment incorporating an antigen binding protein, in particular a human antibody according to the present invention, need not be completely effective in preventing the onset of a condition in order to constitute a viable prophylactic agent. Simply reducing the likelihood that the disease will occur or worsen in a subject, is sufficient.

The term “non-HDL cholesterol” encompasses all cholesterol-containing proatherogenic lipoproteins, including LDL cholesterol, very-low-density lipoprotein, intermediate-density lipoprotein, lipoprotein(a), and chylomicron. Non-HDL cholesterol levels are calculated by subtracting HDL cholesterol levels from total cholesterol levels.

As is understood in the pertinent field, pharmaceutical compositions comprising the antigen binding proteins and/or interfering RNA are administered to a subject in a manner appropriate to the indication and the composition. In one embodiment, pharmaceutical compositions comprise the human antibodies of the present invention. In another embodiment, pharmaceutical compositions comprise interfering RNA. Pharmaceutical compositions may be administered by any suitable technique, including but not limited to parenterally, topically, or by inhalation. If injected, the pharmaceutical composition can be administered, for example, via intra-articular, intravenous, intramuscular, intralesional, intraperitoneal or subcutaneous routes, by bolus injection, or continuous infusion. Delivery by inhalation includes, for example, nasal or oral inhalation, use of a nebulizer, inhalation of the antigen binding protein in aerosol form, and the like. Other alternatives include oral preparations including pills, syrups, or lozenges.

Advantageously, the antigen binding proteins or interfering RNA are administered in the form of a composition comprising one or more additional components such as a physiologically acceptable carrier, excipient or diluent. Optionally, the composition additionally comprises one or more physiologically active agents. In various particular embodiments, the composition comprises one, two, three, four, five, or six physiologically active agents in addition to one or more antigen binding proteins (e.g, human antibodies) or interfering RNA.

Kits for use by medical practitioners are provided including one or more antigen binding proteins or interfering RNA and a label or other instructions for use in treating any of the conditions discussed herein. In one embodiment, the kit includes a sterile preparation of one or more human antibodies, or one or more interfering RNA which may be in the form of a composition as disclosed herein, and may be in one or more vials.

Dosages and the frequency of administration may vary according to such factors as the route of administration, the particular antigen binding proteins or interfering RNA employed, the nature and severity of the disease to be treated, whether the condition is acute or chronic, and the size and general condition of the subject. Appropriate dosages can be determined by procedures known in the pertinent art, e.g. in clinical trials that may involve dose escalation studies.

An antigen binding protein, e.g., monoclonal antibodies, or interfering RNA may be administered, for example, once or more than once, e.g., at regular intervals over a period of time. In particular embodiments, an antigen binding protein or interfering RNA is administered over a period of at least once a month or more, e.g., for one, two, or three months or even indefinitely. For treating chronic conditions, long-term treatment is generally most effective. However, for treating acute conditions, administration for shorter periods, e.g. from one to six weeks, may be sufficient. In general, the antigen binding protein or interfering RNA is administered until the patient manifests a medically relevant degree of improvement over baseline for the chosen indicator or indicators.

One example of therapeutic regimens provided herein comprise subcutaneous injection of an antigen binding protein or interfering RNA once a week, or once every two weeks, or once every month, once every other month, once every three months, once every six months or longer, at an appropriate dosage, to treat a condition in which it is desired to target cells expressing ASGR, ASGR-1 and/or ASGR-2. Weekly or monthly administration of antigen binding protein could be continued until a desired result is achieved, e.g., the subject's symptoms subside. Treatment may resume as needed, or, alternatively, maintenance doses may be administered.

In some embodiments, one or more of the markers in Tables 18.1, 18.2, 19.3, and 19.4 can be used to determine whether or not the amount of ASGR inhibitor (e.g., antigen binding protein and/or antibody and/or RNAi) administered is sufficient for its intended therapeutic application. In some embodiments, when one or more of the alterations in protein level, for the proteins outlined in one or more of Tables 18.1, 18.2, 19.3, and 19.4 changes in response to administering the antigen binding protein, antibody and/or RNAi, the antigen binding protein, antibody and/or RNAi is having an effect in the host. In some embodiments, the amount is sufficient when it alters the level of non-HDL cholesterol to a desired amount or reduces it by a desired amount. In some embodiments, the markers used can be one or more of those in one or more of Tiers 1, 2, 3, 4, and 5 of Table 19.4. In some embodiments, the markers used can be one or more of those in one or more of Tiers 1 and 5 of Table 19.4.

Combination Therapies

Particular embodiments of methods and compositions of the invention involve the use of at least one antigen binding protein and/or interfering RNA and one or more other therapeutics useful for treating or preventing cardiovascular disease, for example. In one embodiment, antigen binding proteins and/or interfering RNA are administered alone or in combination with other agents useful for treating the condition with which the patient is afflicted. Examples of such agents include both proteinaceous and non-proteinaceous drugs. When multiple therapeutics are co-administered, dosages may be adjusted accordingly, as is recognized in the pertinent art. “Co-administration” and combination therapy are not limited to simultaneous administration, but also include treatment regimens in which an antigen binding protein is administered at least once during a course of treatment that involves administering at least one other therapeutic agent to the patient. In certain embodiments, an antigen binding protein or interfering RNA is administered prior to the administration of at least one other therapeutic agent. In certain embodiments, an antigen binding protein or interfering RNA is administered concurrent with the administration of at least one other therapeutic agent. In certain embodiments, an antigen binding protein or interfering RNA is administered subsequent to the administration of at least one other therapeutic agent.

In one embodiment, the at least one antigen binding protein or antibody and/or the interfering RNA is administered to a subject in combination with an anti-PCSK9 antibody (e.g., Repatha®′, Praluent®, bococizumab). In another embodiment, the at least one antigen binding protein or antibody and/or the interfering RNA is administered to a subject in combination with at least one other cholesterol-lowering (serum and/or total body cholesterol) agent. In some embodiments, the agents that increase the expression of LDLR, have been observed to increase serum HDL levels, lower LDL levels or lower triglyceride levels. Exemplary agents include, but are not limited to, statins (e.g., atorvastatin, cerivastatin, fluvastatin, lovastatin, mevastatin, pitavastatin, pravastatin, rosuvastatin, simvastatin), Nicotinic acid (Niacin) (NIACOR, NIASPAN (slow release niacin), SLO-NIACIN (slow release niacin)), Fibric acid (LOPID (Gemfibrozil), TRICOR (fenofibrate), Bile acid sequestrants (QUESTRAN (cholestyramine), colesevelam (WELCHOL), COLESTID (colestipol)), Cholesterol absorption inhibitors (ZETIA (ezetimibe)), combining nicotinic acid with statin (ADVICOR (LOVASTATIN and NIASPAN), combining a statin with an absorption inhibitor (VYTORIN (ZOCOR and ZETIA) and/or lipid modifying agents. In some embodiments, the at least one antigen binding protein and/or interfering RNA is combined with PPAR gamma agonsits, PPAR alpha/gamma agonists, squalene synthase inhibitors, CETP inhibitors, anti-hypertensives, anti-diabetic agents (such as sulphonyl ureas, insulin, GLP-1 analogs, DDPIV inhibitors), ApoB modulators, MTP inhibitoris and/or arteriosclerosis obliterans treatments. In some embodiments, the at least one antigen binding protein and/or interfering RNA is combined with an agent that increases the level of LDLR protein in a subject, such as statins, certain cytokines like oncostatin M, estrogen, and/or certain herbal ingredients such as berberine. In some embodiments, the at least one antigen binding protein and/or interfering RNA is combined with an agent that increases serum cholesterol levels in a subject (such as certain anti-psycotic agents, certain HIV protease inhibitors, dietary factors such as high fructose, sucrose, cholesterol or certain fatty acids and certain nuclear receptor agonists and antagonists for RXR, RAR, LXR, FXR). The combination of the two can allow for the undesirable side-effects of other agents to be mitigated by the antigen binding protein or interfering RNA.

Diagnostic Uses

In one embodiment, antigen binding proteins of the invention are useful for detecting the presence of ASGR, ASGR-1 and/or ASGR-2 in a biological sample. The term “detecting” as used herein encompasses quantitative or qualitative detection. In certain embodiments, a biological sample comprises a cell or tissue. In certain embodiments, such tissues include tissues that express ASGR, ASGR-1 and/or ASGR-2 at higher levels relative to other tissues.

In one embodiment, the invention provides a method of detecting the presence of ASGR, ASGR-1 and/or ASGR-2 in a biological sample. In certain embodiments, the method comprises contacting the biological sample with an antigen binding protein of the invention under conditions permissive for binding of an antigen binding protein to ASGR, ASGR-1 and/or ASGR-2, and detecting whether a complex is formed between the antigen binding protein and ASGR, ASGR-1 and/or ASGR-2.

In one embodiment, the invention provides a method of diagnosing a disorder associated with increased or decreased expression of ASGR, ASGR-1 and/or ASGR-2. In certain embodiments, the method comprises contacting a test cell with an antigen binding protein; determining the level of expression (either quantitatively or qualitatively) of ASGR, ASGR-1 and/or ASGR-2 by the test cell by detecting binding of the antigen binding protein to ASGR, ASGR-1 and/or ASGR-2; and comparing the level of expression of ASGR, ASGR-1 and/or ASGR-2 by the test cell with the level of expression of ASGR, ASGR-1 and/or ASGR-2 by a control cell (e.g., a normal cell of the same tissue origin as the test cell or a cell that expresses ASGR, ASGR-1 and/or ASGR-2 at levels comparable to such a normal cell), wherein a higher or lower level of expression of ASGR, ASGR-1 and/or ASGR-2 by the test cell as compared to the control cell indicates the presence of a disorder associated with increased or decreased expression of ASGR, ASGR-1 and/or ASGR-2. In certain embodiments, the test cell is obtained from an individual suspected of having a disorder associated with increased or decreased expression of ASGR, ASGR-1 and/or ASGR-2.

In certain embodiments, a method of diagnosis or detection, such as those described above, comprises detecting binding of an antigen binding protein of the invention to ASGR, ASGR-1 and/or ASGR-2 expressed on the surface of a cell or in a membrane preparation obtained from a cell expressing ASGR, ASGR-1 and/or ASGR-2 on its surface. In certain embodiments, the method comprises contacting a cell with an antigen binding protein under conditions permissive for binding of an antigen binding protein of the invention to ASGR, ASGR-1 and/or ASGR-2, and detecting whether a complex is formed between the antigen binding protein of the invention and ASGR, ASGR-1 and/or ASGR-2 on the cell surface. An exemplary assay for detecting binding of an antigen binding protein of the invention to ASGR, ASGR-1 and/or ASGR-2 expressed on the surface of a cell is a “FACS” assay.

Certain other methods can be used to detect binding of antigen binding protein of the invention to ASGR, ASGR-1 and/or ASGR-2. Such methods include, but are not limited to, antigen-binding assays that are well known in the art, such as western blots, radioimmunoassays, ELISA (enzyme linked immunosorbent assay), “sandwich” immunoassays, immunoprecipitation assays, fluorescent immunoassays, protein A immunoassays, and immunohistochemistry (IHC).

In certain embodiments, antigen binding proteins of the invention are labeled. Labels include, but are not limited to, labels or moieties that are detected directly (such as fluorescent, chromophoric, electron-dense, chemiluminescent, and radioactive labels), as well as moieties, such as enzymes or ligands, that are detected indirectly, e.g., through an enzymatic reaction or molecular interaction. Exemplary labels include, but are not limited to, the radioisotopes ³²P, ¹⁴C, ¹²⁵I, ³H, and ¹³¹I, fluorophores such as rare earth chelates or fluorescein and its derivatives, rhodamine and its derivatives, dansyl, umbelliferone, luceriferases, e.g., firefly luciferase and bacterial luciferase (U.S. Pat. No. 4,737,456), luciferin, 2,3-dihydrophthalazinediones, horseradish peroxidase (HRP), alkaline phosphatase, beta-galactosidase, glucoamylase, lysozyme, saccharide oxidases, e.g., glucose oxidase, galactose oxidase, and glucose-6-phosphate dehydrogenase, heterocyclic oxidases such as uricase and xanthine oxidase, coupled with an enzyme that employs hydrogen peroxide to oxidize a dye precursor such as HRP, lactoperoxidase, or microperoxidase, biotin/avidin, spin labels, bacteriophage labels, stable free radicals, and the like.

In certain embodiments, antigen binding proteins of the invention are immobilized on an insoluble matrix. Immobilization entails separating the antigen binding protein of the invention from any ASGR, ASGR-1 and/or ASGR-2 that remains free in solution. This conventionally is accomplished by either insolubilizing the antigen binding protein of the invention before the assay procedure, as by adsorption to a water-insoluble matrix or surface (see, e.g., Bennich et al., U.S. Pat. No. 3,720,760), or by covalent coupling (for example, using glutaraldehyde cross-linking), or by insolubilizing the antigen binding protein of the invention after formation of a complex between the antigen binding protein of the invention and ASGR, ASGR-1 and/or ASGR-2, e.g., by immunoprecipitation.

The invention having been described, the following examples are offered by way of illustration, and not limitation.

Numerous sequences have been provided herein. Where there is a discrepancy in the sequences, the sequences in the tables presented within the figures control, unless there is an indication otherwise. If there is any unintended difference between the same consensus sequences, the consensus sequences as provided in the figures (from the tables within the figures) will control (unless indicated otherwise). For any further descrepancies (rather than just alternative sequences) the sequences within Tables 1-7 will control, unless designated otherwise. The figures contain multiple sequences, sequence alignments and sequence components of various nucleic and amino acid sequences. The present specification references this information in terms of the designated tables and/or the designated figures. Either reference (via figure or table) can be used and either designation (figure or table) will indicate the alternative designation as well, where appropriate. Thus, FIG. 48 designates Table 1, FIG. 49 designates Table 2, FIG. 50 designates Table 3, FIG. 51 designates Table 4, FIG. 52 designates Table 5, FIG. 53 designates Table 6, FIG. 54 designates Table 7, FIG. 55 designates Tables 19A, 19B, 19C, 20A, 20B, and 20C, FIG. 56 designates Tables 21-48, and FIG. 57 designates Tables 49-134, and vice versa. As such, any discussion herein in regard to the above figures or tables is interchangeable with respect to the “table” or “figure” nomenclature.

EXAMPLES

Example 1—Identification of Rare Sequence Variants that Disrupt ASGR-1 Function and Lower Non-HDL Cholesterol and Protect Against Coronary Artery Disease

The level of circulating non-high density lipoprotein (non-HDL) cholesterol is heritable and strongly correlated with the risk of coronary artery disease (CAD) and myocardial infraction (MI). Whole-genome sequencing offers the potential to search for rare sequence variants that have large effects on serum lipid levels and hence the risk of cardiovascular disease, such as CAD and MI.

Methods

Study Participants:

Details of the population sample sets from Iceland, Denmark and The Netherlands, used to measure the various lipids traits (non-HDL cholesterol, HDL cholesterol, LDL cholesterol and triglycerides), alkaline phosphatase (ALP), ferritin, and vitamin B12, are outlined in Table 1.2. The dataset for ferritin is not shown. The coronary artery disease case-control sample sets that were a part of the study are outlined in Table 1.1.

Icelandic Study Population

Study participants were enrolled as part of various genetics programs at deCODE. Blood lipid levels (total cholesterol, non-high density lipoprotein cholesterol (non-HDL-C), low density lipoprotein cholesterol (LDL-C), high density lipoprotein cholesterol (HDL-C) and triglycerides), alkaline phosphatase and vitamin B12 levels were obtained from three of the largest laboratories in Iceland: 1) Landspítali—The National University Hospital of Iceland (LUH), Reykjavík (measurements performed between the years 1993 and 2012, hospitalized and ambulatory patients), 2) The Laboratory in Mjódd (RAM), Reykjavik (measurements performed between 2004 and 2012, ambulatory patients) and 3) Akureyri Hospital, The Regional Hospital in North Iceland, Akureyri (performed between 2004 and 2010, hospitalized and ambulatory patients). Information on the participants is outlined in Table 1.2. Lipid levels were adjusted for sex, year of birth and age at measurement, lipid lowering medication and measurement site, using the average of multiple measurements for an individual, and then normalized to a standard normal distribution using quantile normalization. To obtain effect estimates in mmol/L the estimates from the regression analysis were multiplied by the estimated standard deviation of lipid level in the population. Given their approximately log-normal distribution, triglyceride levels were log-transformed before adjustment and the corresponding effect estimates are presented as percentage change instead of units of mmol/L. The total number of individuals with non-HDL cholesterol, LDL cholesterol, HDL cholesterol and triglycerides in Iceland is shown in the Table 1.3 below. For each lipid, the number of chip-typed and directly imputed individuals and those with familial imputations is also shown.

TABLE 1.3
Lipid levels of Icelandic Study Participants
	Non-HDL-C	LDL-C	HDL-C	Triglycerides
Total number	119,146	53,841	119,514	80,111
Direct	69,277	51,029	69,414	59,678
imputation
Familial	49,869	2,812	50,100	20,433
imputation
The total number of Icelandic individuals with lipid values used in the study and the breakdown into those that were chip-typed and directly imputed (Direct imputation) and those that were first and second degree relatives of chip-typed individuals and had their genotypes inferred based on genealogy (Familial imputation).

Non-HDL cholesterol was obtained by subtracting HDL cholesterol from total cholesterol and measures the amount of cholesterol carried within all atherogenic lipoprotein particles (VLDL, IDL, LDL, chylomicrons and Lp(a)). The LDLcholesterol was calculated, using the Friedewald equation (for triglyceride levels <4.00 mmol/L) (Friedewald, W. T., Levy, R. I. & Fredrickson, D. S. Estimation of the concentration of low-density lipoprotein cholesterol in plasma, without use of the preparative ultracentrifuge. Clin. Chem. 18, 499-502 (1972)). Total cholesterol and HDL-cholesterol values are a mixture of fasting and non-fasting values, whereas triglycerides are fasting values exclusively.

Coronary artery disease (CAD) was defined as a) individuals in the MONICA registry who suffered myocardial infarction (MI) before the age of 75 in Iceland between 1981 and 2002 and satisfied the MONICA criteria (Gudbjartsson, et al., Large-scale whole-genome sequencing of the Icelandic population. Nature genetics 2015), b) subjects with CAD discharge diagnoses (ICD 9 codes 410.*, 411.*, 412.*, 414.* or ICD 10 codes I20.0, I21.*, I22.*. I23.*, I24.*, I25.*) from LUH, c) subjects diagnosed with significant angiographic CAD (see defined below) identified from a nationwide clinical registry of coronary angiography and percutaneous coronary interventions at LUH between the years 1987 and 2012, d) subjects undergoing coronary artery bypass grafting (CABG) procedures at LUH between the years 2002 and 2011 or e) cause of death or contributing cause of death listed as MI or CAD (ICD 9 or 10 codes) on death registries between the years 1996 and 2009. Coronary angiograms in the nationwide registry were evaluated by an interventional cardiologist. Patients were considered to have significant angiographic CAD if one or more of the three major epicardial coronary vessels or the left main coronary artery was found to have at least 50% stenosis by visual estimation.

Non-Icelandic Study Populations

Characteristics of the non-Icelandic sample sets are outlined in Table 1.1 and Table 1.2. All the studies outlined in Tables 1.1 and 1.2 were approved by appropriate bioethics and/or data protection authorities. For samples from the Nijmegen Biomedical Study, Netherlands, the lipid values (namely, total cholesterol, HDL-cholesterol and triglycerides) were all non-fasting values. For samples from the Danish Inter99 and Addition studies, the lipid values were all fasting values. All participating subjects donating biological samples signed informed consents. Personal identities of the phenotypes and biological samples were encrypted by a third party system provided by the Icelandic Data Protection Authority.

Data Generation and Analysis

Whole-Genome Sequencing, SNP Calling, and Imputation

The Icelandic samples were genotyped using Illumina microarrays (Samani N J et al., Genomewide association analysis of coronary artery disease. The New England journal of medicine 2007; 357:443-53). The whole-genomes of 2,636 Icelanders were sequenced using the standard TruSeq methodology (Illumina) to a mean depth of at least 10× (median 20×)(Samani N J et al., Genomewide association analysis of coronary artery disease. The New England journal of medicine 2007; 357:443-53). For improved sequencing coverage of the GC-rich intron 4 in ASGR-1 gene, the whole-genome sequence data generated for 738 Icelanders was analyzed using TruSeq PCR-free method from Illumina (mean depth of 30×). The del12 variant in intron 4 of ASGR-1 was detected in this dataset.

Single-Track Assay SNP and Microsatellite Genotyping:

We performed single SNP genotyping of rs186021206, using the Centaurus (Nanogen) platform (Gretarsdottir S, et al., Genome-wide association study identifies a sequence variant within the DAB2IP gene conferring susceptibility to abdominal aortic aneurysm. Nature genetics 2010; 42:692). The del12 variant was genotyped using a PCR based method with the following primers: forward primer (NED labelled) 5′-TTCATCTTTCTTCCCACATTGC-3′ (SEQ ID NO: 32600), reverse primer 5′-GGGCCTGAGAGAGACGTTCA-3′ (SEQ ID NO: 32601). An internal size standard was added to the resulting PCR products and the fragments were separated and detected on an Applied Biosystems model 3730 sequencer, using in-house Allele Caller software.

Statistical Analyses:

Associations between imputed genotypes and serum lipids (non-HDL cholesterol, HDL cholesterol, LDL cholesterol and triglycerides), ALP, ferritin and vitamin B12 levels in the Icelandic dataset were tested using a generalized linear regression, assuming an additive genetic model (Samani N J et al., Genomewide association analysis of coronary artery disease. The New England journal of medicine 2007; 357:443-53; and Olsen M H, et al., N-terminal pro-brain natriuretic peptide, but not high sensitivity C-reactive protein, improves cardiovascular risk prediction in the general population. European heart journal 2007; 28:1374-81). For the Icelandic dataset, logistic regression was used to test for association between the del12 variant and coronary artery disease and myocardial infarction, treating the disease status as the response and the number of copies of del12 an individual carries as the explanatory variable. Coronary artery disease case-control association analysis for the non-Icelandic sample sets was done using the NEMO software (Jorgensen A B, et al., Loss-of-function mutations in APOC3 and risk of ischemic vascular disease. The New England journal of medicine 2014; 371:32-41) assuming a multiplicative risk model. Results for the Icelandic and the non-Icelandic sample sets were combined using a Mantel-Haenszel fixed effects model. To estimate the effect of the del12 variant on myocardial infarction-free survival, Kaplan-Meier curves were estimated for survival to first myocardial infarction in heterozygous carriers and non-carriers (Hoogendoorn E H, et al., Thyroid function and prevalence of anti-thyroperoxidase antibodies in a population with borderline sufficient iodine intake: influences of age and sex. Clinical chemistry 2006; 52:104-11) by dividing the corresponding chi-square statistic by 1.36 for non-HDL cholesterol, 1.57 for HDL cholesterol, 1.40 for triglycerides, 1.53 for ALP, 1.30 for vitamin B12, 1.71 for coronary artery disease and 1.48 for myocardial infarction.

To obtain a reliable imputation of the del12 variant, 3,799 Icelandic individuals were genotyped for the del12 variant and those genotypes were used as a training set for imputation of the del12 variant into the rest of the Icelandic population. The imputation information for del12 was 0.99.

The Icelandic samples were genotyped using Illumina microarrays as described above (Gudbartssoon, D F, et al., Large Scale whole-genome sequencing of the Icelandic population. Nature Genetics 2015). The whole-genomes of 2,636 Icelanders were sequenced using Illumina standard TruSeq methodology to a mean depth of at least 10× (median 20×) (Di Angelantonio E, et al., Major lipids, apolipoproteins, and risk of vascular disease. Jama 2009; 302:1993-2000). A total of 35.5 million autosomal SNPs and INDEL's were identified using the Genome Analysis Toolkit version 2.3.9. Information about haplotype sharing was used to improve variant genotyping, taking advantage of the fact that all sequenced individuals had also been chip-typed and long-range-phased. Variants were annotated using Ensembl release 72 and Variant Effect Predictor (VEP) version 2.8. Of the 35.5 million sequence variants found, 25.3 million variants passed the quality threshold and were imputed into 104,220 Icelanders who had been genotyped using Illumina chips. Additionally, using the Icelandic genealogy, genotype probabilities were calculated for 294,212 untyped individuals who are first and second degree relatives of the chip-typed individuals born after 1880 (Gudbartssoon, D F, et al., Large Scale whole-genome sequencing of the Icelandic population. Nature Genetics 2015). The informativeness of genotype imputation (imputation information) was estimated by the ratio of the variance of imputed expected allele counts and the variance of the actual allele counts:

$\frac{\mathrm{Var}\left(E\left(\theta |\mathrm{chip}\mathrm{data}\right)\right)}{\mathrm{Var}\left(\theta \right)},$

where θ is the allele count. Var(E(θ|chip data)) was estimated by the observed variance of the imputed expected counts and Var(θ) was estimated by p(1−p), where p is the allele frequency.

For improved sequencing coverage of the GC-rich intron 4 in ASGR-1 gene, whole-genome sequence (“WGS”) data generated for 738 Icelanders was analyzed using TruSeq PCR-free method from Illumina (mean depth of 30×). This PCR-free method gave much better coverage of GC-rich regions including the ASGR-1 intron 4. The del12 variant in intron 4 of ASGR-1 was detected in five individuals in this dataset.

To provide improved coverage of the associated region (1 Mb centered on ASGR-1), a new dataset was analyzed that included an additional 5,817 WGS individuals (on top of the 2,636 WGS Icelanders). These additional individuals were sequenced with either Illumina TruSeq PCR free or TrueSeq Nano methods. These Illumina TrueSeq methods give enhanced sequence coverage as compared to the standard Illumina TrueSeq method (median sequencing depth 32×). The identified sequence variants were imputed into 150,656 Icelandic chipped-typed individuals, and with the use of genealogy information, into primary and secondary relatives of chip-typed individuals that were un-typed. In this expanded dataset, we identified another rare (0.027%), novel variant, W158X. The W158X variant is a four by INDEL in exon 7 of ASGR-1 (NM_001671.4:c. 469_472dupAACT) that causes frameshift and introduction of premature stop codon at amino acid 158 out of the 291 amino acid full length protein (NP_001662.1:p.Trp158X). A total of 345 individuals were Sanger-sequenced based on the imputation predicted carriers and non-carriers of c. 469_472dupAACT. In this dataset, 79 c. 469_472dupAACT carriers and 270 non-carriers were identified. This genotype data was then used to re-impute the variant into the Icelandic dataset. For non-HDL cholesterol, a larger sample set (n=136,261) was used in the association analysis outlined in Tables 1.4A and 1.4B.

Associations between imputed genotypes and serum lipids (non-HDL cholesterol, HDL cholesterol, LDL cholesterol and triglycerides), ALP and vitamin B12 levels in the Icelandic dataset were tested using a generalized linear regression, assuming an additive genetic model (Gudbjartsson D F, et al., Large-scale whole-genome sequencing of the Icelandic population. Nature genetics 2015; and Steinthorsdottir V, et al., Identification of low-frequency and rare sequence variants associated with elevated or reduced risk of type 2 diabetes. Nature genetics 2014; 46:294-8). All measurements were adjusted for age, sex and measurement site, and average was taken over the available measurements after adjustment and inverse normal transformation. The lipid measurements were further adjusted for statin use. Removing individual known to take lipid lowering drugs in the Icelandic dataset did not alter the association with non-HDL cholesterol. The effect, in standardized units, changed from −0.29 (95% CI −0.38, −0.20; P=4.0×10⁻¹¹) to −0.30 (−0.39, −0.21; P=6.7×10⁻¹¹). This amounted to excluding 16,295 individuals, out of 119,146 individuals with non-HDL cholesterol information.

The lipid, ALP and vitamin B12 measurements from the Danish Inter99 study, ADDITION Denmark screening cohort, and the Nijmegen biomedical study, were adjusted and transformed in the same way and tested for association with allele count of del12 and rs186021206 using the linear regression implemented in the R software package. Results from the different populations were combined using the inverse variance fixed-effects method with METAL (Willer C J, et al., METAL: fast and efficient meta-analysis of genomewide association scans. Bioinformatics 2010; 26:2190-1). Effect estimates from the regression analysis are expressed in units of standard deviation (SD). To obtain effect estimates in mg/dL for non-HDL cholesterol, LDL cholesterol and HDL cholesterol, the estimates from the regression analysis were multiplied by the estimated SD of the population distributions. Triglyceride, ALP and vitamin B12 levels were log-transformed before adjustment as their distributions are approximately log-normal, and the corresponding effect estimates are presented as percentage change.

For the Icelandic dataset, logistic regression was used to test for association between the del12 variant and coronary artery disease and myocardial infarction, treating the disease status as the response and the number of copies of the deletion an individual carries as the explanatory variable. Other available individual characteristics that correlate with disease status were also included in the model as nuisance variables (Gudbjartsson D F, et al., Large-scale whole-genome sequencing of the Icelandic population. Nature genetics 2015). Coronary artery disease case-control association analysis for the non-Icelandic sample sets was done using the NEMO software (Gretarsdottir S, et al., The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nature genetics 2003; 35:131-8) assuming a multiplicative risk model. Results for the Icelandic and the non-Icelandic sample sets were combined using a Mantel-Haenszel fixed-effects model. Heterogeneity in the effect estimate was tested assuming that the estimated odds ratios for different groups follows a log-normal distribution using a likelihood ratio test with degrees of freedom equal to the number of groups compared minus one.

To estimate the effect of the del12 variant on myocardial infarction free survival, we estimated the Kaplan-Meier curves for survival to first myocardial infarction in heterozygous carriers and non-carriers stratified by sex and tested the difference in survival between carriers and non-carriers using the Cox proportional model. The analysis was performed using the survival library in the R software package. The survival analysis was based on 87,718 chip genotyped Icelanders and 44,655 Icelandic first and second degree relatives of chip typed individuals after restricting our analysis to those who lived to be at least 40 years old. Death was treated as a censoring event.

Functional Characterization of the Del12 Variant in ASGR-1

cDNA Preparation, Amplification, Sanger Sequencing and Next Generation Sequencing:

RNA was isolated from blood samples from carriers and non-carriers of del12. Following cDNA generation, the region between exon 3 and 5 in ASGR-1 was PCR amplified and the identified PCR products (two for del12 carriers and one for non-carriers) were Sanger sequenced using standard methodology to determine the sequence difference between the identified cDNA products. To quantify the ratio between the two amplified cDNA PCR products, they were sequenced using Illumina MiSeq instrument coupled with the MiSeq v2 reagent kit.

Western Blot Analysis:

The wild type ASGR-1 cDNA and ASGR-1 cDNA with the 22 bp deletion were transiently overexpressed in HeLa cells to determine if ASGR-1 transcripts with the 22 bp deletion generated stable truncated ASGR-1 protein as evaluated by western blot analysis.

RNA was isolated from blood samples using a Qiagen RNA maxi kit. Concentration and quality of the RNA was determined using an Agilent 2100 Bioanalyzer (Agilent Technologies), all samples had RIN values over 7. Following cDNA generation, the region between exon 3 and 5 in ASGR-1 was PCR amplified using the Advantage® 2 Polymerase kit (Clontech) with the forward primer, CACTCAGGTCCTTCTGCTGTTTC (SEQ ID NO: 32602) and the reverse primer, 5′-ACCTCGCCTCCTCCTGCT-3′ (SEQ ID NO: 32603). The resulting products were resolved on agarose gel and the identified PCR products (two for del12 carriers and one for non-carriers) were Sanger sequenced using standard methodology to determine the sequence difference between the identified cDNA products. To quantitate the ratio between the two amplified cDNA PCR products, they were sequenced using Illumina MiSeq instrument coupled with the MiSeq v2 reagent kit.

Transient Overexpression of Wild Type and Mutated ASGR-1 Harbouring the 22 bp Deletion at the End of Exon 4 in HeLa Cells.

Generation and Cloning of Wild Type and Mutated ASGR-1 cDNA:

cDNA of ASGR-1 was obtained by PCR on human liver marathon ready cDNA (BD biosciences Clontech). The primers used were Forward 5′GCCAGCCCTATCATGACCAA′3 (SEQ ID NO: 32604) and Reverse 5′GCAGGTCGAGGCATTGAAGA′3 (SEQ ID NO: 32605). The resulting cDNA contained all exons including the start and stop codons of ASGR-1. PCR product was run on 1.6% Agarose gel and a band of the correct size was excised out and purified using QIAquick gel extraction kit (QIAGEN 28704) following the manufacturer's protocol. For cloning of ASGR-1 cDNA into pcDNA3.1/V5-His TOPO vector (Invitrogen K4800-01), 20 of the gel extraction product was used and the manufacturer's protocol was followed resulting in pcDNA3.1_ASGR-1_WT. Transformed TOP10 chemically competent cells (Invitrogen C4040-10) were plated on LB plates containing 50 μg/ml ampicillin. Colonies were expanded in 3 ml LB medium containing 50 μg/ml ampicillin. Plasmids were purified using QIAGEN plasmid mini kit (QIAGEN 12125) following the manufacturer's protocol. The plasmid sequence was confirmed by Sanger sequencing using the following sequencing primers: T7: 5′TAATACGACTCACTATAGGG′3 (SEQ ID NO: 32606), BGH: 5′TAGAAGGCACAGTCGAGG′3 (SEQ ID NO: 32607) and ASGR-1: 5′GAGGCAATGTGGGAAGAAAGATG′3 (SEQ ID NO: 32608) Introduction of 22 bp deletion in ASGR-1:

In order to generate a cDNA representative of the del12 carrier mRNA, targeted mutagenesis was performed. The Q5 Site-directed mutagenesis kit (New England BioLabs E0554S) and the pcDNA3.1_ASGR-1_WT plasmid was used as a template. In short, a PCR reaction was performed using the following primers 5′GAGGCAATGTGGGAAGAAAGATGAAGTCG′3 (SEQ ID NO: 32609) and 5′CTGGGCCTCCGTGCTCGC′3 (SEQ ID NO: 32610), resulting in a double-stranded DNA fragment representing the entire pcDNA3.1_ASGR-1_WT plasmid lacking the 22 bp at the end of exon 4. Following the manufacturers recommendation, 1 uL of the PCR reaction was used in the KLD reaction (New England BioLabs E0554S) wherein the PCR fragment is phosphorylated, re-circularized and the non-mutated template plasmid is removed. Mutated plasmids were transformed into NEB 5-alpha Competent cells (New England BioLabs C2987H) and plated on LB plates containing 50 μg/ml ampicillin. Colonies were expanded in 3 ml LB medium containing 50 μg/ml ampicillin. Plasmids were purified using QIAGEN plasmid mini kit (QIAGEN 12125) following the manufacturer's protocol. ASGR-1_22_bp_del sequence was confirmed by Sanger sequencing.

Expression of ASGR-1 in Cultured Cells:

Two days prior to transfection, 100,000 HeLa cells (Public Health England 93021013) were seeded into each well of a 6-well plate in 3 mL of DMEM medium (11995-065, ThermoFisher) supplemented with 10% fetal calf serum (ThermoFisher 10500-064) and 50 units/mL penicillin and 50 ug/mL streptomycin (ThermoFisher 15070-063). Cells were incubated at 37° C. and 5% CO₂ in a humidified incubator.

The day before transfection, media was replaced with the without antibiotics. On the day of transfection, for each transfected well, 2.5 ug of plasmids containing ASGR-1_WT or ASGR-1_del22 cDNA were diluted in 125 uL Opti-Mem medium (ThermoFisher 31985-047) and 5 uL of P3000 reagent (ThermoFisher L3000-008). Next, 3.75 uL Lipofectamine 3000 (ThermoFisher L3000-008) were mixed with 125 uL of Opti-Mem. Subsequently, the diluted plasmid solution was mixed with the Lipofectamine 3000 solution at a 1:1 ratio and incubated at room temperature for 5 minutes before the addition of 250 uL of the combined solution to each transfected well.

24 hours post transfection, the spent media was replaced with fresh without antibiotics. Selected wells were supplemented with 10 uM MG132 (TOCRIS 1748) for 4.5 hours prior to harvesting of cells. 48 hours post transfection cells were harvested for analysis by washing wells 2× with PBS (ThermoFisher 14190-250) followed by an 8 minute incubation with 1 mL of 0.5 mM EDTA in PBS (ThermoFisher 15575-020). Next, the EDTA solution was aspirated and cells dislodged by pipetting of 2 mL of fresh media. 3×6-wells were pooled for each experimental condition and cells were spun down at 300×g for 5 minutes. The equivalent of 2×6-wells were lysed in 200 uL of RIPA buffer for Western blot analysis. The remainder of cells were split in two and lysed in 300 uL RLT buffer (Qiagen 74106) or 900 uL Tissue and Cell lysis solution (Epicentre MTC096H) and snap frozen on dry ice for RNA and DNA extraction respectively. Three different transient expression experiments were done and all gave the same results.

Quantitative PCR Analysis:

RNA was isolated from cells using the RNeasy Mini Kit (Qiagen 74106) according to manufacturer's recommendations, and concentration and quality was determined with Nanodrop 1000 spectrophotometer (Thermo Scientific). cDNA was synthesized using the High capacity cDNA reverse transcriptase kit (ThermoFisher). DNA was isolated from cells using the MasterPure DNA Purification Kit (Epicentre MCD85201) according to manufacturer's recommendation.

Analysis of gene expression and transfection efficiency was performed on total cDNA and DNA respectively, with real-time PCR on an ABI Prism 7900HT Sequence Detection System (ThermoFisher) using forward (AGACCTTCAGCATCTGGACAATG (SEQ ID NO: 32611)) and reverse (CGAGGTCCGGAGCAGAGA (SEQ ID NO: 32612)) primers and fluorescent labelled probe spanning exon junction 2-3 of the ASGR-1 gene (6FAM-CAGAAAAGGGCCACCTC-MGB (SEQ ID NO: 32613) (ThermoFisher). Human betaActin assay (ThermoFisher 4326315E) was run in parallel to verify normalization of input cDNA and DNA.

Western Blot Analysis:

Cells corresponding to two wells of a 6 well plate were lysed using 200 μl of RIPA buffer with 1:100 Halt protease and phosphatase inhibitor cocktail (Thermo Scientific 78442). Lysates were kept on ice for 10 min with agitation followed by sonication for 20 sec (Branson 2510) and additional agitation on ice for 10 min. Lysates were spun down at 4° C. for 15 min at 14,000×g. Total protein amount of lysates was estimated using the Pierce BCA protein assay kit (Thermo Scientific 23227). Samples were prepared using Novex Bolt LDS sample buffer (4×) (Life technologies B0007) and Novex Bolt sample reducing agent (10×) (Life technologies B0009) and run on Novex Nupage 4-12% Bis-Tris gel (Life technologies NP0335BOX). Total protein amount per lane was 24 μg and PageRuler (Thermo scientific 26616) was used to estimate protein size. The gel was run at a constant of 200V for 50 min. Proteins were transferred to a nitrocellulose membrane (Life technologies IB23002) using iBlot2 (Life technologies). Membranes were allowed to dry and were then hydrated with MQ water before blotting. Membranes were blocked for 1 hour at room temperature using Odyssey blocking buffer PBS (Li-Cor 927-40000). Primary antibodies used were α-ASGR-1 (Sigma-Aldrich HPA011954) 1:500 (recognizes amino acid 1-41) and α-beta-actin (Abcam ab6276) 1:5000 incubated in blocking buffer with the addition of 0.1% Tween for 3 hours at room temperature. Secondary antibodies used were α-Rabbit 680RD (Li-Cor 926-68073) and α-Mouse 800CW (Li-Cor 926-32212) both 1:20,000 in PBST+0.01% SDS for 1 hour at room temperature. After washing the membrane it was allowed to dry and then scanned using the Odyssey infrared imaging system (Li-Cor Biosciences).

Other Diseases and Traits in deCODE Database:

The deCODE Genetics phenotype database contains medical information on diseases and traits obtained through collaboration with specialists in each field. This includes information on cardiovascular diseases (e.g., myocardial infarction, coronary arterial disease, peripheral arterial disease, atrial fibrillation, sick sinus syndrome and stroke), metabolic disorders (e.g., obesity, diabetes, and metabolic syndrome), psychiatric disorders (e.g., schizophrenia, bipolar disorder, anxiety and depression), addictions (e.g., nicotine, alcohol), inflammatory diseases (e.g., rheumatoid arthritis, lupus, and asthma), musculoskeletal disorders (e.g., osteoarthritis, osteoporosis), eye diseases (e.g., glaucoma), kidney diseases (e.g., kidney stones, kidney failure) and 29 types of cancer. Anthropometric measures have also been collected through several of these projects. Routinely measured traits from patient workups (e.g., sodium, potassium, bicarbonate, calcium, phosphate, creatinine, blood cell counts, hemoglobin, hematocrit, immunoglobulins, iron, vitamins, lipids, liver function tests and more) were obtained from the Landspitali University Hospital, Reykjavik, and the Icelandic Medical Center Laboratory in Mjodd (Laeknasetrid), Reykjavik. The number of independent and uncorrelated secondary traits tested for association with del12 amounts to 400.

Results

Association of Sequence Variants with Non-HDL Cholesterol Levels

Sequence variants were first identified through whole-genome sequencing (“WSG”) of 2,636 Icelanders to a median depth of 20×. These variants were imputed (assisted by long-range phased haplotypes) into the genomes of 104,220 Icelanders who had been genotyped using Illumina single nucleotide polymorphism (SNP) arrays. In addition, Icelandic genealogical information was used to calculate genotype probabilities for 294,212 close relatives to those genotyped. Using these data we screened for novel rare variants that associated with non-HDL cholesterol levels (n=119,146). A set of seven correlated (pairwise r2>0.7) rare non-coding SNPs on chromosome 17p13.1 associated with non-HDL cholesterol level. The seven variants span 80 kb, including the asialoglycoprotein receptor 1 and 2 (ASGR-1 and ASGR-2) genes. The strongest association was represented by rs186021206 (minor allele frequency (MAF)=0.43%) located downstream of ASGR-1 that associates with 8.9±1.5 mg/dl lowering of non-HDL cholesterol (P=1.4×10-9)(Table 1.4B).

The associated region was well covered by the whole-genome sequencing except for intron 4 of ASGR-1. This intron is 79 base pairs (bp) long and very GC rich. To explore this region further 738 individuals were whole genome sequenced with PCR-free sequencing (Illumina), that gave enhanced coverage of the intron and led to the identification of a 12 bp deletion within the intron; NM_001671.4:c. 284-36_283+33delCTGGGGCTGGGG here after referred to as del12. Following direct genotyping of del12 and imputation into the Icelandic dataset, we observed that del12 (MAF=0.41%) is highly correlated with rs186021206 (r2=0.86) and the six other correlated SNPs and associates even more strongly with lowering of non-HDL cholesterol levels (decrease of 10.2±1.5 mg/dl, P=2.5×10-10) (Table 1.9A). Del12 also increases HDL cholesterol and decreases triglyceride (TG) levels, albeit to a much lesser degree than for non-HDL cholesterol (Tables 1.4A and 1.9B). None of the seven SNPs maintained a significant association with non-HDL cholesterol after adjusting for del12 indicating that del12 is sufficient to explain the non-HDL association.

To validate the del12 association with non-HDL cholesterol levels, del12 in samples from The Netherlands (Nijmegen Biomedical Study18) and Denmark (Danish Inter9919 and Danish Addition study20) were genotyped. Del12 associated with non-HDL cholesterol in each sample set with similar effect size as in Iceland (Table 1.2, Tables 1.4A and 1.4B and Table 1.9B). When all three datasets were combined with the Icelandic discovery data, it was established that del12 lowers non-HDL cholesterol by 11.6±1.5 mg/dl (P=1.0×10-16)(Table 1.9B).

To identify additional loss of function variants in ASGR-1, an extended dataset was screened based on sequence variants identified through whole-genome sequencing (“WSG”) of an additional group of 5,817 WGS Icelanders on top of the 2,636 described above. In this dataset, a rare four by insertion mutation was identified; namely, MAF=0.027%; NM_001671.4:c. 469_472dupAACT. As mentioned throughout, this frameshift mutation introduces a premature stop codon at amino acid 158 out of the 291 amino acid full length protein (NP_001662.1:p.W158X). Potential carriers and non-carriers were directly genotyped using Sanger sequencing. Those genotypes were then used to re-impute p.W158X into 150,656 Icelandic chipped typed individuals and their first and second degree relatives. In this dataset, c. 469_472dupAACT associates significantly with a decrease in non-HDL cholesterol (−21.6 mg/dL, 95% C1-34.2 to −9.6) and an increase in ALP (45.3% increase, 95% CI 20.4 to 68.2, P=7.9×10⁻⁶) (Table 1.8). The direction of the effects of c. 469_472dupAACT and the effect sizes are similar to that of del12 (Table 1.8). Given that a single test was performed, these results provide a significant replication of the ASGR-1 loss of function effect on non-HDL and ALP. Furthermore, since W158X is not correlated with del12 (i.e. there was no overlap between individuals carrying W158X and del12), the W158X variant provides yet further proof that the loss of function in the ASGR-1 gene is responsible for the observed changes in non-HDL, Triglycerides, Alkaline Phosphatase, Ferritin and Vitamin B12 levels. For coronary artery disease, the odds ratio for W158X (c. 469_472dupAACT) was 0.65 (95% CI 0.26 to 1.40; P=0.24). As mentioned above, the W158X (c. 469_472dupAACT) variant is independent of del12 and none of the 79 carriers found in Iceland carried del12. The variant also appears to be specific to the Icelandic population as it is not detected in large population databases such as (Exome Aggregation Consortium (ExAC), Exome Variant Server (EVS), Genomes of the Netherlands (GoNL) and dbSNP.

Del12 within Intron 4 of ASGR-1 Causes a Splicing Error Resulting in a Frameshift

Since del12 is located in intron 4 of ASGR-1, we examined its effect on splicing between exons 4 and 5. The region between exon 3 and 5 in cDNA generated from blood samples from 12 non-carriers and 12 heterozygous carriers of del12 was PCR amplified (FIG. 4). The PCR products were resolved by gel electrophoresis demonstrating a band of 239 bp in non-carrier. In del12 carriers, however, a smaller 217 bp band was noted in addition to the expected 239 bp PCR product (FIG. 4B). Upon Sanger sequencing of the cDNA products we identified in the 217 bp cDNA fragment a 22 bp deletion at the end of exon 4 (FIG. 4C). The deletion of these 22 bp from the ASGR-1 transcript appears to be driven by a pseudo 5′-splice site in exon 4 (FIG. 4D). It causes a frameshift in carriers such that, if translated, the resulting protein would lack both the oligomerization and carbohydrate recognition domains. To quantify this splicing defect we used the Illumina TruSeq method for direct digital counting of sequencing reads that were generated by sequencing the two cDNA products found in del12 carriers. On average, 32±13% of the total ASGR-1 transcripts were accounted for by the incorrectly spliced isoform (FIG. 4E). This form could not be detected in non-carriers (FIG. 4E). Together, these data identify ASGR-1 as the target gene for the non-HDL association at this locus and are consistent with the associated mutation, del12, disrupting the function of the ASGR-1 protein. ASGR-1 is the major subunit of the hepatic asioaloglycoprotein receptor (ASGR) known to recognize and mediate the endocytosis and degradation of a wide variety of desialylated glycoproteins that contain terminal galactose (Gal) or N-acetylgalactosamine (Gal-NAc) residues on their N-linked carbohydrate chains (Morell A G, Gregoriadis G, Scheinberg I H, Hickman J, Ashwell G. The role of sialic acid in determining the survival of glycoproteins in the circulation. The Journal of biological chemistry 1971; 246:1461-7; Van Den Hamer C J, Morell A G, Scheinberg I H, Hickman J, Ashwell G. Physical and chemical studies on ceruloplasmin. IX. The role of galactosyl residues in the clearance of ceruloplasmin from the circulation. The Journal of biological chemistry 1970; 245:4397-402; Ashwell G, Harford J. Carbohydrate-specific receptors of the liver. Annual review of biochemistry 1982; 51:531-54; Weigel P H. Galactosyl and N-acetylgalactosaminyl homeostasis: a function for mammalian asialoglycoprotein receptors. BioEssays: news and reviews in molecular, cellular and developmental biology 1994; 16:519-24).

The Del12 Variant in ASGR-1 and Risk of Coronary Artery Disease

Given the effect of del12 on non-HDL cholesterol levels, its impact on risk of CAD in 33,090 cases and 236,254 controls from Iceland and 8,558 cases and 11,120 controls from the USA, the UK, New Zealand and Denmark was assessed. It was found that carriers of del12 have a lower risk of CAD than non-carriers (odds ratio 0.66; 95% confidence interval [CI] 0.55 to 0.79; P=6.3×10-6) (FIG. 5A). There was no evidence of heterogeneity across the eight study populations (Phet=0.96). Del12 also decreases risk of MI in Iceland (hazard ratio 0.64; 95% CI, 0.64 to 0.80; P=8.5×10-5) (FIG. 5B). In addition, del12 carriers have a 1.5 years longer lifespan than non-carriers (95% CI, 0.2 to 2.8 years; P=0.020).

There is a strong positive correlation between the effect of sequence variants on non-HDL cholesterol levels and risk of CAD (Haddad L, Day I N, Hunt S, Williams R R, Humphries S E, Hopkins P N. Evidence for a third genetic locus causing familial hypercholesterolemia. A non-LDLR, non-APOB kindred. Journal of lipid research 1999; 40:1113-22; Timms K M, Wagner S, Samuels M E, et al. A mutation in PCSK9 causing autosomal-dominant hypercholesterolemia in a Utah pedigree. Human genetics 2004; 114:349-53; Varret M, Rabes J P, Saint-Jore B, et al. A third major locus for autosomal dominant hypercholesterolemia maps to 1p34.1-p32. American journal of human genetics 1999; 64:1378-87; Hunt S C, Hopkins P N, Bulka K, et al. Genetic localization to chromosome 1p32 of the third locus for familial hypercholesterolemia in a Utah kindred. Arterioscler Thromb Vasc Biol 2000; 20:1089-93; Do R, Willer C J, Schmidt E M, et al. Common variants associated with plasma triglycerides and risk for coronary artery disease. Nature genetics 2013; 45:1345-52) (FIG. 6, Table 1.5). However, several published variants, deviate from the overall trend. For example, LPA and ANGPTL4 variants have a substantially greater effect on CAD than their non-HDL effects would predict while the effect of the APOE variants is weaker than predicted by the non-HDL effect. Del12 in ASGR-1 is another example of a variant whose effect on CAD is stronger than predicted by the effect non-HDL cholesterol effect (FIG. 6, Table 1.5).

Association of Del12 with Serum Levels of Alp and Vitamin B12

To determine the overall effect of del12 in ASGR-1, its effect on a variety of human diseases and other traits in the Icelandic dataset was screened. A highly significant association of del12 with higher levels of circulating alkaline phosphatase (ALP) (33.6±2.8 U/L increase, P=3.6×10-63) and vitamin B12 (58.4±8.3 pmol/L increase, P=3.1×10-12) was observed (Tables 8A and 8B and Table 18). An increase in ALP levels may reflect liver disease, however, there was no increase in del12 carriers in serum gamma glutamyl transferase (GGT), bilirubin, alanine aminotransferase or other measures of liver function that commonly parallel changes in ALP in liver disease (Table 1.6).

The del12 association with higher levels of ALP and vitamin B12 in individuals from the Danish Inter99 study with comparable effect sizes (P=9.9×10-69 for ALP and P=9.9×10-14 for vitamin B12) was replicated (Table 1.10).

A common variant upstream of ASGR-1 (rs314253; MAF=35.1%) has been reported to associate modestly with both LDL cholesterol and ALP levels (Chambers J C, Zhang W, Sehmi J, et al. Genome-wide association study identifies loci influencing concentrations of liver enzymes in plasma. Nature genetics 2011; 43:1131-8; Willer C J, Schmidt E M, Sengupta S, et al. Discovery and refinement of loci associated with lipid levels. Nature genetics 2013; 45:1274-83). This common variant association is replicated in the data of the present invention (strongest association for both ALP and non-HDL with the correlated rs56093546; MAF=21.6%) and that its associations with ALP and non-HDL are independent of the rare signal represented by del12 (r2<0.001, Table 1.5) as demonstrated. As for del12, this common variant has opposite effects on ALP and non-HDL; the allele that increases ALP decreases non-HDL (see Chambers; Willer) (Table 1.7).

TABLE 1.1
		Definition of CAD and MI
Study	Design	cases	Assertainment of controls	Reference
Iceland	Case/control	CAD and MI cases were	Study participants from	Helgadottir A,
		defined by: a) discharge	various deCODE genetics	Thorleifsson G,
		diagnoses (ICD 9 codes	programs without known	Manolescu A,
		410.*, 411.*, 412.*, 414.*	CVD.	et al. A
		or ICD 10 codes I20.0,		common
		I21.*, I22.*. I23.*, I24.*,		variant on
		I25.*) from LUH, b)		chromosome
		significant angiographic		9p21
		CAD (≧50% stenosis of the		affects the
		major coronary vessels),		risk of
		c) undergone coronary		myocardial
		revascularisation (CABG)		infarction.
		d) MI or CAD (ICD 9 or 10		Science
		codes) listed in death		(New York,
		registries, or e) MI before		NY)
		the age of 75 from		2007; 316: 1491-3.
		MONICA registry
UK 1 -	Case/control	Cases included MI patients	Controls included adult	Helgadottir A,
Leicester MI		admitted to the coronary	visitors of individuals with	Manolescu A,
Study		care units of the Leicester	non-cardiovascular	Thorleifsson G,
		Royal Infirmary, Leicester	disease from each hospital	et al. The
		and the Royal Hallamshire	or individuals from three	gene
		Hospital, Sheffield and	primary care practices	encoding 5-
		satisfied the WHO criteria	located in the same	lipoxygenase
		for acute MI.	geographical area.	activating
			Individuals who reported a	protein
			history of CAD were	confers risk
			excluded.	of
				myocardial
				infarction
				and stroke.
				Nature
				genetics
				2004; 36: 233-9.
UK2 - BHF	Case/control	The British Heart	Controls were blood	Genome-
Family Heart		Foundation Family Heart	donors recruited by the	wide
Study		Study (BHF-FHS) CAD	United Kingdom Blood	association
		cases were index cases	Service (UKBS) as part of	study of
		from families of European	the Wellcome Trust Case	14,000
		ancestry with a strong	Control Consortium Study.	cases of
		familial history of defined		seven
		CAD recruited from		common
		throughout the United		diseases
		Kingdom. CAD was		and 3,000
		defined as a validated		shared
		history of myocardial		controls.
		infarction or coronary		Nature
		revascularisation (PTCA or		2007; 447: 661-78,
		CABG) before the 66th		and
		birthday.		Samani N J,
				Erdmann J,
				Hall AS, et
				al.
				Genomewide
				association
				analysis of
				coronary
				artery
				disease.
				The New
				England
				journal of
				medicine
				2007; 357: 443-53.
Emory	Case/control	Cases were identified from	Controls included	Helgadottir A,
(Atlanta,		subjects undergoing	individuals undergoing	et al.
Georgia,		cardiac catheterization at	cardiac catheterization	(2007)
USA)		the Emory University	with no or minimal CAD
		Hospital. CAD cases	(<20% stenosis) and had
		included those that had at	no prior history of MI or
		least one significant	CAD. Additional controls
		stenosis (≧50%) in any of	were recruited from the
		the major coronary	Grady Memorial Hospitals
		arteries on angiography,	and Clinical Registry in
		or those without	Neurology (CRIN) and
		significant stenosis but	included individuals with
		had history of MI, CABG,	non-vascular neurological
		or PCI.	diseases (mainly
			Parkinson's and
			Alzheimer's diseases),
			their spouses, unrelated
			friends and community
			volunteers; excluding
			those with a known
			history of CAD.
Duke	Case/control	Participants were enrolled	Controls included those	Helgadottir A,
(Durham,		at Duke University Medical	with no history of MI prior	et al.
North		Center through the	or subsequent to the	(2007)
Carolina,		cardiac catheterization	index cardiac
USA)		laboratories. MI cases	catheterization and no PCI
		included those with self-	or CABG ejection fraction
		reported history of MI	on left ventriculogram
		(corroborated by review	greater than 40%, and
		of medical records), or	stenosis less than 50% on
		those who suffered an MI	coronary angiography.
		during the study follow-up
		period.
UPenn	Case/control	The study participants	Controls included	Helgadottir A,
(Philadelphia,		were enrolled at the	individuals without	et al.
Pennsylvania,		University of Pennsylvania	significant luminal stenosis	(2007)
USA)		Medical Center and	on coronary angiography
		included subjects	(luminal stenosis less than
		undergoing cardiac	50%).
		catheterization. CAD cases
		included those that had at
		least one significant
		stenosis (≧50%) in any of
		the major coronary
		arteries on angiography,
		or those without
		significant stenosis but
		had history of MI, CABG,
		or PCI.
New Zealand	Case/control	a) Significant angiographic	Study participants without	Gretarsdottir S,
		CAD (≧50% stenosis of the	known CAD and	Baas A F,
		major coronary vessels),	ultrasound screened for	Thorleifsson G,
		b) CABG-procedures c) MI	carotid artery disease and	et al.
		or CAD (ICD 9 or 10 codes)	abdominal aortic	Genome-
		in a clinical registry.	aneurysm, with ankle	wide
			brachial index to exclude	association
			peripheral artery disease.	study
				identifies a
				sequence
				variant
				within the
				DAB2IP
				gene
				conferring
				susceptibility
				to
				abdominal
				aortic
				aneurysm.
				Nature
				genetics
				2010; 42: 692-7.
Denmark 1	Case/control	Cases were identified from	Individuals in Monica10
(Gentofte		subject investigated by	and Inter99 studies
cadlab)		coronary artery	without CAD diagnosis
		angiography because of	based on information
		suspected ischemic heart	from the Danish National
		disease, valvular heart	Patient Registry and the
		disease or	Danish Register of Causes
		cardiomyopathy. CAD	of Death.
		cases included those that
		had at least one significant
		stenosis (≧50%) in any of
		the major coronary
		arteries on angiography
Denmark 2	Case/control	Monica10 is a population	Individuals in Monica10	Olsen M H,
(Monica10)		based study. Participants	and Inter99 studies	Hansen T W,
		were recruited from the	without CAD diagnosis	Christensen M K,
		Danish Central Personal	based on information	et al.
		Register as random	from the Danish National	N-terminal
		samples of the population	Patient Registry and the	pro-brain
		in the southern part of the	Danish Register of Causes	natriuretic
		former Copenhagen	of Death.	peptide,
		County. Cardiovascular		but not high
		events were defined as		sensitivity
		first ever non-fatal or fatal		C-reactive
		CVD (ICD-8: 390-448/ICD-		protein,
		10: I00-I79). Assessment		improves
		of the cardiovascular		cardiovascular
		endpoints was based on		risk
		data from the Danish		prediction
		National Patient Registry		in the
		and the Danish Register of		general
		Causes of Death.		population.
				European
				heart
				journal
				2007; 28: 1374-81.
Denmark 3	Case/control	The Inter99 study is a	Individuals in Monica10	14.
(Inter99)		population-based	and Inter99 studies	Jorgensen A B,
		randomized controlled	without CAD diagnosis	Frikke-
		trial (CT00289237,	based on information	Schmidt R,
		ClinicalTrials.gov)	from the Danish National	Nordestgaard B G,
		investigating the effects of	Patient Registry and the	Tybjaerg-
		lifestyle intervention on	Danish Register of Causes	Hansen A.
		cardiovascular disease.	of Death.	Loss-of-
		Cardiovascular events		function
		were defined as first ever		mutations
		non-fatal or fatal CVD		in APOC3
		(ICD-8: 390-448/ICD-10:		and risk of
		I00-I79). Assessment of		ischemic
		the cardiovascular		vascular
		endpoints was based on		disease.
		data from the Danish		The New
		National Patient Registry		England
		and the Danish Register of		journal of
		Causes of Death.		medicine
				2014; 371: 32-41.
Sweden	Case/Control	Ischemic stroke patients	Population-based	Gretarsdottir
		from the clinic at	controls, either healthy	et al
		Karolinska Univerity	blood donors or healthy	(2008)
		Hospital, Stockholm. The	volunteers recruited at the	Traylor et al
		ischemic stroke diagnosis	Karolinska Hospital	(2012)
		was based on clinical
		findings and brain imaging
		(CT or MRI).
South	Case/Control	Ischemic stroke patients	Gender and age matched	Traylor et al
Germany		recruited at the stroke	individuals without history	(2008)
		unit of the Department of	of cardiovascular disease	Gschwendtner
		Neurology, Klinikum	selected from the KORA S4	et al
		Grosshadern, University of	Study	(2009)
		Munich. Diagnoses were		Wichmann
		based on clinical findings		et al (2005)
		and imaging evidence
		(either CT or MRI), and
		were clinically confirmed
		by neurologists.
West Germany	Case/Control	Ischemic stroke patients	Population controls with a	Traylor et al
		recruited through hospitls	self-reported history of	(2008)
		participating in the regional	stroke from the population	Berger et al
		Westphalian Stroke Register.	based Dortmund Health	(2007)
		Diagnoses were based on	Study
		clinical findings and imaging
		evidence (either CT or MRI),
		and were clinically confirmed
		by neurologists.
United	Case/Control	Ischemic stroke patients	Community controls, age	Traylor et al
Kingdom		recruited through a	and gender matched and	(2008)
		cerebrovascular service	free of symptomatic	Gschwendtner
		clinic. All cases were	cerebrovascular disease	et al
		phenotyped by one	were recruited from the	(2009)
		experienced stroke	same geographic area as
		neurologist with review of	the patients.
		original brain imaging with
		CT or MRI.

TABLE 1.2
Characteristics of Participants in the Discovery and Replication Studies of the association
of del12 Variant with Plasma Lipid, Alkaline Phosphatase, and Vitamin B12 levels
		Nijmegen
		Biomedical Study	Inter99 study	Addition Study
Traita	Iceland	(Netherlands)c	(Denmark)d	(Denmark)e
Ancestry	Caucasian	Caucasian	Caucasian	Caucasian
Nb	194,958	5,645	7,633	9,689
Mean age (SD), yrs	58.2 (40.6-75.8)	55.8 (38.0-73.6)	48.5 (36.1-55.5)	59.9 (53.1-66.7)
Gender, % female	53.4%	53.6%	49.9%	46.4%
Non-HDL cholesterol	154.7 (109.1-200.3)	170.7 (129.4-212.0)	161.6 (117.5-205.7)	164.7 (124.0-205.4)
(SD), mg/dL
LDL cholesterol (SD),	133.0 (91.6-174.4)	138.6 (102.2-175.0)	137.2 (99.7-174.7)	139.3 (101.9-176.1)
mg/dL
HDL cholesterol (SD),	54.7 (37.7-71.7)	52.6 (39.2-66.0)	54.2 (38.4-70.0)	60.0 (43.6-76.4)
mg/dL
Total Cholesterol	208.0 (162.6-253.4)	223.4 (180.9-265.9)	215.8 (173.6-258.0)	224.7 (183.9-265.5)
(SD), mg/dL
Triglycerides (SD),	133.6 (67.6-190.5)	155.8 (94.5-256.8)	105.8 (60.8-183.9)	117.4 (73.5-187.3)
mg/dL
Alkaline phosphatase	87.1 (53.5-141.7)	na	41.3 (30.7-55.6)	na
(SD), IU/l
Vitamin B12 (SD),	398 (256-618)	na	398 (286-554)	na
pmol/l
aThe average values (where available) for each of the traits listed is shown (±one SD).
bNumber of individuals with measurements for at least one of the traits.
cWetzels et al (2007)5,
dJörgensen et al (2003)6,
eLauritzen et al (2000)7.

TABLE 1.4A
Association of del12 with Non-HDL Cholesterol, LDL Cholesterol, HDL Cholesterol,
Triglyceride, ALP and Vitamin B12 in Iceland, Denmark and The Netherlands
					Population mean
	Study population (n)		Effect (95% CI)a	P value	valuee (±1SD)
		del12 freq.
	Non-HDL cholesterol	(%)	mg/dL		mg/dL
Discovery	Iceland (119,146)	0.41	−13.6	(−17.7, −9.4)	2.5 × 10−10	154.7	(109.1-200.3)
Replication	Denmark Ab (6,182)	0.22	−21.3	(−36.8, −5.9)	0.0069	161.6	(117.5-205.7)
Replication	Denmark Bc (9,656)	0.32	−22.2	(−32.8, −11.7)	3.8 × 10−5	164.7	(124.0-205.4)
Replication	The Netherlandsd (5,537)	0.50	−17.0	(−28.3, −5.7)	0.0032	170.7	(129.4-212.0)
	Combined		−15.3	(−18.9, −11.7)	1.0 × 10−16
	LDL cholesterol	mg/dL
Discovery	Iceland (53,841)	0.41	−9.5	(−14.0, −5.1)	2.8 × 10−5	133.0	(91.6-174.4
Replication	Denmark A(6,098)	0.22	−22.1	(−35.5, −8.7)	0.0012	137.2	(99.7-174.7)
Replication	Denmark B (8,080)	0.32	−19.0	(−29.2, −8.8)	0.00026	139.3	(101.9-176.1)
Replication	The Netherlands (5,523)	0.50	−16.0	(−26.1, −6.0)	0.0018	138.6	(102.2-175.0)
	Combined		−12.5	(−16.2, −8.8)	3.9 × 10−11
	HDL cholesterol	mg/dL		mg/dL
Discovery	Iceland (119,514)	0.41	2.4	(0.7, 4.1)	0.0058	54.7	(37.7-71.7)
Replication	Denmark A (6,182)	0.22	4.6	(−0.8, 9.9)	0.096	54.2	(38.4-70.0)
Replication	Denmark B (9,656)	0.32	2.4	(−1.8, 6.7)	0.26	60.0	(43.6-76.4)
Replication	The Netherlands (5,537)	0.50	2.4	(−1.3, 6.0)	0.20	52.6	(39.2-66.0)
	Combined		2.5	(1.1, 4.0)	0.00039
	Triglyceride	% change		mg/dL
Discovery	Iceland (80,011)	0.41	−6.1	(−10.8, −1.5)	0.012	133.6	(67.6-190.5)
Replication	Denmark A (6,182)	0.22	−6.0	(−25.2, 11.4)	0.53	105.8	(60.8-183.9)
Replication	Denmark B (8,163)	0.32	−8.9	(−21.0, 2.3)	0.15	117.4	(73.5-187.3)
Replication	The Netherlands (5,537)	0.50	−4.4	(−17.9, 8.2)	0.52	155.8	(94.5-256.8)
	Combined		−6.3	(−10.3, −2.3)	0.0032
	ALP	% change		U/L
Discovery	Iceland (126,060)	0.41	50.1	(42.9, 57.2)	3.6 × 10−63	87.1	(53.5-141.7)
Replication	Denmark Ac (5,829)	0.22	29.1	(14.8, 42.5)	3.1 × 10−6	41.3	(30.7-55.6)
	Combined		46.5	(40.1, 52.7)	5.6 × 10−69
	Vitamin B12	% change		pmol/L
Discovery	Iceland (97,910)	0.41	16.6	(11.5, 21.5)	3.1 × 10−12	398	(256-618)
Replication	Denmark Ac (5,826)	0.22	18.6	(3.9, 32.4)	0.0053	398	(286-554)
	Combined		16.8	(12.0, 21.5)	8.3 × 10−14
aEffect estimates and 95% confidence intervals (95% CI) in mg/dL for the non-HDL cholesterol and HDL cholesterol and as percentage change for triglyceride, ALP and vitamin B12.
bThe Danish Inter99 study (Jørgensen et al. 2003).
cThe Danish Addition study (van den Donk et al. 2011).
dThe Nijmegen Biomedical Study (Hoogendoorn et al. 2006).
eFor triglyceride, ALP and vitamin B12, the population mean and the SD are calculated for log-transformed values and transformed back to original units. To convert the values for non-HDL and HDL cholesterol to millimoles per liter, multiply by 0.02586. To convert triglyceride to mmol/L, multiply by 0.01129.

TABLE 1.4B
Association of del12 and rs186021206 with Cholesterols, Triglyceride, Alkaline Phosphatase and
Vitamin B12 Measurements in Iceland, Denmark and the Netherlands.
	rs186021206	del12
Trait/Cohort (n)a	Effectb	Effect (95% CI)c	P	Padjd	Effectb	Effect (95% CI)c	P
Non-HDL
cholesterol	SD	mg/dL				mg/dL
Iceland	−0.28	−12.9 (−17.1, −8.7)	1.4 × 10−9	0.39	−0.30	−13.6 (−17.7, −9.4)	2.5 × 10−10
(119,146)
Denmark A	−0.38	−16.7 (−27.9, −5.4)	0.0038	0.64	−0.48	−21.3 (−36.8, −5.9)	0.0069
(6,182)
Denmark B	−0.32	−13.1 (−21.0, −5.3)	0.0011	0.74	−0.55	−22.2 (−32.8, −11.7)	3.8 × 10−5
(9,656)
The Netherlands	−0.23	−9.7 (−19.9, 0.5)	0.062	0.19	−0.41	−17.0 (−28.3, −5.7)	0.0032
(5,537)
Combined	−0.29	−12.9 (−16.3, −9.6)	2.0 × 10−14	0.24	−0.34	−15.3 (−18.9, −11.7)	1.0 × 10−16
LDL cholesterol		mg/dL				mg/dL
Iceland	−0.22	−9.2 (−13.6, −4.7)	5.5 × 10−5	0.78	−0.23	−9.5 (−14.0, −5.1)	2.8 × 10−5
(53,841)
Denmark A	−0.43	−16.1 (−25.8, −6.3)	0.0012	0.56	−0.59	−22.1 (−35.5, −8.7)	0.0012
(6,098)
Denmark B	−0.34	−12.5 (−20.3, −4.7)	0.0016	0.86	−0.51	−19.0 (−29.2, −8.8)	0.00026
(8,080)
The Netherlands	−0.36	−13.2 (−22.3, −4.2)	0.0041	0.81	−0.44	−16.0 (−26.1, −6.0)	0.0018
(5,523)
Combined	−0.28	−11.1 (−14.5, −7.8)	1.0 × 10−10	0.70	−0.31	−12.5 (−16.2, −8.8)	3.9 × 10−11
Total cholesterol		mg/dL				mg/dL
Iceland	−0.22	−9.9 (−14.0, −5.7)	3.1 × 10−6	0.78	−0.23	−10.5 (−14.7, −6.4)	6.5 × 10−7
(125,381)
Denmark A	−0.32	−13.5 (−24.2, −2.8)	0.014	0.54	−0.33	−14.0 (−28.7, 0.8)	0.063
(6,182)
Denmark B	−0.30	−12.0 (−19.9, −4.2)	0.0027	0.97	−0.47	−19.2 (−29.8, −8.6)	0.00040
(9,656)
The Netherlands	−0.21	−9.0 (−19.5, 1.5)	0.0927	0.48	−0.33	−14.1 (−25.7, −2.5)	0.018
(5,537)
Combined	−0.24	−10.5 (−13.8, −7.2)	5.1 × 10−10	0.68	−0.27	−12.0 (−15.6, −8.5)	5.6 × 10−11
HDL cholesterol		mg/dL				mg/dL
Iceland	0.13	2.2 (0.5, 3.9)	0.011	0.0055	0.14	2.4 (0.7, 4.1)	0.0058
(119,514)
Denmark A	0.15	2.4 (−1.5, 6.4)	0.22	0.84	0.29	4.6 (−0.8, 9.9)	0.096
(6,182)
Denmark B	0.03	0.4 (−2.7, 3.6)	0.79	0.32	0.15	2.4 (−1.8, 6.7)	0.26
(9,656)
The Netherlands	0.02	0.2 (−3.1, 3.5)	0.9	0.043	0.18	2.4 (−1.3, 6.0)	0.20
(5,537)
Combined	0.10	1.6 (0.4, 2.9)	0.01	0.001	0.15	2.5 (1.1, 4.0)	0.00039
Triglyceride		% change				% change
Iceland	−0.11	−5.4 (−10.1, −0.8)	0.027	0.13	−0.12	−6.1 (−10.8, −1.5)	0.012
(80,011)
Denmark A	−0.26	−13.4 (−26.1, −1.6)	0.046	0.11	−0.11	−6.0 (−25.2, 11.4)	0.53
(6,182)
Denmark B	−0.03	−1.3 (−11.2, 8.0)	0.79	0.099	−0.2	−8.9 (−21.0, 2.3)	0.15
(8,163)
The Netherlands	0.13	6.5 (−7.0, 19.1)	0.32	0.0057	−0.09	−4.4 (−17.9, 8.2)	0.52
(5,537)
Combined	−0.09	−4.2 (−7.9, −0.6)	0.028	0.0066	−0.13	−6.3 (−10.3, −2.3)	0.003
ALP		% change				% change
Iceland	0.82	48.9 (41.8, 55.8)	1.2 × 10−61	0.10	0.84	50.1 (42.9, 57.2)	3.6 × 10−63
(126,060)
Denmark A	0.70	23.0 (13.2, 32.4)	2.2 × 10−7	0.092	0.86	29.1 (14.8, 42.5)	3.1 × 10−6
(6,035)
Combined	0.80	41.5 (35.9, 47.0)	1.9 × 10−67	0.026	0.84	46.5 (40.1, 52.7)	5.6 × 10−69
Vitamin B12		% change				% change
Iceland	0.33	15.8 (10.8, 20.7)	2.0 × 10−11	0.15	0.35	16.6 (11.5, 21.5)	3.1 × 10−12
(97,910)
Denmark A	0.49	17.6 (7.2, 27.7)	0.00027	0.011	0.52	18.6 (3.9, 32.4)	0.0053
(6,032)
Combined	0.35	16.1 (11.6, 20.6)	4.3 × 10−14	0.84	0.36	16.8 (12.0, 21.5)	8.3 × 10−14
aNumber of individuals with trait value and genotypes.
bEffect estimates from the regression in units of standard deviations (SD) of the distributions of the adjusted values.
cEffect estimates and 95% confidence intervals (95% CI) in mg/dL for the cholesterol, and as percentage change for triglyceride, ALP and vitamin B12.
dP-values adjusted for the effect of del12. “The Netherlands”, The Nijmegen Biomedical Study15; “Denmark A”, The Danish Inter99 study6; “Denmark B”, The Danish Addition study16.

TABLE 1.5
The association of published lipid variants with non-HDL
cholesterol levels and coronary artery disease in Iceland.
			Coronary
Build 36			artery
position		Non-HDL)	disease
	Position		(mg/dL)		95%
Chr	(hg18)	MAF	Info	Effect	SE	OR	CI
1	25,641,524	0.47184	0.996	0.7	0.2	0.99	0.97	1.02
1	55,278,235	0.01173	0.986	−17.2	1.0	0.73	0.66	0.81
1	62,725,961	0.21814	0.996	1.6	0.3	1.01	0.98	1.03
1	62,906,518	0.33844	0.998	−2.3	0.2	0.99	0.97	1.01
1	92,766,395	0.19052	0.999	0.8	0.3	0.99	0.97	1.02
1	109,620,053	0.20789	0.999	4.8	0.3	1.08	1.06	1.11
1	110,000,250	0.41287	0.995	1.0	0.2	1.01	0.99	1.03
1	149,225,460	0.15162	0.997	−0.7	0.3	1.03	1.00	1.06
1	154,967,275	0.28892	0.998	−0.5	0.2	0.99	0.97	1.02
1	219,036,651	0.28689	0.994	0.9	0.2	1.01	0.98	1.03
1	228,362,314	0.39128	0.999	−1.1	0.2	0.99	0.97	1.01
1	232,915,962	0.4424	0.999	1.2	0.2	1.00	0.98	1.03
2	21,087,477	0.04518	0.999	−6.1	0.5	0.94	0.89	0.99
2	21,117,405	0.3491	0.997	2.9	0.2	1.05	1.03	1.07
2	21,139,562	0.1408	0.999	4.3	0.3	1.08	1.04	1.11
2	27,584,444	0.34466	0.998	−1.8	0.2	1.00	0.98	1.03
2	27,584,716	0.20151	0.995	−1.4	0.3	1.00	0.97	1.02
2	43,927,385	0.27892	0.999	−2.6	0.2	0.95	0.93	0.98
2	43,953,086	0.19027	0.997	−1.5	0.3	0.96	0.94	0.99
2	63,003,061	0.32014	0.997	0.9	0.2	1.02	1.00	1.05
2	118,293,189	0.07895	0.998	−0.8	0.4	1.02	0.98	1.06
2	121,025,958	0.41077	0.994	0.6	0.2	1.03	1.01	1.06
2	169,538,401	0.37685	0.999	−0.5	0.2	0.99	0.97	1.01
2	216,012,629	0.32322	0.998	0.8	0.2	0.95	0.93	0.97
3	12,271,469	0.3667	0.998	−1.2	0.2	0.99	0.97	1.02
3	32,508,014	0.07924	0.997	−1.6	0.4	0.98	0.94	1.02
3	133,691,893	0.11977	0.998	−1.1	0.3	0.99	0.96	1.03
3	172,209,912	0.07646	0.999	0.8	0.4	1.08	1.04	1.12
4	3,442,937	0.40281	0.991	0.7	0.2	1.03	1.00	1.05
4	25,672,088	0.14802	0.993	0.9	0.3	1.04	1.01	1.07
4	88,249,285	0.40279	0.999	0.7	0.2	1.00	0.98	1.02
4	100,233,828	0.42298	0.998	0.5	0.2	1.01	0.99	1.03
5	74,661,243	0.35407	0.999	2.8	0.2	1.04	1.02	1.06
5	122,883,315	0.47211	0.995	0.5	0.2	1.00	0.98	1.02
5	156,322,875	0.35741	0.998	1.7	0.2	1.01	0.99	1.03
6	16,217,142	0.46163	0.995	−0.8	0.2	0.99	0.97	1.01
6	26,201,120	0.06713	1.000	−1.5	0.4	0.99	0.95	1.03
6	31,373,469	0.29084	0.993	0.8	0.2	1.02	1.00	1.04
6	43,865,874	0.47286	0.993	0.9	0.2	1.02	1.00	1.04
6	100,706,818	0.19956	0.998	−1.0	0.3	1.00	0.97	1.02
6	116,444,196	0.40848	0.998	−0.6	0.2	0.98	0.96	1.00
6	127,494,332	0.47183	0.999	0.9	0.2	1.01	0.99	1.03
6	139,873,450	0.42692	0.999	−0.7	0.2	0.98	0.96	1.00
6	160,881,127	0.01773	1.000	4.0	0.8	1.31	1.21	1.41
6	160,930,108	0.06104	0.984	2.3	0.4	1.27	1.22	1.33
7	21,573,877	0.22512	0.992	1.5	0.3	1.00	0.98	1.02
7	25,958,351	0.14423	0.993	0.9	0.3	1.05	1.02	1.08
7	44,548,856	0.2013	0.990	2.0	0.3	1.02	1.00	1.05
7	44,567,220	0.42549	0.998	−1.2	0.2	0.97	0.95	0.99
7	72,620,810	0.11552	0.998	−0.9	0.3	1.02	0.99	1.06
7	72,697,942	0.46468	0.997	0.5	0.2	0.99	0.97	1.01
7	130,095,474	0.44163	0.998	−0.5	0.2	0.96	0.94	0.98
8	9,221,641	0.07554	0.997	1.9	0.4	1.04	1.00	1.08
8	18,316,718	0.18705	0.996	−1.3	0.3	0.96	0.94	0.99
8	19,888,502	0.08181	0.996	−2.1	0.4	0.93	0.89	0.97
8	19,910,123	0.45471	0.996	−1.0	0.2	0.96	0.94	0.98
8	55,584,167	0.24432	1.000	1.0	0.2	1.02	0.99	1.04
8	59,548,473	0.31037	0.998	−1.4	0.2	0.99	0.97	1.01
8	116,733,072	0.26318	0.999	−1.1	0.2	1.00	0.97	1.02
8	126,543,488	0.22755	0.997	−1.9	0.3	0.96	0.94	0.99
8	126,551,803	0.49199	0.999	−2.3	0.2	0.95	0.93	0.97
8	145,094,645	0.385	0.990	0.7	0.2	0.98	0.96	1.00
9	2,630,759	0.09898	0.998	−1.3	0.4	0.97	0.94	1.01
9	16,894,846	0.31865	0.998	−0.5	0.2	0.97	0.95	0.99
9	106,704,122	0.25781	0.999	−1.1	0.2	0.97	0.95	0.99
9	106,724,051	0.28833	0.997	−0.6	0.2	0.99	0.97	1.02
9	135,122,694	0.38646	0.997	−0.9	0.2	0.99	0.97	1.01
9	135,143,989	0.15248	0.995	1.0	0.3	1.05	1.02	1.08
10	94,829,632	0.42892	0.993	−0.6	0.2	0.99	0.97	1.01
11	18,612,847	0.30731	0.998	0.8	0.2	1.02	1.00	1.04
11	61,305,450	0.27208	0.991	0.8	0.2	1.01	0.99	1.04
11	61,354,548	0.38782	0.998	−1.1	0.2	1.00	0.98	1.02
11	116,144,314	0.06787	0.999	−5.8	0.4	0.94	0.91	0.98
11	116,159,645	0.46743	0.999	−0.5	0.2	0.97	0.95	0.99
11	116,206,564	0.00228	0.979	−15.1	2.3	0.91	0.73	1.14
11	122,039,714	0.40275	0.996	0.6	0.2	1.01	0.99	1.03
11	125,749,162	0.10572	0.999	0.7	0.3	1.02	0.99	1.06
12	110,492,139	0.38236	0.999	0.8	0.2	0.94	0.92	0.96
12	110,794,963	0.2284	0.999	0.8	0.3	0.94	0.92	0.97
12	119,901,033	0.30901	0.994	0.9	0.2	1.03	1.01	1.05
13	31,851,388	0.44766	0.999	−0.7	0.2	0.99	0.97	1.01
14	23,953,727	0.49889	0.995	0.8	0.2	0.98	0.96	1.01
15	56,518,445	0.19278	0.999	−0.6	0.3	0.99	0.97	1.02
16	55,542,640	0.38939	0.991	−1.8	0.2	0.97	0.95	0.99
16	55,572,592	0.06047	0.997	2.9	0.5	1.04	1.00	1.09
16	66,485,543	0.10432	1.000	−0.8	0.3	0.97	0.94	1.01
16	70,665,594	0.14755	0.997	1.3	0.3	1.03	1.00	1.06
17	7,032,374	0.35058	0.996	−1.0	0.2	0.98	0.96	1.00
17	8,101,874	0.49481	0.998	−0.4	0.2	0.96	0.94	0.98
17	39,281,652	0.03364	0.989	1.3	0.6	1.08	1.02	1.15
17	42,746,803	0.28266	0.998	0.6	0.2	1.02	1.00	1.04
17	64,394,061	0.32561	0.995	0.5	0.2	1.03	1.01	1.05
18	45,363,953	0.01171	0.999	4.8	1.0	1.00	0.91	1.09
19	8,335,323	0.02392	0.965	−4.7	0.7	0.80	0.74	0.86
19	11,063,306	0.0888	0.995	−6.8	0.4	0.89	0.86	0.92
19	11,088,602	0.45236	0.997	1.4	0.2	1.02	1.00	1.04
19	19,268,718	0.07838	0.997	−3.8	0.4	0.96	0.92	1.00
19	50,103,781	0.16819	0.980	8.4	0.3	1.05	1.02	1.08
19	50,103,919	0.05236	0.968	−16.9	0.5	0.83	0.79	0.87
19	53,898,229	0.39118	0.997	1.1	0.2	1.00	0.98	1.03
19	57,016,028	0.27115	0.999	0.6	0.2	1.03	1.01	1.06
19	59,489,660	0.21613	0.990	−0.6	0.3	0.99	0.96	1.02
20	12,910,718	0.45731	0.998	0.4	0.2	1.00	0.98	1.03
20	17,793,921	0.15541	0.991	0.8	0.3	0.98	0.95	1.01
20	38,613,850	0.34358	0.997	−1.1	0.2	0.98	0.96	1.00
20	39,157,752	0.45945	0.997	1.1	0.2	0.99	0.97	1.01
20	42,475,778	0.04599	0.993	−1.3	0.5	0.98	0.93	1.03
20	44,018,827	0.21978	0.998	1.3	0.3	0.98	0.96	1.01
Shown are the build 36 positions (hg18), minor allele frequency (MAF), imputation information, the non-HDL effect in mg/dL and the standard error of the estimate (SE), and the OR for coronary artery disease and 95% CI for the minor allele.

TABLE 1.6
Association of del12 with various measures of liver function in Iceland
Phenotype	na	Effectb	Effect (95% CI)c	P	Mean (±1 SD)d
			% change
Alanine	144,402	0.087	5.8 (−0.4, 12.2)	0.065	28.7 (15.0-54.8)	units/L
Transaminase
Alkaline	126,060	0.840	50.1 (42.9, 57.2)	3.6 × 10−63	87.1 (53.5-141.7)	units/L
Phosphatase
Aspartate	144,931	0.072	4.1 (−2.9, 11.4)	0.095	28.1 (14.2-55.6)	units/L
Transaminase
Bilirubin	94,805	0.054	3.7 (−2.6, 10.4)	0.25	9.1 (4.6-18.0)	μm/L
Gamma Glutamyl	138,844	0.113	10.3 (1.7, 19.2)	0.015	30.9 (13.1-72.9)	units/L
Transpeptidase
			g/L
Albumin	78,555	−0.109	−0.72 (−1.37, 0.06)	0.033	39.5 (33.0-46.0)	g/L
aNumber of individuals used in the association analysis for each of the traits.
bEffect estimate, in units of standard deviation, from regression of adjusted trait values on the expected genotype count of del12.
cEffect estimates and 95% CI in original units. For traits with log-normal distribution the effects are presented as percentage change with 95% CI.
dMean trait values, ±one SD, in the Icelandic population. For traits with log-normal distribution the mean and SD is calculated for log-transformed trait values and transformed back to original units.

TABLE 1.7
Common Variants at the ASGR-1 Locus Associated with Non-HDL
Cholesterol and Alkaline Phosphatase in Iceland
	rs314253	rs56093546	del12
Chromosome position	17:7032374	17:7004539	17:7020979
MAF (%)	35.06	21.63	0.43
Effecta on non-HDL	−0.03	−0.04	−0.30
cholesterol
(P value)	(5.9 × 10−6)	(2.0 × 10−6)	(2.5 × 10−10)
Adjusted for rs314253 (P)	—	0.022	7.9 × 10−11
Adjusted for rs56093546 (P)	0.0068	—	7.2 × 10−11
Adjusted for del12 (P)	6.4 × 10−7	1.7 × 10−6	—
Effecta on ALP	0.050	0.068	0.82
(P value)	(3.9 × 10−21)	(7.4 × 10−28)	(3.6 × 10−63)
Adjusted for rs314253 (P)	—	5.7 × 10−12	4.1 × 10−66
Adjusted for rs56093546 (P)	0.000042	—	2.0 × 10−66
Adjusted for del12 (P)	4.2 × 10−24	4.0 × 10−31	—
r2, D′ (relative to rs314253)	—	0.29, 0.76	0.001, 0.60
r2, D′ (relative to rs56093546)	0.29, 0.76	—	0.001, 1.00
aEffect estimates from the regression in units of standard deviations of the distributions of the adjusted values.
The association of rs314253 with LDL cholesterol was reported in Willer et al 2013 and with ALP in Chambers et al., 2011.

TABLE 1.8
Association of p.w158X and del12 with Cholesterols, Triglyceride,
Alkaline Phosphatase, Vitamin B12 and CAD in an extended Icelandic dataset
	p.W158X	del12
Trait/(n)a	Effectb	Effect (95% CI)c	P	Effectb	Effect (95% CI)c	P
Non-HDL cholesterol	SD	mg/dL		SD	mg/dL
(136,261)	−0.45	−21.6 (−34.2, −9.6)	0.00057	−0.29	−13.3 (−17.2, −9.3)	4.0 × 10−11
LDL cholesterol		mg/dL			mg/dL
(53,932)	−0.38	−15.9 (−32.7, 0.9)	0.064	−0.23	−9.7 (−14.1, −5.1)	2.8 × 10−5
Total cholesterol		mg/dL			mg/dL
(131,879)	−0.30	−13.5 (−29.3, 2.2)	0.091	−0.23	−10.4 (−14.2, −6.5)	1.4 × 10−7
HDL cholesterol		mg/dL			mg/dL
(124,437)	0.14	2.4 (−3.9, 8.7)	0.45	0.15	2.5 (1.0, 4.0)	0.0016
Triglyceride		% change			% change
(82,569)	−0.17	−8.4 (−25.5, 7.2)	0.33	−0.12	−6.0 (−10.4, −1.8)	0.0075
ALP		% change			% change
(131,966)	0.77	45.3 (20.4, 68.2)	7.9 × 10−6	0.80	47.7 (2.2, 87.1)	5.6 × 10−76
Vitamin B12		% change			% change
(102,624)	0.26	15.6 (−4.3, 34.0)	0.084	0.33	17.5 (3.1, 30.9)	5.6 × 10−16
CAD		OR	P		OR	P
(35,134/275,567)		0.61 (0.26, 1.40)	0.24		0.66 (0.54, 0.81)	4.5 × 10−5
aNumber of individuals with trait value and genotypes.
bEffect estimates from the regression in units of standard deviations (SD) of the distributions of the adjusted values.
cEffect estimates and 95% confidence intervals (95% CI) in mg/dL for the cholesterols, and as percentage change for triglyceride, ALP and vitamin B12.
dP-values adjusted for the effect of del12. This analysis was done on an updated Icelandic dataset that includes 8,453 WGS individuals and imputation into 150,656 Icelandic individuals. For none-HDL cholesterol association analysis an updated sample set was used that contained 136,261 Icelanders.

TABLE 1.9A
Correlation and conditional analysis for del12 and the seven other SNPs that
show the strongest association at 17p13.1 with non-HDL cholesterol in Iceland
	non-HDL
Variant	Pos	EA	OA	EA. freq (%)	r2 d	Effectc	P	Padjdel12a	PadjSNPb
chr17: 6930020:S	6930020	T	C	0.39	0.85	−0.243	5.2 × 10−7	0.10	2.8E−05
rs188743906	6931736	T	C	0.39	0.85	−0.243	5.2 × 10−7	0.18	2.9E−05
rs150983647	6942021	T	C	0.44	0.76	−0.232	5.3 × 10−7	0.39	7.6E−05
chr17: 6944653:S	6944653	A	G	0.39	0.85	−0.242	5.9 × 10−7	0.10	2.3E−05
rs146261845	6952978	T	C	0.40	0.75	−0.259	1.1 × 10−7	0.88	0.00053
chr17: 6961021:S	6961021	C	T	0.39	0.85	−0.250	2.2 × 10−7	0.18	0.00010
rs186021206	7010136	A	G	0.43	0.86	−0.283	1.4 × 10−9	0.39	0.067
del12	7020979	del12	—	0.41		−0.297	2.5 × 10−10	—	—
aP-value for correlation between the SNP and the trait, tested conditional on the association of the trait with del12.
bP-value for the correlation between the trait and del12, tested conditional on the association of the trait with the SNP.
cEffect estimated in units of standardized trait values.
dCorrelation r2 between del12 and sequencing genotypes of the SNPs in 2,128 Icelandic individuals. Shown are the build 36 positions (hg18).

TABLE 1.9B
Association of del12 with Non-HDL Cholesterol, HDL Cholesterol and Triglyceride
Measurements, in Iceland, Denmark and the Netherlands
				Mean valueb in
	Study population (n)	Changea    SE	P value	non-carriers (SD)
	Non-HDL cholesterol	mg/dl		mg/dl
Discovery	Iceland (119,146)	−10.4 ± 1.5	2.5 × 10−10	156.8 (38.2)
Replication	The Netherlandsc (5,156)	−15.4 ± 5.4	0.0032	170.7 (41.3)
Replication	Denmark Ad (5,968)	−17.4 ± 8.1	0.0069	158.3 (42.9)
Replication	Denmark Be (8,822)	−21.6 ± 5.4	3.8 × 10−5	164.5 (40.5)
	Combined	−11.6 ± 1.5	1.0 × 10−16
	HDL cholesterol	mg/dl		mg/dl
Discovery	Iceland (119,514)	0 ± 0.4	0.0058	55.2 (15.8)
Replication	The Netherlands (5,537)	2.7 ± 1.5	0.20	52.2 (13.1)
Replication	Denmark A (6,182)	1.2 ± 2.7	0.096	55.2 (15.4)
Replication	Denmark B (9,656)	1.5 ± 1.2	0.26	59.9 (16.2)
	Combined	0 ± 0.4	0.00039
	Triglyceride - mg/dl	mg/dl		mg/dl
Discovery	Iceland (80,011)	−1.2 ± 1.5	0.012	130.9 (75.2)
Replication	The Netherlands (5,537)	−0.4 ± 5.8	0.52	176.9 (121.2)
Replication	Denmark A (6,182)	8.1 ± 6.9	0.53	116.8 (84.0)
Replication	Denmark B (8,163)	−3.5 ± 2.3	0.15	131.8 (118.5)
	Combined	−1.5 ± 1.2	0.0030
aEffect size, ±standard error, represents the difference in mean values between heterozygote carriers and non-carriers of the variants after adjusting for age, sex and, for Iceland, site and statin use.
bCalculated based on unadjusted values.
cThe Nijmegen Biomedical Study (Wetzels et al. 2007).
dThe Danish Inter99 study (Jørgensen et al. 2003).
eThe Danish Addition study (Lauritzen et al. 2000). To convert the values for non-HDL cholesterol to millimoles per liter, multiply by 0.02586

TABLE 1.10
Association of del12 with Alkaline Phosphatase and Vitamin B12 Serum Measurements
in Iceland and Denmark
				Mean valueb in non-
	Study population (n)	Changea ± SE	P value	carriers (SD)
	ALP	U/L		U/L
Discovery	Iceland (126,060)	+33.6 ± 2.8	3.6 × 10−63	92.8 (64.0)
Replication	Denmark A (5,829)	+15.8 ± 2.6	1.7 × 10−6	42.9 (13.5)
	Combined	+24.1 ± 1.9	9.9 × 10−69
	Vitamin B12	pmol/L		pmol/L
Discovery	Iceland (97,910)	+58.4 ± 8.3	3.1 × 10−12	439.0 (171.0)
Replication	Denmark A (5,826)	+75.9 ± 29.2	0.0069	420.0 (146.0)
	Combined	+59.7 ± 7.9	9.9 × 10−14
aEffect size, ±standard error, represents the difference in mean values between heterozygote carriers and non-carriers of the variants after adjusting for age, sex and, for Iceland, site and statin use.
bCalculated based on unadjusted values.
cThe Nijmegen Biomedical Study (Wetzels et al. 2007).
dThe Danish Inter99 study (Jørgensen et al. 2003).
eThe Danish Addition study (Lauritzen et al. 2000). To convert the values for non-HDL cholesterol to millimoles per liter, multiply by 0.02586

Example 2—ALP Data from ASGR-1 Knockout Mice

ASGR-1 KO mice (strain B6.129S4-ASGR-1^tm1Sau/SaubJxmJ) were obtained from Jackson Labs and maintained on a chow diet. Serum was collected from male and female animals after a 4 hr fast and tested in an Olympus AU640 Clinical Chemistry Analyzer. Compared to wild-type mice, serum ALP is elevated in ASGR-1 knockout mice (*, p<0.05; ****, p<0.0001, one-way ANOVA with Dunnett test). Levels of alanine transaminase (ALT) and aspartate transaminase (AST) were not significantly different between the groups. These data are summarized in FIG. 7 herein. WT=wild-type; HE=heterozygous; HO=homozygous.

Example 3—RNAi

Material and Methods

siRNA Constucts

TABLE 3.1
		Primary
	Vendor	Gene	Target	SEQ	matched	SEQ
Vendor	catalog#	Target	Sequence	ID NO:	control	ID NO:
Fisher/Ambion	S1662	hASGR-1	ACUUCACAGC	32614	ACUUCACACGC	32632
			GAGCACGGA		AGCACGGA
GE/Dharmacon	D-011215-	hASGR-2	GCCAAGGACU	32615	GCCAAGGAGAA	32633
	01		UUCAAGAUA		UCAAGAUA
GE/Dharmacon	D-011215-	hASGR-2	UGACGGAGGU	32616	UGACGGAGCAG	32634
	03		CCAGGCAAU		CAGGCAAU
GE/Dharmacon	D-011215-	hASGR-2	AGUGAUGGCU	32617	AGUGAUGGGAG	32635
	04		CUUGGAAAU		UUGGAAAU
Fisher/Ambion	S1665	hASGR-2	GACUAUAGGC	32618	GACUAUAGCGU	32636
			ACAACUACA		CAACUACA
Fisher/Ambion	S194296	hASGR-2	CUGUGUGACUG	32619	CUGUGUGAGAC	32637
			GGUCCCAA		GGUCCCAA
Fisher/Ambion	S194297	hASGR-2	CACCUCUGGCU	32620	CACCUCUGCGAA	32638
			AACCCAUA		ACCCAUA
GE/Dharmacon	D-042958-	mASGR-1	GAGACAGGCUU	32621	GAGACAGGGAA	32639
	01		CCAGAAUU		CCAGAAUU
GE/Dharmacon	D-042958-	mASGR-1	UGAAGUUAGUG	32622	UGAAGUUACAC	32640
	04		GAGUCGAA		GAGUCGAA
Fisher/Ambion	S62656	mASGR-1	AGAUCACUCCA	32623	AGAUCACUGGU	32641
			GUUUGCUA		GUUUGCUA
Qiagen	S102735796	mASGR-1	CCAUCAUGACA	32624	CCAUCAUGUGU	32642
			AAGGAUUA		AAGGAUUA
GE/Dharmacon	D-061966-	mASGR-2	GGAUGGAACU	32625	GGAUGGAAGAC	32643
	01		GAUUAUAGA		AUUAUAGA
GE/Dharmacon	D-061966-	mASGR-2	GGAAUUGGGCC	32626	GGAAUUGGCGG	32644
	02		UUCACUCA		UUCACUCA
GE/Dharmacon	D-061966-	mASGR-2	GACGGAACAUC	32627	GACGGAACUAG	32645
	03		ACCCACUA		ACCCACUA
GE/Dharmacon	D-061966-	mASGR-2	GGAUAGGUCUU	32628	GGAUAGGUGAA	32646
	04		ACCGACAG		ACCGACAG
GE/Dharmacon	S62659	mASGR-2	GCAGGAUCCU	32629	GCAGGAUCGAU	32647
			AGGAUAGAA		GGAUAGAA
Fisher/Ambion	S62660	mASGR-2	ACAUUGCUCU	32630	ACAUUGCUGAA	32648
			UUCACCUGA		UCACCUGA
Fisher/Ambion	S62661	mASGR-2	GAAGAGUUUC	32631	GAAGAGUUAGC	32649
			GGACCCUGA		GACCCUGA

Expression Analysis

RNA was isolated from the HepG2, CHOs stable cell lines, or liver tissues treated with scrambled siRNA, matched control siRNA or siRNAs against hASGR-1, hASGR-2, mASGR-1 or mASGR-2 using the Qiacube and standard Qiagen RNA isolation protocol. The RNA was DNase treated using the RQ1 DNase kit (Promega). Quantitative PCR was performed according to the manufacturer's protocol on the Quantstudio 7 using the indicated primer probe set (hASGR-1: Hs01005019_m1; hASGR-2: Hs00910102_m1; mASGR-1: Mm01245581_m1, mASGR-2:Mm00431863_m1) from Applied Biosystems. 50 ng RNA/well was used and normalized with 18S internal control.

siRNA Transfection

Cells were transfected with 10 nM indicated scrambled siRNA, matched control siRNA or siRNAs against hASGR-1, hASGR-2, mASGR-1 or mASGR-2 siRNA for 3-4 days, using Lipofectamine RNAMAX (Thermo Scientific) following manufacturer's RNAi reverse transfection protocol. Transfection was done in 96 well Screenstar microplates (Greiner bio-one) for internalization assay as well as in 96 well clear tissue culture plates (Corning) for QPCR and Western blotting.

Western Blotting

Cells were lysed in RIPA buffer containing inhibitors 3-4 days after siRNA transfection. Cell lysates were passed through a 21 gauge syringe five times and then centrifuged at 13000 rpm at 4 C for 15 mins. Supernatants were collected and protein concentrations were determined. If needed, 30 ug of protein was deglycosylated using the deglycosylation kit (Genzyme). 10 ug-30 ug of total protein was loaded in each well. The gel was transferred onto a nitrocellulose membrane and the membrane was blocked with 5% blocking buffer for 1 hr at RT. Membrane was then probed with anti-mASGR-1 (1:1000, R &D), hASGR-1 (1:1000, ProteinTech), hASGR-2 (1:1000, Abcam), anti-flag (1:5000, Sigma), anti-his (1:1000, Cell signaling) and mouse anti β-actin (1:5000, Thermo Fisher or Cell signaling) o/n at 4 C. The membrane was further probed with anti-mouse and anti-rat secondary antibodies to detection the indicated bands.

Ligand Internalization Assay

CHO stable cell lines were treated with scrambled siRNA, matched control siRNA or siRNAs against hASGR-1, hASGR-2, mASGR-1 or mASGR-2 siRNA for 3-4 days and plated in 96-well plate. Biotin-GalNAc-PAA was incubated and strepavidin-Alexa488 was further added to cells. Draq5 was used to counterstain cells (for both cytoplasm and nuclei). Cells were scanned with Operetta Image System and data analyzed by Columbus.

Animal Study

All animal housing conditions and research protocols were approved by the Amgen Institutional Animal Care and Use Committee (IACUC). Mice were housed in a specified-pathogen free, AAALAC, Intl-accredited facility in ventilated microisolators. Procedures and housing rooms are positively pressured and regulated on a 12:12 dark:light cycle. All animals received reverse-osmosis purified water ad libitum via an automatic watering system. 10-12 week old C57BL/6J animals (The Jackson Laboratory) were singly housed and were fed standard chow (2020× Teklad global soy protein-free extruded rodent diet; Harlan).

siRNAs modified for in vivo studies were formulated with Invivofectamine 3.0 (Thermo Scientific) following the manufacturer's protocol. In brief, siRNAs were pre-mixed with complex buffer (provided by manufacturer) and Invivofectamine 3.0, and then incubated at 50° C. for 30 minute and further diluted by PBS before injection.

Mice were i.v. injected with buffer, indicated siRNA and matched control siRNA at 1-2 mg/kg body weight in 0.25 ml buffer at indicated time. Liver total RNA from harvested animals was processed for qPCR analysis.

Data from these studies is provided in FIGS. 8-17 herein.

Example 4—Y272C Mutant Data

Stable pools of Chinese hamster ovary (CHO) cells expressing C-terminal FLAG epitope-tagged murine wild-type or Y272C ASGR-1 were generated by established methods using puromycin selection. Cell surface expression of ASGR-1 was confirmed by FACS using anti-FLAG antibody both during selection process and at the time of the experiment. Ligand binding was assessed by FACS using β-GalNAc-PAA-biotin (Glycotech Corporation) and streptavidin-phycoerythrin (PE). Briefly, ligand was added to 100 ul cells (1×10⁶ cells) in Dulbeco's Modified Eagle Medium (DMEM) without phenol red plus 2% bovine serum albumin (BSA) and incubated on ice for 60 minutes. Cells were then washed 3× with DMEM without phenol red plus 2% BSA. Streptavidin-PE was then added at 1 μg/ml for 20 minutes on ice followed by 3 more washes in DMEM without phenol red plus 2% BSA, at which point the cells were resuspended in 0.5 ml DMEM without phenol red plus 2% BSA and 5 ul of 0.1 mM SyTOx Blue viability dye and analyzed on a BD LSR II (BD Biosciences). Data are presented as Median Fluorescence Intensity as shown in Table 4.1, below.

TABLE 4.1
ASGR-1 Y272C has reduced ligand
binding compared to wild-type ASGR-1
	β-GalNAc-PAA-biotin,
	ug/ml	Anti-FLAG
	0	0.1	0.3	antibody
	Parental	5.23	5.52	5.57	7.3
	WT	4.87	763.51	1394.86	3959.65
	Y272C	5.28	5.47	6.10	973.38

Example 5—Generation of Antibodies

Molecular Cloning of ASGR-1 and ASGR-2 Sequences

For production of recombinant ASGR-1 and ASGR-2 vectors, cDNA sequences were synthesized, obtained from a commercial source or compiled from RNA sequencing data (Amgen). Human, mouse and rat ASGR cDNA clones were from obtained commercially (OriGene Technologies, Inc.). All other ASGR cDNAs were synthesized (Integrated DNA Technologies, Inc.). GenBank accession numbers are as follows: human ASGR-1 (NM_001671.4), human ASGR-2 (NM_080913.3), mouse ASGR-1 (BC022106.1), mouse ASGR-2 (BC011197.1), rat ASGR-1 (NM_012503), rat ASGR-2 (NM_017189), pig ASGR-1 (NM_001244458), pig ASGR-2 (XM_005669199), dog ASGR-1 (XM_546579), dog ASGR-2 (XM_003434599), cynomologus monkey ASGR-1 (XP_005582755). Since the NCBI entry for cynomologus ASGR-2 was a partial amino acid sequence (NCBI protein accession # EHH57653), the complete nucleotide sequence was compiled through the analysis of the cyno genome (genome build Macaca_fascicularis_5.0; GenBank accession number GCA_000364345.1; Washington University) and RNA sequencing data (Amgen) from cyno liver, heart and skin tissue. For transient or stable mammalian expression, cDNAs were cloned into pTT5 (National Research Council of Canada), pSLX235a (SureTech) or pJiFl (Boyce Lab, Massachusetts General Hospital, U.S. Pat. No. 7,192,933). For individual recombinant protein production in mammalian cells, most sequences were tagged at their C-termini with a 6×His purification tag. For complexes of huASGR-1 and huASGR-2, huASGR-2 was expressed without the 6×His tag. For recombinant expression in E. coli, sequences were cloned into pET21a (Novagen, EMD Millipore). The amino acid sequences of the resultant ASGR proteins are shown in Table 1.

Expression and Purification of Recombinant Proteins

Generation of Stable CHO—S Cell Pools for Recombinant Protein Expression

CHO—S(Invitrogen, Carlsbad, Calif.) cells were transfected with the pSLX235a vector encoding ASGR-1 or ASGR-2 using Lipfectamine LTX according to the manufacturer's recommendations (ThermoFisher Scientific). Stable pools were selected using 10 ug/ml puromycin (single selections) or 10 ug/ml puromycin and 400 ug/ml hygromycin (double selections) and by culturing the cells in fresh media every 2 days. Stable pools were then used for recombinant protein production.

Recombinant Protein Production and Purification from CHO—S Cell Stable Pools

Cells from the selected stable pools were expanded in growth medium. When sufficient cell numbers had been obtained, cultures were seeded in 2 L conical flasks in a volume of 1 L of growth medium at a viable cell density of 8×10⁵ cells/ml. Cells were then cultured in suspension at 37° C., in 5% CO₂ for three days, after which the temperature was dropped to 31° C. for the final 7 days of production. Centrifugation was used to pellet the cells, and the resulting supernatant was filtered to generate conditioned medium.

Individual recombinant proteins were purified via the 6×His tag using Ni-Excel resin (GE Healthcare). Briefly, 1.4 L of conditioned medium was loaded onto 3×5 ml Ni-Excel Hi-trap columns and then washed with 10 column volumes of wash buffer (25 mM HEPES, pH7.6, 250 mM NaCl, 1 mM CaCl₂, 50 mM imidazole). Protein was eluted from the columns with 7 column volumes of elution buffer (25 mM HEPES, pH7.6, 250 mM NaCl, 1 mM CaCl₂, 400 mM imidazole). The eluted fractions were loaded onto a HiLoad Superdex 200 column via 2×10 ml injections and eluted with 25 mM HEPES, pH 7.6; 150 mM NaCl, 1 mM CaCl₂. The final fractions were collected based on their expected molecular weight. The identity of the proteins in each eluted peak was confirmed by LC-TOF-MS after deglycosylation (with N-glycanase, O-glycanase and sialidase) and reduction. ASGR-1/ASGR-2 complexes were purified by pre-incubating the ASGR-1-6×His Tag conditioned medium with ASGR-2-no 6×His Tag conditioned medium. These conditions permitted association of both proteins giving a complex that could be purified via the standard two-step Ni-Excel/SEC method.

Recombinant Protein Production and Purification from E. coli

E. coli codon optimized sequences were cloned into the pET21a expression plasmid. Plasmids were transformed into E. coli strain BL21(DE3) Star (ThermoFisher Scientific Inc.) and individual clones were selected using carbinicillin. For expression, cells were grown in 1 L TB growth medium (supplemented with carbinicillin) in a 4 L flask at 37° C. with shaking. When an optical density of 2 was achieved, protein expression was induced by the addition of 1 mM IPTG (final concentration). After 4 hours of induction at 37° C., the cell paste was harvested by centrifugation (recovering between 7 and 14 g cell paste/L culture). Protein localization into the insoluble fraction was confirmed by SDS-PAGE.

Inclusion bodies were recovered from the cell paste and solubilized in 6M guanidinium containin 10 mM DTT. Successful protein refolding was established by screening a matrix of 32 conditions that included a variety of buffers, pHs, denaturants, stabilizing agents and reducing agents. The refolding procedure was initiated by rapidly diluting the dissolved inclusion bodies at a ratio of 1:15 into the appropriate refold buffer, maintaining approximately 1 mg of protein per condition. The samples were then incubated at 4° C. for 60 hours. The resulting batches were analysed by SDS-PAGE and Ion Exchange chromatography to identify the optimal refolding conditions. For the ASGR-1 CBD (148-291), the final refold conditions were: pH 9.5, 2.5M urea, 20% glycerol, 4 mM cysteine and 4 mM cystamine.

Generation of Anti-ASGR Immune Responses

Mouse Strains

Fully human antibodies to human ASGR were generated by immunizing XENOMOUSE® transgenic mice (U.S. Pat. Nos. 6,114,598; 6,162,963; 6,833,268; 7,049,426; 7,064,244, which are incorporated herein by references in their entirety; Green et al., 1994, Nature Genetics 7:13-21; Mendez et al., 1997, Nature Genetics 15:146-156; Green and Jakobovitis, 1998, J. Ex. Med, 188:483-495; Kellerman and Green, Current Opinion in Biotechnology 13, 593-597, 2002). Animals from the XMG2-K, XMG2-KL, XMG4-K and XMG4-KL XENOMOUSE® strains were used for all immunizations.

Mouse anti-human ASGR antibodies were generated by immunizing BALB/c, C57BL/6 and CD-1 mice (Charles River Laboratories, San Diego, Calif.) as well as B6.12954-ASGR-1^tm1Sau/SaubJxmJ (ASGR-1 KO mice) and C57BL6 ×129 F1 mice (Jackson Laboratory, Sacramento, Calif.).

Fully human, heavy chain only antibodies (HCAbs) were generated by immunizing the VH4 and 8V3 strains of transgenic Harbour mice (Janssens et al. 2006, PNAS 103:15130-15135; Harbour Biologics, Rotterdam, Netherlands). Rat anti-mouse ASGR antibodies were generated using Brown Norway Rats (Charles River Laboratories, San Diego, Calif.).

Immunizations

Multiple immunogens and routes of immunization were used to generate anti-human ASGR immune responses. For genetic immunizations, mice were immunized 12-14 times over 6-8 weeks using the Helios Gene Gun system according to the manufacturer's instructions (BioRad, Hercules, Calif.). Briefly, expression vectors encoding wild type human or mouse ASGR-1 (or both huASGR-1+huASGR-2, muASGR-1+muASGR-2) were coated onto gold beads (BioRad, Hercules, Calif.) and delivered to the epidermis of a shaved mouse or rat abdomen. For cell-based immunizations, mice and rats were immunized with CHO-s cells (Invitrogen, Carlsbad, Calif.) or 293-6E cells (National Resource Council of Canada) transiently transfected with expression vectors encoding human or mouse ASGR-1 (or both huASGR-1+huASGR-2, muASGR-1+muASGR-2). Animals were immunized with cells mixed with Alum prepared from aluminum potassium sulfate (EMD Chemicals Inc., Gibbstown, N.J.) and CpG-ODN (Eurofins MWG Operon LLC, Huntsville, Ala.) 10 times over 6 weeks using a protocol that alternated between sub-cutaneous and intraperitoneal injections. The initial boost was comprised of 4×10⁶ cells while subsequent boosts contained 2×10⁶ cells. For soluble protein immunizations, mice were immunized with a variety of human ASGR recombinant proteins representing the complete extracellular domain (ECD), the carbohydrate binding domain (CBD) or the complex of ASGR-1 and ASGR-2 ECDs (Table 5.1). Animals were immunized with recombinant protein (or recombinant protein conjugated to KLH using standard methods) mixed with Alum and CpG-ODN, Complete Freund's Adjuvant (Sigma), or MPL+Adjuvant (Sigma) 10 times over 4-6 weeks using sub-cutaneous injections. The initial boost was comprised of 10 μg while subsequent boosts contained 5-10 μg. Human ASGR-1-specific serum titers were monitored by live-cell FACS analysis on an Accuri flow cytometer (BD Biosciences). Animals with the highest antigen-specific serum titers were sacrificed and used for hybridoma generation (Kohler and Milstein, 1975).

TABLE 5.1
Soluble, Recombinant Protein Antigens Used for Immunizations
Recombinant Protein Immunogen    Source
huASGR-1 (Cat#: C428) ECD-KLH conjugate Novoprotein
huASGR-1 (64-291) ECD-KLH conjugate Amgen
huASGR-1 (64-291) ECD            Amgen
huASGR-1 (154-291) CBD           Amgen
huASGR-1(64-291)/huASGR-2 (61-287) ECD Complex Amgen
huASGR-1(64-291)/huASGR-2 (61-287) ECD Complex- Amgen
KLH conjugate
muASGR-1 (63-284)                Amgen

Preparation of Monoclonal Antibodies

Hybridoma Generation

Animals exhibiting suitable serum titers were identified and lymphocytes were obtained from spleen and/or draining lymphnodes. Pooled lymphocytes (from each immunization cohort) were dissociated from lymphoid tissue by grinding in a suitable medium (for example, Dulbecco's Modified Eagle Medium (DMEM); Invitrogen, Carlsbad, Calif.). B cells were selected and/or expanded using standard methods, and fused with a suitable fusion partner using techniques that were known in the art.

Antigen Enrichment of Hybridoma Pools

Fused hybridoma pools from each immune tissue harvest were used as a source of material for FACS-based enrichments using a variety of probes. To enrich for hybridomas expressing antibodies specific to native (full length, on-cell) human, cyno, mouse, rat, dog, or pig ASGR-1 (and native human ASGR-2) membranes were prepared from 293T cells transiently expressing the relevant ASGR cDNA construct. 24 hours after transfection using 293-fectin (ThermoFisher Scientific Inc.), cells were biotinylated with E-Z link NHS-LC-LC-Biotin according to the manufacturer's recommendation (ThermoFisher Scientific Inc.). After biotinylation, cells were homogenized with a needle and syringe to form membrane fragments and referred to as “membrane preps”. The biotinylated membrane preps were then used to detect hybridomas expressing surface antibodies specific to the target of interest via standard biotin-streptavidin chemistry. To enrich for hybridomas capable of binding to the recombinant ASGR-1 ECD or CBD, soluble, 6×His-tagged ASGR-1 proteins were used (Amgen).

To enrich hybridoma pools for the antigen of interest, they were first incubated with the appropriate membrane prep or soluble probe. For soluble forms of ASGR-1, the recombinant protein probes were added to the hybridomas and allowed to bind. Excess probe was then washed away and the antigen-specific hybridomas were identified by simultaneous detection of surface IgG (with an Alexa 488 conjugated secondary antibody (Jackson ImmunoResearch) (Gt anti-mouse Fc for wild type mouse hybridomas and Gt anti-human Fc for transgenic mouse hybridomas)) and the soluble ASGR-1 probe via its 6×His tag (using an Amgen-derived anti-6×His monoclonal antibody conjugated to Alexa 647 via an Alexa 647 labeling kit (ThermoFisher Scientific Inc). Hybridomas expressing surface IgG and binding antigen were detected by FACS analysis on an Accuri flow cytometer. Dual positive events were sorted as single cells into 384-well plates on a FACS Aria cell sorter (BD Biosciences). For native forms of ASGR-1, biotinylated membrane preps were prepared as described from 293T cells transiently expressing the appropriate antigen. After washing away unbound probe, dual positive hybridomas expressing cell surface IgG and binding antigen were detected using an Alexa 488 conjugated secondary antibody (to detect IgG) and streptavidin conjugated to Alexa 647 (Jackson ImmunoResearch) to detect antigen. These events were sorted as single cells into 384-well plates on a FACS Aria cell sorter. After several days of culture, the hybridoma supernatants containing monoclonal antibodies were collected and used in the screening assays described in the examples below.

Example 6: Identification of ASGR-1 Specific Antibodies

The following Table 6.1 summarizes the approximate numbers of antibodies assayed:

TABLE 6.1
Summary of the identification and selection of
huASGR-1 binding, ligand blocking antibodies.
ASGR-1 Screen                    Number of Antibodies
huASGR-1 Binders                 15731
huASGR-1-Ligand Blockers (>60%)  5306
Sequences Unique huASGR-1-Ligand 2603 (disclosed in Table 3)
Blockers
huASGR-1-Ligand Blockers (>50%)  172 (disclosed in Table 3)

Example 6-A: Initial Selection of ASGR-1 Specific Binding Antibodies

Hybridoma supernatants (monoclonal antibodies) were screened for binding to human ASGR-1 transiently expressed on Human Embryonic Kidney (HEK) 293 cells using the Cell Insight™ High Content Imaging Platform (ThermoFisher Scientific). Human ASGR-1 was transiently expressed on host HEK 293 cells by transfection using human ASGR-1 DNA, Gibco™ Opti-MEM® media and 293Fectin™ reagents following the protocol set out by the manufacturer. Transfected HEK 293 cells expressing the human ASGR-1, hybridoma supernatant or control samples, Alexa Fluor® 488 IgG Fc fragment-specific detection antibody and Hoechst 33342 stain were mixed and incubated for 3 hours at room temperature. Samples were then washed and analyzed on the CellInsight™ system. Supernatants were counter-screened against HEK 293 cells transfected with empty parental vector (referred to as mock). Analysis was done using irrelevant IgG antibody supernatant sample signal; hybridoma supernatant samples showing two times or greater signal over irrelevant IgG antibody sample were considered to be exhibiting ASGR-1-specific binding profiles and selected for further characterization. See Table 6.1.

Example 6-B: Identification of ASGR-1 Receptor-Ligand Blocking Antibodies

ASGR-1-binding hybridoma supernatants were tested for their ability to block ASGR-1 from binding ligand. Competitive binding assays were performed on the antigen specific hybridoma supernatant samples using FACS on either HEK 293 cells transiently expressing human ASGR-1 or CHO—S cells stably expressing Human ASGR-1 as follows. HEK 293 cells or CHO—S cells expressing human ASGR-1 were mixed with the antibody sample (hybridoma supernatants specific for ASGR-1) and incubated for 1 hour at 4° C., and then washed twice. Cells with bound sample were then incubated with precomplexed β-GalNAc-PAA-Biotin (GlycoTech, Gaithersburg, Md.)/Alexa Fluor® 647-Streptavidin for 45 minutes at 4° C. The concentration of β-GalNAc-PAA-Biotin was used at the binding EC50 concentration on the specific cell line. The concentration of Alexa Fluor® 647 Streptavidin was used at a 2:1 molar ratio to β-GalNAc-PAA-Biotin. The 7-AAD cell viability stain was then added and the cells incubated for a further 15 minutes at 4° C., washed twice and resuspended in FACS buffer. Where tolerated by cell viability, FACS buffer supplemented with 1 mM Calcium Chloride was used in all steps. Samples were analyzed using a BD Accuri™ Flow Cytometer and an Intellicyt HyperCyt Autosampler. Analysis was done using irrelevant (non-ASGR-1 specific) IgG antibody supernatant control signal on both mock transfected HEK 293 cells and Human ASGR-1 transfected HEK 293 cells to determine maximum and minimum β-GalNAc-PAA-Biotin binding signal. Using these maximum and minimum binding signals, the % β-GalNAc-PAA-Biotin binding inhibition was determined. ASGR-1 antibodies having the ability to reduce ligand binding ≧60% were identified (Table 6.1), and sequenced using methods available to those skilled in the art. The sequences of unique ASGR-1-specific, ligand blocking antibodies are displayed in Table 2-7 herein.

The unique ASGR-1-specific, ligand blocking antibodies were then tested for their ability to block the GalNAc ligand under more stringent conditions using a single, known antibody concentration (5 ug/ml). The receptor-ligand blocking assays were performed using 293T cells transiently expressing ASGR-1 or CHOs cells that had been stably transfected with ASGR-1. ASGR-1 antibodies having the ability to reduce ligand binding ≧50% were identified. See Table 6.1.

Example 7: Antibody Characterization Assays

A. ASGR-1 Species Cross Reactivity, ASGR-2 Selectivity Assays and Hepatoma (HEPG2) Binding Assays

Human ASGR-1-specific, ligand competing antibody samples were tested for binding to ASGR-1 from other species (cynomologus monkey ASGR-1, mouse ASGR-1, rat ASGR-1, dog ASGR-1, and pig ASGR-1) as well as to human ASGR-2 in FACS binding assays at normalized antibody concentrations. For cell-based assays, HEK 293 cells expressing the appropriate antigen of interest were mixed with antibody sample or controls, incubated for 1 hour at 4° C., and then washed twice. Cells with bound antibody were then incubated with Alexa Fluor® 647 IgG Fc fragment-specific detection antibody and 7-AAD viability stain for 15 minutes at 4° C., washed once and resuspended in FACS buffer. Samples were analyzed using a BD Accuri™ Flow Cytometer and an Intellicyt HyperCyt Autosampler. As a negative control, supernatants and controls were also screened against HEK 293 cells transfected with empty parental vector. Analysis was done using irrelevant (non-ASGR-1 specific) IgG antibody supernatant sample signal; hybridoma supernatant samples showing at least two times the signal over irrelevant IgG antibody sample were considered to be exhibiting ASGR-1-species specific binding profiles. For membrane-prep binding assays, ASGR-1 species specific membrane preps were used to coat LumAvidin® microspheres (beads) and tested for binding to selected hybridoma supernatants or controls. Briefly, ASGR-1 species specific membrane preps were incubated with streptavidin-coated LumAvidin® beads for 45 minutes in the dark at room temperature and washed twice. Beads were resuspeneded in FACS buffer containing Stabilguard®. Antigen-bound beads were then incubated with normalized antibody sample for 1 hour in the dark at room temperature, washed twice, incubated with Alexa Fluor® 488 IgG Fc fragment-specific detection antibody for 15 minutes in the dark at room temperature, washed once and finally resuspended in FACS buffer. Samples were analyzed using an Intellicyt iQue™ Screener Platform. FACS buffer supplemented with 1 mM Calcium Chloride was used in all steps. As a negative control, supernatants and controls were also screened against a non-ASGR-1 antigen membrane prep coated on the LumAvidin® beads. Analysis was done using irrelevant (non-ASGR-1 specific) IgG antibody supernatant sample signal; hybridoma supernatant samples showing at least two times the signal over irrelevant IgG antibody sample were considered to be exhibiting specific binding profiles. See Table 7.1.

Human ASGR-1-specific, ligand competing hybridoma supernatant samples were screened for binding to the human hepatocellular carcinoma cell line HepG2 (ATCC HB-8065) at normalized antibody concentrations. For FACS binding assays, HepG2 cells were mixed with normalized antibody samples or controls, incubated for 1 hour at 4° C., and washed twice. Cells with bound antibody were then incubated with Alexa Fluor® 647 IgG Fc fragment-specific detection antibody and 7-AAD viability stain for 15 minutes at 4° C., washed once and resuspended in FACS buffer. Samples were analyzed using a BD Accuri™ Flow Cytometer and an Intellicyt HyperCyt Autosampler. For high content imaging binding assays, HepG2 cells were mixed with normalized antibody samples or controls, incubated for 1 hour at room temperature and washed twice. Cells with bound antibody were then incubated with Alexa Fluor® 488 IgG Fc fragment-specific detection antibody and Hoechst 33342 stain for 30 minutes at room temperature, washed twice and analyzed on the CellInsight™ system. Where tolerated by cell viability, FACS buffer supplemented with 1 mM Calcium Chloride was used in all steps. Analysis was done using irrelevant (non-ASGR-1 specific) IgG antibody supernatant sample signal; hybridoma supernatant samples showing two times or greater signal over irrelevant IgG antibody sample were considered to be exhibiting HepG2 ASGR-1 specific binding profiles. See Table 7.1.

TABLE 7.1
Summary of the binding specificities of the selected human ASGR-1 binding antibodies.
	Binding Data Summary
	Human	Cyno	Mouse	Rat	Dog	Pig	HEPG2	Human
mAb	ASGR-1	ASGR-1	ASGR-1	ASGR-1	ASGR-1	ASGR-1	Cells	ASGR-2
25A4	Y	Y	N	Y	N	Y	Y	N
26C4	Y	Y	N	Y	N	Y	Y	N
29H8	Y	Y	N	Y	N	Y	Y	N
4A2	Y	Y	N	Y	N	Y	Y	N
4H6	Y	Y	Y	Y	N	Y	Y	N
56E5	Y	Y	N	N	N	Y	Y	N
7F4	Y	Y	N	no data	Y	Y	Y	Y
7G4	Y	Y	N	N	N	Y	Y	N
48B12	Y	Y	N	N	N	Y	Y	N
184E7	Y	Y	Y	Y	Y	Y	Y	N
194A4	Y	Y	N	Y	Y	Y	Y	N
4B1	Y	Y	Y	Y	Y	Y	Y	N
72G9	Y	Y	Y	Y	Y	Y	Y	N
190F8	Y	Y	N	N	Y	Y	Y	N
191G1	Y	Y	N	N	Y	Y	Y	N
191G10	Y	Y	N	N	Y	Y	Y	N
194C1	Y	Y	N	N	Y	Y	Y	N
197G3	Y	Y	N	N	Y	Y	Y	N
198G3	Y	Y	N	N	Y	Y	Y	N
75G3	Y	Y	N	N	Y	Y	Y	N
218G4	Y	Y	N	N	Y	Y	Y	N
193E7	Y	Y	N	N	Y	N	Y	N
198D2	Y	Y	N	Y	N	Y	Y	N
202A3	Y	Y	N	N	Y	Y	Y	N
7E11	Y	Y	N	N	N	Y	Y	N
22G5	Y	Y	N	N	N	N	Y	N
5E5	Y	Y	N	Y	N	N	Y	N
54E9	Y	Y	N	N	Y	N	Y	N
6G7	Y	Y	N	Y	N	N	Y	Y
176H4	Y	Y	N	N	Y	Y	Y	N
194C10	Y	Y	N	N	Y	Y	Y	N
12D2	Y	Y	Y	Y	Y	Y	Y	N

B. Relative Binding Affinities for ASGR-Specific mAbs

To assess antibody and antigen interaction strength (relative binding affinity), ASGR-1 specific, ligand competing antibody hybridoma supernatants were tested in a limiting antigen binding assay. Titrated amounts of recombinant, soluble ASGR-1 biotinylated protein was incubated with streptavidin-coated LumAvidin Beads® for 45 minutes in the dark at room temperature and washed twice. Beads were resuspeneded in FACS buffer containing Stabilguard® and 0.05% Sodium Azide. Antigen-bound beads were then incubated with normalized hybridoma supernatant sample or controls for 18 hours in the dark at room temperature, washed twice, incubated with Alexa Fluor® 488 IgG fragment-specific detection antibody for 15 minutes in the dark at room temperature, washed once and finally resuspended in FACS buffer. Samples were analyzed using an Intellicyt iQue™ Screener Platform. FACS buffer supplemented with 1 mM Calcium Chloride was used in all steps. Analysis was done using irrelevant (non-ASGR-1 specific) IgG antibody supernatant sample signal; hybridoma supernatant samples showing at least two times or greater signal over irrelevant IgG antibody sample were considered to be exhibiting ASGR-1 specific binding profiles. In this assay method, the antibody binding signal correlates with antibody affinity. Antibody binding data for a representative antigen coating concentration that fell in the linear range of the instrument signal detection is shown in Table 7.2. The degree of antibody binding to the target (ASGR-1) correlates with the measured fluorescent intensity and thus allows a relative comparison of affinities across the panel.

TABLE 7.2
Limited Antigen Binding Assay to Assess Relative Affinities of selected mAbs
			Soluble		Soluble		Soluble
	Soluble		ASGR-1		ASGR-1		ASGR-1
	ASGR-1 2.5 ng/mL		2.5 ng/mL		2.5 ng/mL		2.5 ng/mL
	(FACS		(FACS		(FACS		(FACS
mAb	Geomean)	mAb	Geomean)	mAb	Geomean)	mAb	Geomean)
25A4	17952	48B12	26989	194C1	16937	7E11	4662
26C4	12007	184E7	40198	197G3	17708	22G5	1078
29H8	12179	194A4	38934	198G3	25969	5E5	3278
4A2	16604	4B1	10060	75G3	35840	54E9	6487
4H6	2990	72G9	34014	218G4	15105	6G7	2290
56E5	22648	190F8	13899	193E7	18315	176H4	29444
7F4	4910	191G1	9546	198D2	1872	194C10	21854
7G4	6795	191G10	24154	202A3	2152	12D2	105

C. pH and Calcium Sensitivity

This Example characterizes ASGR-1 antibodies based on the effect of pH and/or calcium on their ability to bind the target. For this example, a label-free, kinetic antibody-ASGR-1 binding assay was employed to assess the sensitivity of the antibodies to changes in pH and calcium. Briefly, the ASGR-1-specific, ligand-competing antibodies were first immobilized and then allowed to bind recombinant, soluble huASGR-1 under physiological conditions (ie. pH 7.4, 1 mM CaCl2). The amount of binding was determined and set to 100%. In order to determine if the antibody-ASGR-1 interaction was sensitive to changes in pH or Ca, the assay buffer was then changed to conditions lacking calcium, a reduced pH (pH 5.6) or both lacking calcium and reduced pH (pH 5.6), and dissociation of ASGR-1 from the mAbs monitored. The amount of ASGR-1 remaining bound under each condition was assessed and expressed as a percent of the starting signal. If a >10% difference in ASGR-1 binding signal was calculated (when compared to that measured under physiological conditions), a particular antibody was classified as being sensitive to that condition. Using this method, the selected antibodies were classified into 5 categories:

1. affected by the removal of calcium

2. unaffected by the removal of calcium or drop in pH

3. affected when both calcium is removed and pH is dropped

4. affected by calcium removal, pH drop and both combined

5. affected by the drop in pH

The relative dissociation of ASGR-1 from antibodies was measured using a label-free assay on an OctetHTX instrument (Fortebio). Antibody samples were captured on anti-HuFc kinetic biosensors (ForteBio cat #18-5064) at 5 ug/mL in assay buffer (10 mM Tris, 0.1% Triton, 150 mM NaCl, 1 mg/mL BSA, 1 mM CaCl2, pH7.4) for three minutes. A one minute baseline stabilization step was performed in assay buffer. Soluble ASGR-1 (Amgen) at 6 ug/ml in assay buffer was added and association to the antibodies was monitored for two minutes. Subsequent dissociation of ASGR-1 from the antibodies was performed by incubating the ASGR-1-mAb complexes for 10 minutes under each of the following conditions:

pH 7.4 + calcium 10 mM Tris, 0.1% Triton, 150 mM NaCl,
                 1 mg/mL BSA, pH 7.4, 1 mM CaCl2
pH 7.4 − calcium 10 mM Tris, 0.1% Triton, 150 mM NaCl,
                 1 mg/mL BSA, pH 7.4
pH 5.6 + calcium 10 mM Tris, 0.1% Triton, 150 mM NaCl,
                 1 mg/mL BSA, pH 5.6, 1 mM CaCl2
pH 5.6 − calcium 10 mM Tris, 0.1% Triton, 150 mM NaCl,
                 1 mg/mL BSA, pH 5.6

The binding signal at the end of the 2 minute association phase for each dissociation experiment was set to 100% and used to represent the maximal level of ASGR-1 binding. After 1 minute of dissociation, the percentage of ASGR-1 remaining bound was calculated. The lower the percent remaining at a given time point indicates increased levels of dissociation in response to the test conditions (ie. different pH and/or calcium concentrations). The change in the percentage of ASGR-1 remaining bound in response to each test condition relative to the percent remaining in the control conditions (ie. pH 7.4+calcium) was determined. Cut-offs for an antibody to be categorized as being sensitive to a particular condition were set to >10% (ie. if >10% of the ASGR-1 dissociates from the antibody under a particular test condition compared to control condition, it was deemed sensitive to that condition). The analysis was done using the 1 minute dissociation time point (except for mAb 149A1 which was binned based on the 4 minute dissociation time point). Using this analysis, the ASGR-1-binding, receptor-ligand blocking antibodies were separated into groups according to their dissociation profiles in response to pH and calcium (Table 7.3). Antibodies belonging to each category were observed.

TABLE 7.3
pH and Calcium Sensitivity of ASGR-1-mAb Interactions
pH and Calcium Sensitivity Determination
(% Change Compared to pH 7.4 + Calcium)
	pH 7.4		pH 5.6			pH and
	minus	pH 5.6 plus	minus	Calcium	pH	calcium
mAb	Calcium	Calcium	Calcium	sensitive	sensitive	sensitive	pH bin
10G6	7%	4%	15%	N	N	Y	3
148E10	7%	19%	33%	N	Y	Y	5
154F4	10%	41%	67%	N	Y	Y	5
159H8	6%	10%	26%	N	Y	Y	5
160B12	6%	8%	22%	N	N	Y	3
175D10	4%	−3%	2%	N	N	N	2
177D2	3%	2%	10%	N	N	Y	3
25A4	2%	−3%	−1%	N	N	N	2
26C4	3%	2%	2%	N	N	N	2
27E7	20%	35%	46%	Y	Y	Y	4
29E2	5%	25%	38%	N	Y	Y	5
29H8	2%	−2%	2%	N	N	N	2
31D12	10%	27%	34%	Y	Y	Y	4
32D6	26%	33%	55%	Y	Y	Y	4
45B4	4%	10%	23%	N	Y	Y	5
49F10	4%	−2%	8%	N	N	N	2
4A2	1%	−3%	1%	N	N	N	2
4B3	12%	33%	45%	Y	Y	Y	4
4H6	5%	−1%	2%	N	N	N	2
50D4	6%	0%	9%	N	N	N	2
50G9	37%	62%	44%	Y	Y	Y	4
51E9	3%	−5%	2%	N	N	N	2
52G11	15%	1%	13%	Y	N	Y	1
52H1	5%	−1%	10%	N	N	N	2
53F2	15%	1%	13%	Y	N	Y	1
53F7	9%	3%	13%	N	N	Y	3
55B1	5%	−2%	4%	N	N	N	2
56E5	1%	−6%	−1%	N	N	N	2
57A7	13%	13%	29%	Y	Y	Y	4
58G11	38%	12%	51%	Y	Y	Y	4
59F2	48%	52%	74%	Y	Y	Y	4
5E5	7%	18%	42%	N	Y	Y	5
60D2	20%	42%	49%	Y	Y	Y	4
60E8	3%	11%	18%	N	Y	Y	5
63A10	8%	3%	47%	N	N	Y	3
63G7	20%	15%	59%	Y	Y	Y	4
64B12	6%	6%	7%	N	N	N	2
65F10	25%	18%	37%	Y	Y	Y	4
68G6	22%	39%	47%	Y	Y	Y	4
6D9	14%	25%	42%	Y	Y	Y	4
6G6	1%	−3%	0%	N	N	N	2
70D1	17%	12%	29%	Y	Y	Y	4
7E11	9%	5%	14%	N	N	Y	3
7F4	4%	6%	9%	N	N	N	2
7G4	2%	1%	7%	N	N	N	2
9G9	25%	38%	55%	Y	Y	Y	4
65E9	22%	30%	35%	Y	Y	Y	4
72B4	32%	26%	43%	Y	Y	Y	4
147D10	13%	4%	11%	Y	N	Y	1
149D11	11%	3%	11%	Y	N	Y	1
149F8	1%	−8%	−1%	N	N	N	2
22G5	40%	35%	No Data	Y	Y	No Data	4*
48B12	4%	−6%	0%	N	N	N	2
52H2	26%	11%	32%	Y	Y	Y	4
6G7	8%	4%	16%	N	N	Y	3
64G12	24%	10%	24%	Y	N	Y	1
72F5	64%	20%	30%	Y	Y	Y	4
147E9	5%	−4%	20%	N	N	Y	3
184E7	1%	−9%	−3%	N	N	N	2
194A4	−1%	−7%	−3%	N	N	N	2
208A2	−4%	−10%	−5%	N	N	N	2
210G10	−3%	−10%	−5%	N	N	N	2
4B1	6%	−5%	−2%	N	N	N	2
62H10	13%	−2%	14%	Y	N	Y	1
72G9	1%	−7%	−1%	N	N	N	2
148H10	45%	10%	47%	Y	N	Y	1
173C11	17%	0%	29%	Y	N	Y	1
179C2	25%	0%	45%	Y	N	Y	1
47C1	13%	−1%	10%	Y	N	Y	1
49C1	72%	23%	64%	Y	Y	Y	4
60C12	14%	−3%	12%	Y	N	Y	1
60G2	36%	7%	31%	Y	N	Y	1
65D5	34%	7%	61%	Y	N	Y	1
66H11	81%	36%	52%	Y	Y	Y	4
73G1	100%	33%	62%	Y	Y	Y	4
51E3	65%	16%	42%	Y	Y	Y	4
53E8	68%	20%	64%	Y	Y	Y	4
54E9	79%	24%	75%	Y	Y	Y	4
56E3	75%	21%	16%	Y	Y	Y	4
190C11	−1%	−6%	−6%	N	N	N	2
190E6	−1%	−12%	−6%	N	N	N	2
190F12	−1%	−6%	−6%	N	N	N	2
190F8	−1%	−5%	−5%	N	N	N	2
190G11	−2%	−8%	−5%	N	N	N	2
190H9	−1%	−6%	−7%	N	N	N	2
191A10	0%	−5%	−5%	N	N	N	2
191G1	−10%	−15%	−11%	N	N	N	2
191G10	0%	−5%	−5%	N	N	N	2
191G12	−2%	−5%	−6%	N	N	N	2
192C10	−1%	−6%	−6%	N	N	N	2
192C8	−9%	−14%	−14%	N	N	N	2
192E4	−2%	−9%	−8%	N	N	N	2
192G6	−1%	−6%	−6%	N	N	N	2
192G8	−1%	−5%	−6%	N	N	N	2
192H10	0%	−5%	−4%	N	N	N	2
193C7	−1%	−8%	−8%	N	N	N	2
194B7	1%	−4%	−4%	N	N	N	2
194C1	−7%	−12%	−8%	N	N	N	2
196C7	−8%	−12%	−12%	N	N	N	2
197B6	−1%	−8%	−7%	N	N	N	2
197E11	−1%	−5%	−4%	N	N	N	2
197F2	0%	−6%	−6%	N	N	N	2
197G3	2%	−3%	−3%	N	N	N	2
198G3	−1%	−4%	−4%	N	N	N	2
213B3	−1%	−7%	−3%	N	N	N	2
219H1	2%	−3%	1%	N	N	N	2
74C8	1%	−7%	−3%	N	N	N	2
74G6	1%	−9%	−4%	N	N	N	2
75G3	−1%	−1%	2%	N	N	N	2
74B2	8%	−9%	−5%	N	N	N	2
74H7	1%	−2%	1%	N	N	N	2
85F7	2%	−2%	2%	N	N	N	2
198B9	3%	2%	11%	N	N	Y	3
199A7	1%	1%	10%	N	N	Y	3
218G4	1%	−4%	0%	N	N	N	2
146A8	2%	−9%	25%	N	N	Y	3
146B6	2%	−5%	13%	N	N	Y	3
149A1	2%	−7%	9%	N	N	Y	3*
172B12	−14%	−27%	−13%	N	N	N	2
172C3	−9%	−26%	0%	N	N	N	2
193E7	−9%	−9%	−4%	N	N	N	2
199E3	−5%	−4%	−4%	N	N	N	2
226F9	100%	51%	77%	Y	Y	Y	4
227C1	100%	54%	73%	Y	Y	Y	4
227F2	80%	50%	100%	Y	Y	Y	4
65C12	13%	0%	23%	Y	N	Y	1
176H4	2%	−4%	26%	N	N	Y	3
194C10	2%	10%	16%	N	Y	Y	5
191E10	−1%	−9%	−9%	N	N	N	2
196F4	−8%	−5%	−6%	N	N	N	2
198D2	−8%	−30%	−28%	N	N	N	2
202A3	−21%	−22%	−23%	N	N	N	2
204G6	−5%	−11%	−10%	N	N	N	2
224G1	77%	41%	65%	Y	Y	Y	4
52D10	21%	3%	45%	Y	N	Y	1
64E2	48%	29%	49%	Y	Y	Y	4
*No actual data; bin predicted on the totality of information regarding the antibody.

D. Relative Epitope Binning/Profiling

A common way to characterize epitopes is through competition experiments. Antibodies that compete with each other can be thought of as binding the same or overlapping site on the target. This example describes a method of determining competition for binding to hASGR-1 and the results of the method when applied to a number of antibodies described herein.

Binning experiments can be conducted in a number of ways, and the method employed may have an effect on the assay results. Common to these methods is that ASGR-1 is typically bound by one reference antibody and probed by another. If the reference antibody prevents the binding of the probe antibody then the antibodies are said to be in the same bin. The order in which the antibodies are employed is important. If antibody A is employed as the reference antibody and blocks the binding of antibody B the converse is not always true: antibody B used as the reference antibody will not necessarily block antibody A. There are a number of factors in play here: the binding of an antibody can cause conformational changes in the target which prevent the binding of the second antibody, or epitopes which overlap but do not completely occlude each other may allow for the second antibody to still have enough high-affinity interactions with the target to allow binding. In general, if competition is observed in either order the antibodies are said to bin together, and if both antibodies can block each other then it is likely that the epitopes overlap more completely.

For this example, a modified antibody-antibody competition assay was used to determine the relative epitope binning profiles of the ASGR-1 specific, ligand blocking antibodies in a high throughput manner. Briefly, individual antibodies were tested for their ability to compete for binding with a panel of reference antibodies chosen based on their different binding characterstics (eg. species cross reactivity, HEPG2 binding, etc.) and primary sequences. The pattern of competition/binding of each test antibody with the reference antibody panel was then determined and compared to those produced from the other test antibodies. The degree of correlation between the individual test antibody competition/binding profiles was then compared. Antibodies that showed similar competition/binding profiles were binned (grouped) together (eg. Binning Profile A, B, etc.).

Biotinylated recombinant soluble human ASGR-1 protein was coupled to streptavidin coated, uniquely barcoded LumAvidin Beads® (LumAvidin Microspheres, Cat#L101-LXXX-01; Luminex Corp., Austin, Tex., U.S.A.) for 45 minutes in the dark at room temperature and washed twice. The reference antibody hybridoma supernatant samples were incubated with the antigen-coated beads for 1 hour in the dark at room temperature and washed three times. Beads were resuspended in FACS buffer containing Stabilguard®. The antigen-coated, reference antibody-bound beads were pooled and then divided into individual sample wells containing a normalized (2.5 ug/ml) test antibody (hybridoma supernatant) sample (or negative control), incubated for 1 hour in the dark at room temperature and washed twice. The samples were then incubated with Alexa Fluor® 488 IgG fragment-specific detection antibody for 15 minutes in the dark at room temperature, washed once and resuspended in FACS buffer. FACS buffer supplemented with 1 mM Calcium Chloride was used in all steps. Samples were analyzed using an Intellicyt iQue™ Screener Platform.

To determine the antibody competition/binding profiles of the individual test antibodies, the reference-only antibody binding signal was subtracted from the reference plus test antibody signal for each competition/binding reaction (ie. across the entire reference antibody set). An individual antibody binding profile was defined as the collection of net binding values for each competition/binding reaction. The degree of similarity between individual profiles was then assessed by calculating the coefficient of determination between each of the test antibody profiles. Test antibodies showing high degrees of similarity (R²≧0.8) to each other were then grouped into common binning profiles. Separate binning profiles were only defined if there were two or more samples with a high degree of correlation. If individual unique antibody binning profiles were observed (ie. they displayed a low degree of similarity to other test antibody binding profiles), the bin was classified as unknown. Using this method, the ASGR-1-binding, receptor-ligand blocking antibodies were sub-divided into 14 unique binning profiles (A, B, C, D, E, L, M, N, O, P, Q, R, T and unknown) (Table 7.4). Antibodies that displayed a unique binning profile (as defined above) but shared a relatively high degree of similarity to another profile (R²=0.6-0.8) were categorized as a sub-bin (ie. A. 1, A. 2, etc.) of that profile.

TABLE 7.4
Relative Epitope Binning/Profiling of ASGR-1 Specific
Receptor-Ligand Blocking mAbs
							Epi-
	Epitope		Epitope		Epitope		tope
mAb	BIN	mAb	BIN	mAb	BIN	mAb	BIN
10G6	A	52H1	A	9C11	A.3	60G2	E
11E2	A	53F2	A	12B12	B	65D5	E
11F5	A	53F7	A	147D10	B	66H11	E
12E9	A	55B1	A	149D11	B	71A6	E
12F11	A	56E5	A	149F8	B	73G1	E
12F12	A	57A7	A	151B9	B	49C5	E.1
13F6	A	58G11	A	175F4	B	49D10	E.1
148E10	A	59F2	A	22G5	B	51E3	E.1
154F4	A	5E5	A	48B12	B	51F4	E.1
159H8	A	60D2	A	52H2	B	53E8	E.1
160B12	A	60E8	A	6G7	B	54E9	E.1
175D10	A	63A10	A	7G2	B	56E3	E.1
177D2	A	63G7	A	64G12	B.1	56G1	E.1
25A4	A	64B12	A	72F5	B.1	190C11	L
25D12	A	65F10	A	147E9	C	190E6	L
26C4	A	68G6	A	184E7	C	190F12	L
27E7	A	6A6	A	194A4	C	190F8	L
28H2	A	6D4	A	208A2	C	190G11	L
29E2	A	6D9	A	210G10	C	190H9	L
29E6	A	6G6	A	4B1	C	191A10	L
29H8	A	70D1	A	60E12	C	191G1	L
31D12	A	7A10	A	61A1	C	191G10	L
32D6	A	7C3	A	62H10	C	191G12	L
3G7	A	7E11	A	63H8	C	192C10	L
45B4	A	7F4	A	72G9	C	192C8	L
49F10	A	7F8	A	8D8	D.1	192E4	L
4A2	A	7G4	A	12D2	E	192G6	L
4B3	A	8D12	A	148H10	E	192G8	L
4H6	A	9F12	A	173C11	E	192H10	L
50D4	A	9G9	A	179C2	E	193C7	L
50G9	A	65E9	A.1	47C1	E	194B7	L
51E9	A	72B4	A.1	49C1	E	194C1	L
52G11	A	7H7	A.2	60C12	E	196C7	L
197B6	L	197F2	L	198G3	L	219H1	L
197E11	L	197G3	L	213B3	L	74C8	L
74G6	L	74H7	M.1	218G4	O	172B12	Q
75G3	M	85F7	M.1	146A8	P	172C3	Q
89A11	M	198B9	N	146B6	P	193E7	Q
74B2	M.1	199A7	N	149A1	P	199E3	Q
226F9	Q	227F2	Q	176H4	R
227C1	Q	65C12	Q	194C10	T

E. Epitope Mapping—Arginine/Glutamic Acid Mutational Profiling

This Example characterizes ASGR-1 antibodies based on the effect of mutagenesis of ASGR-1 on their ability to bind the target. Previous data indicated that the ASGR-1 CBD is primarily responsible for antibody binding for the panel of antibodies. As such, only the ASGR-1 CBD was considered structurally in the context of the full length ASGR-1 in the design of mutation sites.

Arginine/Glutamic acid mutational mapping was used to characterize epitopes bound by human ASGR-1-specific, ligand blocking antibodies. Briefly, 144 individual point mutations were made across the CBD domain of human ASGR-1 protein (SEQ ID NO:5) starting at position 148. Ninety-one constructs, representing surface residues (modelled using the ASGR-1 crystal structure in the PyMOL Molecular Graphics System (Version 1.8; Schrödinger, LLC.)) and therefore potentially accessible for antibody binding, were selected for these assays. Mutant hASGR-1 variants were constructed such that non-arginine residues were changed to arginine and where wild type arginine residues were mutated to glutamic acid. Each mutant hASGR-1 sequence was then cloned into a mammalian expression vector and used to transiently transfect CHOs cells. The ability of human ASGR-1-specific, ligand competing antibodies to bind to the mutant hASGR-1 proteins was assessed by FACS as described above.

Antibodies were tested for binding to the individual mutant and wild type ASGR-1 constructs using normalized antibody concentrations (5 ug/ml). CHO—S cells transiently expressing the appropriate mutated or non-mutated antigen of interest were mixed with antibody sample or controls, incubated for 1 hour at 4° C., and then washed twice. Cells with bound antibody were then incubated with Alexa Fluor® 647 IgG Fc fragment-specific detection antibody and 7-AAD viability stain for 15 minutes at 4° C., washed once and resuspended in FACS buffer. Samples were analyzed using a BD Accuri™ Flow Cytometer and an Intellicyt HyperCyt Autosampler. As a negative control, supernatants and controls were also screened against CHO—S cells transfected with empty parental vector (referred to as mock). In order to exclude mutants that were poorly expressed or produced mis-folded antigen, only constructs that yeilded a binding data average of at least 25% or greater compared to the average binding observed on wildtype hASGR-1 was used for further analysis. Because mutant hASGR-1 expression levels varied relative to each other, sample binding data for each construct was normalized for expression by dividing the binding data from an antibody not affected by the mutations (e.g., 65C12) by the binding values of each test antibody on a given mutant construct. Also, because the antibody binding affinities varied amongst the samples, the expression corrected data (above) was further normalized by comparing test antibody binding on each mutant construct to wild type hASGR-1. Identification of specific mutations that affected test antibody binding was performed by an interquartile range (IQR) analysis to determine statistical outliers. A mutation was identified as a “hit” if the calculated values were ≧3× the IQR (above the 3^rd quartile/upper fence) for a given mutant construct. Although IQR analysis was used here to determine signifance and identify hits, one skilled in the art will recognize that a number of methods could be employed in order to normalize the data (eg. using epitope-tagged constructs or other ASGR-1-binding antibodies directed against non-CBD epitopes). Any statistically significant reduction in antibody binding signal to a mutant construct (compared to that determined for binding to wild type ASGR-1) determined by these methods could be used for hit identification.

For illustrative purposes, Table 7.5 shows the IQR analysis with a single mutant construct (i.e., H203).

The grayed values for antibodies 4B3, 50G9, 60D2, 59F2, 60E8, and 65E9 represent the statistically significant hits (i.e., ≧3× the IQR) whose binding was affected by mutations H203.

A summary of the hASGR-1 residues important for binding of the representative antibodies is shown in Table 7.6. In addition, this analysis revealed that the mutation of some ASGR-1 residues had more dramatic effects on a given antibody binding than others. This likely reflects the relative contribution or importance that these residues have in mediating interactions with specific test antibodies. The degree by which each mutation impacted the ability of a test antibody to bind was determined by calculating the magnitude of an individual binding data point above the upper gate determined by each IQR analysis. The relative impact of each mutation on the binding of a given test antibody was then ranked using this method and displayed as a heatmap in Table 7.6. Dark grey coloring indicates the data point deviated dramatically from the upper gate (ie. a large effect on antibody binding), while light grey/white indicates the data point was very close to the cut offs (ie. 3× the IQR)(Table 7.6). When aligned with the relative epitope profiling bin assignments (Example 7D above), this analysis reveals a set of core ASGR-1 amino acid positions that, when mutated, disrupt test antibody binding. As such, these positions are likely part of the ASGR-1 epitopes bound by the selected antibodies. These amino acid residues either directly contact or are involved in the interaction with the antibody, or are in close enough proximity that, when mutated, interfere with antibody binding. Amino acid positions identified as statistically significant hits, but barely made the cut offs, and map to surface ASGR-1 locations distinct from the main epitope bins (FIG. 47) may represent residues that, when mutated, disrupt the conformation of ASGR-1 such that an antibody that binds to a distinct epitope is affected (ie. an indirect effect). mAb 197G3 is an example of an antibody displaying a range of binding sensitivities in this assay, yet the most important residues (R274 and R271) can be identified by rank ordering them as described.

In order to compare the mutational hit patterns of the individual test antibodies with each other, the coefficient of determination between the test antibodies was determined. The expression and antibody binding normalized data set was used to generate binding profiles for each test antibody across the mutant panel. The resulting profiles for each individual test antibody were then compared for their degree of similarity to all of the other test antibodies. The coefficient of determination (R²) for each combination was determined and converted into a heat map in order to visualize the resulting patterns (FIG. 46). For simplicity, a representative antibody from each unique mutational profile (Reference Antibody) is shown in FIG. 46. This analysis revealed 7 predominant hit patterns or mutational clusters. Test antibodies affected by the 7 predominant mutational clusters correspond to those from competition/binding binning profiles A, B, C, E and L (3 distinct hit/mutational clusters of bin A antibodies and 1 distinct hit/mutational cluster of bin B, bin C, bin E and bin L antibodies). The remaining antibodies, categorized as displaying separate binning profiles (compared to bins A, B, C, E and L), are affected by distinct mutations in ASGR-1, but also include residues that partially overlap with test antibodies belonging to the predominant bins.

This data indicates the selected antibodies bind to epitopes that partially overlap with the 7 predominant epitope regions. The residues important for the binding of antibodies belonging to the 7 predominant epitope regions were then mapped onto a computer representation of the surface of the ASGR-1 structure using the PyMOL Molecular Graphics System (Version 1.8; Schrödinger, LLC.) (FIG. 47). A residue on the surface of ASGR-1 was considered part of the same epitope region if at least one antibody from a distinct binning profile (ie. A, B, C, E and L) was identified as being sensitive to mutation. For example, the predominant epitope region for antibodies belonging to binning profile C includes hASGR-1 residues P241, D242, D243, Y245, G251 and E253 (SEQ ID NO:5). The binding of antibody 147E9 is affected by mutation of all of these residues, while antibody 184E7 is only disrupted by mutation of P241, D243 and E253. Thus, the predominant epitope region of ASGR-1 bound by antibodies belonging to binning profile C is defined as including one or more of (but not limited to) P241, D242, D243, Y245, G251 and E253 (SEQ ID NO:5). Also, note that the antibody 194A4 was classified as belonging to Bin C as determined in Example 7D, however, the results of this arginine/glutamic acid mutational profiling (as well as the results from crystal structure analysis of the ASGR-1 CBD/194A4 complex described in Example 10H) suggests that the relative epitope profiling may have been inaccurate.

Antibodies belonging to binning profile A were further sub-divided into 3 distinct mutational clusters. These clusters mapped to ASGR-1 surface positions that overlap with, or are in extremely close physical proximity to, each other consistent with a common binning profile. Antibodies that displayed binning profiles distinct from the 5 major bins (i.e., A, B, C, E and L) also showed distinct patterns of mutations that affected their binding (FIG. 46). Some binning profiles (R, O, M, M. 1 and T) share significant overlap with antibodies from binning profile L, and can be considered sub-bins of this profile. Taken together, this data indicates that antibodies capable of blocking ASGR-1-ligand interactions bind to 5 major epitope regions. In addition, blocking antibodies were identified that bind to partially overlapping epitopes of these major regions.

Example 8: ASGR Internalization Assay

To determine whether the antibodies bind and also prevent internalization of ASGR-1 into cells expressing ASGR-1, an in vitro internalization assay is performed of various antibody samples.

Human ASGR-1 Internalization Cellular Imaging Assay Protocol

Reagents:

U2OS (Human Osteosarcoma) cell line

McCoy's 5A Medium: Gibco, #16600-082

MEM NEAA (100×): Gibco, #11140-050

Penicillin-Streptomycin (10,000 U/ml, 100×) Gibco, #15140-122

L-Glutamine (100×): Gibco, #25030-081

Fetal Bovine Serum: Gibco, #16000-044

DPBS (without Ca and Mg): Gibco, #14190-136
DPBS (with Ca and Mg): Gibco, #14040-133

Cell Dissociation Buffer: Gibco, #13151-014

1 Liter Filter: Corning, #430517

Hepes Buffer (1M): Gibco, #15630-080

BacMam Virus—huASGR-1: GS: SNAP26f

β-GalNAc-PAA-Biotin: GlycoTech, #01-011

SNAP-Surface Alexa Fluor 546: New England Biolabs, #S9132S

Streptavidin-Alexa Fluor 633: Life Technologies, #S21375

Hoechst 33342: Invitrogen, #H3570

Pitstop2: abcam Biochemical, #ab120687
Pitstop2—negative control: abcam Biochemical, #ab120688

Paraformaldehyde (8% Aqueous Solution): Electron Microscopy Sciences, #157-8-100

Imaging plate—96 well Optical Bottom: Thermo Scientific Nunc, #165305

Operetta High Content Imager: Perkin Elmer

U2OS Complete Growth Medium:

McCoy's 5A with 10% FBS, 1×MEM NEAA, 1XL-Glutamine, and 1× Penicillin-Streptomycin
Medium was filtered before use on cells

U2OS Cell Plating and Culturing:

U2OS cells were grown to 75-85% confluence in T175 before plating into a 96 well plate.
1. The U2OS culture medium was aspirated off the cells in the T175 flask
2. Cells were washed with 10 mls of DPBS and aspirated off
3. 3 mls of Cell Dissociation Buffer was added to the cells and incubated for 5 minutes inside a cell incubator (37° C., 5% CO2) to detach the cells from the T175 flask.
4. The detached cells were diluted with 7 mls of the growth medium
5. 1 ml of cells were used to count the number of cells available to plate
6. The cells were diluted in growth medium to give a final concentration of 28,000 cells/well and BacMam virus (huASGR-1: GS: SNAP26f) was also added to the cells at this time with the desired concentration (MOI).
7. The cells were mixed together with the BacMam virus for 1-2 minutes and then plated on the 96 well imaging plate at a volume of 100 ul/well.
8. The plate was placed inside an incubator (37° C., 5% CO2) for 16-20 hours before treatment.

Treatment of Cells (16-20 Hours Incubation)

1. The next day, the medium on the 96 well plate was dumped out and washed once with DPBS.
2. McCoy's 5A Medium plus 10 mM of Hepes buffer (assay buffer) was added to the cells (100 ul) for 1 hour inside the incubator.
3. After the 1 hour incubation, the medium was dumped out and washed once with DPBS containing Ca and Mg.
4. Pitstop2 and Pitstop2 negative control were prepared in assay buffer at 20 uM.
5. Volume of 100 ul per well of the inhibitors were added to the U2OS cells for 15 minutes inside the incubator.
6. GalNAc-biotin (100 nM) and strepavidin-Alexa633 (100 nM) were pre-mixed in assay buffer and incubated for 10 minutes at room temperature.
7. SNAP-Surface Alexa Fluor 546 (2.5 uM) was prepared in assay buffer.
8. After the 15 minutes incubation, both GalNAc-biotin-strepavidin-Alexa633 and SNAP-Surface Alexa Fluor 546 were directly added (10 ul) to the medium containing Pitstop2 inhibitors for 30 minutes inside the incubator.
9. After the 30 minutes incubation, medium was dumped out and the cells were washed once with DPBS.
10. The cells were fixed by adding 50 ul of 4% Paraformaldehyde (8% paraformaldehyde was diluted with DPBS) containing Hoechst dye (1:5000 dilution) to the cells for 10 minutes at room temperature.
11. After 10 minutes incubation, the cells were washed twice with DPBS and 100 ul of DPBS was added to each well.
12. The plate was imaged on the Operetta instrument with three channels measuring the different fluorescence dyes.
1) Hoechst was measured using filters in the range of excitation: 360-400 nm and emission: 410-480 nm
2) GalNAc-biotin-strepavidin-Alexa633 was measured using filters in the range of excitation: 600-630 nm and emission: 640-680 nm
3) SNAP-Surface Alexa Fluor 546 was measured using filters in the range of excitation: 520-550 nm and emission: 560-630
13. Harmony 3.5 software (Perkin Elmer) was used to identify and quantify internalized spots for fluorescence dyes added in the assay.
This internalization assay can be performed to assay the antigen binding proteins of the invention to determine how much they reduce or inhibit internalization of ASGR, ASGR-1, and/or ASGR-2.

Example 9: Additional Ligand Blocking Assays

Preparation of Desialated Protein Ligands (Asialofetuin and Orosomucoid)

A. Asialofetuin

Bovine fetuin (AHSG) was obtained commercially (Sigma) and purified using a CaptoQ Impres (GE Healthcare Life Sciences) matrix. Briefly, the material was loaded in 25 mM TRIS pH 7.9 at up to 17 mg/ml resin, resolved in 20 mM BisTRIS (pH6.5) with a gradient of sodium chloride. The main peak was gradient pooled (˜0.15M NaCl final) and resolved on a SuperDex200 SEC (GE Healthcare Life Sciences) in Hepes-buffered saline (pH 7.9). The purified AHSG was then concentrated and incubated with Innolink Biotin 354S (EMD Millipore) according to the manufacturer's instructions. The biotinylated protein was then desalted by gel filtration and concentrated once again.

The purified, biotinylated protein was subsequently desialated by incubation with C. perfringens neuraminidase (Sigma; 1 unit/10 mg protein for 12 hours at 37° C. in 50 mM sodium phosphate, 9 mM HEPES, 0.12M NaCl, pH6). The resulting material was harvested and digested for an additional 3 hours with A. ureafaciens neuraminidase (QAbio; 0.5 units/10 mg protein at 37° C.). The digested sample was diluted 3 fold with 20 mM HEPES containing 0.15M NaCl (pH 7.5) (HBS) to neutral pH and applied to a monomeric Avidin agarose (Pierce) HR16/10 column, run at 60 cm/hour. The loaded column was held for 15 minutes then washed with four column volumes of HBS. The biotinylated, desialated protein was finally eluted with three column volumes of HBS containing 2 mM Biotin plus an additional two column volumes of 0.1M Glycine-HCl (pH 2.8), which was immediately neutralized during collection with 50 mM TRIS Base). Protein-containing fractions from both types of elutions were identified, pooled, concentrated, dialyzed extensively against 10 mM HEPES, 0.14M NaCl (pH 7.5), re-concentrated and finally filtered sterilized. The purified lots were then analyzed by SDS-PAGE and mass spectrometry prior to use in the described assays.

B. Orosomucoid

Bovine orosomucoid (AGP) was obtained commercially (Sigma) and purified over SuperDex200 resin equilibrated in HBS (pH7.9) by size exclusion chromatography. The front of the main AGP peak was combined from 3 individual runs to generate hyperglycosylated AGP, with the remainder of the main peaks (from the 3 combined runs) to generate hypoglycosylated AGP. For biotinylation, the purified AGP was concentrated to 5 mg/ml and incubated with Innolink Biotin 354S as described. The biotinylated protein was then desalted by gel filtration and concentrated.

After biotinylation, the protein was desialated by incubating it for 18 hours at 37° C. with one unit of C. perfringens neuraminidase (Sigma) per 10 mg protein in 50 mM sodium phosphate, 9 mM HEPES, 0.12M NaCl (pH6). The resulting material was harvested and digested for an additional 6 hours at 37° C. with 0.5 units A. ureafaciens neuraminidase (QAbio) per 10 mg protein. The sample was diluted 3 fold with HBS to achieve a neutral pH and applied to a monomeric Avidin agarose (Pierce) HR16/10 column, run at 60 cm/hour. The loaded column was held for 15 minutes and then washed with four column volumes of HBS. The biotinylated, desialated protein was subsequently eluted with three column volumes of HBS containing 2 mM Biotin, plus two column volumes 0.1M Glycine-HCl (pH 2.8), which was immediately neutralized during collection with 50 mM TRIS Base. Protein-containing fractions from both types of elutions were identified, pooled, concentrated, dialyzed extensively against 10 mM HEPES, 0.14M NaCl (pH 7.5), re-concentrated and finally filtered sterilized. The purified lots were then analyzed by SDS-PAGE and mass spectrometry prior to use in the described assays.

These ligands can be used in additional ligand binding assays to determine antigen binding protein inhibition of ligand binding to ASGR, ASGR-1 and/or ASGR-2.

Example 10: Crystal Stucture Analysis of Interaction Between Ligands and ASGR-1 and Antibodies and ASGR-1

A. Crystal Structures of ASGR-1 Carbohydrate Binding Domain with Ligand Bound

Introduction

The crystal structure of ligand free ASGR-1 CBD (carbohydrate binding domain) has been previously described (1). Protein expression of ASGR-1 CBD (SEQ ID NO:5), purification and crystallization was performed similar to the published method, however the structures described here differ from the published crystal structure. Analysis of these structures shows extra N- and C-terminal amino acids compared to the published structure, how various ligands interact with the ASGR-1 carbohydrate binding domain, and possible selectivity determinants between ASGR-1/ASGR-2 for various saccharides.

Results

Lactose Binds in the Carbohydrate Binding Pocket of ASGR-1

Protein crystals of the ASGR-1/Lactose complex were grown and the crystal structure was determined at 2.05 Å. Although a method similar to that of the published structure was followed, clear electron density is present for the lactose disaccharide in the carbohydrate binding pocket. See FIGS. 18A and 18B. In this structure, the galactose ring of the lactose disaccharide sits on top of the calcium ion at the carbohydrate binding domain and forms the majority of the contacts with the ASGR-1 protein. Hydrogen bonds are formed between lactose and ASGR-1 amino acids Q240, D242, E253, and N265. Additionally, van der Waals interactions are formed with at least W244 (SEQ ID NO:5). See FIG. 18C.

Analysis of the crystal structure identifies specific amino acids involved in the interaction between ASGR-1 and lactose. Interacting with at least these amino acids by an alternate molecule can completely or partially affect the interaction between ASGR-1 and lactose.

ASGR-1/Lactose Analysis (Distances Below were Calculated with PyMOL):

Amino acids with at least one non-hydrogen atom 4.5 Å or less to the bound lactose molecule were identified and include: Q240, D242, W244, E253, N265, D266, D267 (SEQ ID NO:5).

Amino acids with at least one non-hydrogen atom 5 Å or less to the bound lactose molecule were identified and include: Q240, D242, W244, E253, N265, D266, D267 (SEQ ID NO:5).

Amino acids with at least one non-hydrogen atom 5-8 Å from the bound lactose molecule were identified and include: N209, R237, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, D260, V268, R271, Y273 (SEQ ID NO:5).

Galactose Binds in the Carbohydrate Binding Pocket of ASGR-1 Similar to Lactose

Protein crystals of the ASGR-1/Galactose complex were grown and the crystal structure was determined at 2.4 Å. Although a method similar to that of the published structure was followed, clear electron density is present for the galactose saccharide in the carbohydrate binding domain. See FIGS. 19A and 19B.

In this structure, galactose sits on top of the calcium ion at the carbohydrate binding site and forms contacts with the ASGR-1 protein. Hydrogen bonds are formed between galactose and ASGR-1 amino acids Q240, D242, E253, and N265 (SEQ ID NO:5). Additionally, van der Waals interactions are formed with at least W244. See FIG. 19C.

Analysis of the crystal structure identifies specific amino acids involved in the interaction between ASGR-1 and galactose. Interacting with at least these amino acids by an alternate molecule may completely or partially affect the interaction between ASGR-1 and galactose. Distances below were calculated with PyMOL.

ASGR-1/Galactose Analysis (Distances Below were Calculated with PyMOL):

Amino acids with at least one non-hydrogen atom 4.5 Å or less to the bound galactose molecule were identified and include: R237, Q240, D242, W244, E253, N265, D266, D267 (SEQ ID NO:5). Amino acids with at least one non-hydrogen atom 5 Å or less to the bound lactose molecule were identified and include: R237, Q240, D242, W244, E253, N265, D266, D267 (SEQ ID NO:5).

Amino acids with at least one non-hydrogen atom 5-8 Å from the bound lactose molecule were identified and include: N209, P238, E239, P241, D243, Y245, G246, H247, G252, C255, H257, T259, V268, R271, Y273 (SEQ ID NO:5).

When comparing the ASGR-1/Lactose and ASGR-1/Galactose structures, the galactose rings of each saccharide superimpose very well. One difference in the proteins in the two structures is the conformation of R237, an amino acid in close proximity to the carbohydrate binding site. In the superimposition shown in FIG. 20, the ASGR-1/Lactose structure is shown in white and the ASGR-1/Galactose structure is shown in black.

N-Acetyl-D-Galactosamine (GalNAc) Binds in the Carbohydrate Binding Pocket of ASGR-1 Similar to Galactose, Buts Forms Additional Interactions

Protein crystals of the ASGR-1/GalNAc complex were grown and the crystal structure was determined at 2.2 Å. Although a method similar to that of the published structure was followed, clear electron density is present for the GalNAc saccharide in the carbohydrate binding pocket. See FIG. 21A and FIG. 21B.

In this structure, GalNAc sits on top of the calcium ion at the carbohydrate binding site and forms contacts with the ASGR-1 protein. Hydrogen bonds are formed between GalNAc and ASGR-1 amino acids Q240, D242, E253, and N265. Additionally, van der Waals interactions are formed with at least W244. In this structure, R237 is in a similar conformation as observed in the galactose complex. However, in this case hydrogen bonds are formed between R237 and the acetyl of GalNAc. These additional interactions with R237 help explain both the observed tighter binding of GalNAc (than galactose) to ASGR-1, and the tighter binding to GalNAc to ASGR-1 (than ASGR-2, in which this amino acid is Ala rather than Arg). See FIG. 21C

ASGR-1/GalNAc Analysis (Distances were Calculated with PyMOL):

Analysis of the crystal structure identifies specific amino acids involved in the interaction between ASGR-1 and GalNAc. Interacting with at least one of these amino acids by an alternate molecule may completely or partially inhibit the interaction between ASGR-1 and GalNAc.

Amino acids with at least one atom 4.5 Å or less to the bound GalNAc molecule were identified and include: N209, R237, Q240, D242, W244W244, E253, H257, T259, N265, D266, D267, Y273 (SEQ ID NO:5). Amino acids with at least one non-hydrogen atom 5 Å or less to the bound lactose molecule were identified and include: N209, R237, Q240, D242, W244, E253, H257, T259, N265, D266, D267, Y273 (SEQ ID NO:5).

Amino acids with at least one non-hydrogen atom 5-8 Å from the bound lactose molecule were identified and include: P238, E239, P241, D243, Y245, G246, H247, G252, C255, F258, D260, R263, W264, V268, R271 (SEQ ID NO:5).

The coordinates for the ASGR-1 CBD/GalNAc crystal structure complex are presented in Table 10.1.

Methods

ASGR-1 Expression and Purification

For all chrystallography experiments in Example 12, Human ASGR-1 CBD protein (SEQ ID NO:5) was expressed in E. coli and refolded and purified.

ASGR-1 Crystallization

Purified human ASGR-1 CBD (148-291) protein was concentrated to 8-12 mg/ml. ASGR-1/carbohydrate complex crystals grow in 0.1 M sodium cacodylate pH 6.8, 0.08 M ammonium sulfate, 21-23% PEG 8000 in the presence of 20 mM ligand (lactose, galactose or GalNAc).

Data Collection and Structure Determination

Datasets for ASGR-1 CBD complexes were collected on a Rigaku FR-E X-ray source (ASGR-1/Lactose and ASGR-1/Galactose) or at Berkeley Advanced Light Source beamline 5.0.2 (ASGR-1/GalNAc). All datasets were processed with iMosflm(2) and scaled with AIMLESS(3) from the CCP4 program suite(4).

ASGR-1/Lactose crystals grow in the C2 space group with unit cell dimensions a=113.5, b=32.3, c=40.4 Å, β=92.3° with one complex molecule per asymmetric unit, and diffract to 2.05 Å resolution. The ASGR-1 structure was solved by molecular replacement with the program PHASER(5) using the published ASGR-1 structure(1) as the starting search model. The structure was improved with multiple rounds of model building with Coot(6) and refinement with PHENIX(7). The refined structure has R=18.9 and R_free=24.4.

ASGR-1/Galactose crystals grow in the C2 space group with unit cell dimensions a=113.1, b=32.7, c=40.7 Å, β=91.6° with one complex molecule per asymmetric unit, and diffract to 2.4 Å resolution. The ASGR-1/Lactose structure was used as the starting molecule for molecular replacement, and model building and refinement were performed as described for the ASGR-1/Lactose complex to R=15.8 and R_free=22.9.

ASGR-1/GalNAc crystals grow in the C2 space group with unit cell dimensions a=112.7, b=32.3, c=40.5 Å, β=91.7° with one complex molecule per asymmetric unit, and diffract to 2.2 Å resolution. The ASGR-1/Lactose structure was used as the starting molecule for molecular replacement, and model building and refinement were performed as described for the ASGR-1/Lactose complex to R=16.5 and R_free=23.0.

Structure analysis and distance calculations were performed with the program PyMOL(8).

REFERENCES

• 1. Meier, M., Bider, M. D., Malashkevich, V. N., Spiess, M., and Burkhard, P. (2000) Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. Journal of molecular biology 300, 857-865
• 2. Battye, T. G., Kontogiannis, L., Johnson, O., Powell, H. R., and Leslie, A. G. (2011) iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta crystallographica 67, 271-281
• 3. Evans, P. (2006) Scaling and assessment of data quality. Acta crystallographica 62, 72-82
• 4. CCP4. (1994) The CCP4 suite: programs for protein crystallography. Acta crystallographica 50, 760-763
• 5. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., and Read, R. J. (2007) Phaser crystallographic software. Journal of applied crystallography 40, 658-674
• 6. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Features and development of

Coot. Acta crystallographica 66, 486-501

• 7. Adams, P. D., Afonine, P. V., Bunkoczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta crystallographica 66, 213-221
• 8. DeLano, W. L. (2002) The PyMOL Molecular Graphics System. Palo Alto

B. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 5E5

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 5E5, determined to 1.95 Å resolution (the conditions for which are described in the below). This structure, depicted in FIGS. 22A&B, shows that when 5E5 binds to/interacts with ASGR-1, a conformational rearrangement of the carbohydrate binding loop occurs, impairing the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). This demonstrates that the 5E5 Fab indirectly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 5E5 with ASGR-1. This was defined as residues that are within 5 Å of the 5E5 protein. The core residues are as follows: H161, E162, W195, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, K234, N235, W236, R237, P238, D261, G262, R263 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 5E5. These residues were ASGR-1 residues that were from 5-8 Å of the 5E5 protein. The boundary residues are as follows: V159, E160, R163, T193, S194, E197, V201, I205, G206, P207, Y229, E230, T231, E239, F258, T259, D260, W264 (SEQ ID NO:5).

Specific core 5E5 amino acid residues of the interaction interface with ASGR-1 were defined as 5E5 residues that are within 5 Å of the ASGR-1 protein. The core 5E5 Heavy Chain residues include: S30, N31, W52, Y53, D54, S56, N57, Y59, Y101, S102, S103, G104, W105, Y106, D107; and the core 5E5 Light Chain residues include: 5E5 Light Chain: Q27, R30, D32, H91, Y92, S93, Y94.

Boundary 5E5 amino acid residues of the interaction interface with ASGR-1 were defined as 5E5 residues that are 5-8 Å from the ASGR-1 protein. The boundary 5E5 Heavy Chain residues include: Y32, V33, V50, G55, K58, N74, E99, V100, Y108; and the boundary 5E5 Light Chain residues include: I2, G28, I29, L33, Q90, P95, R96.

Methods

Expression and Purification of Protein Samples

The 5E5 Fab fragment was generated by cleaving the 5E5 mAb with caspase 3. Post caspase cleavage, the Fab was isolated by purification on a MonoS ion exchange column. Ni Sepharose Excel subtraction was then performed to ensure the Fc domain was removed from the sample.

5E5 mAb Heavy Chain (SEQ ID NO: 32695):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSNYVMHWVRQAPGKGLEWVA
VIWYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCTR
EVYSSGWYDYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAA
LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPS
SSLGTQTYICNVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPA
PELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD
GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALP
APIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIA
VEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV
MHEALHNHYTQKSLSLSPGHHHHHH
5E5 mAb Light Chain (SEQ ID NO: 32696):
DIQMTQSPSSLSASVGDRVTITCRASQGIRNDLGWYQQKPGKAPKRLIY
AASSLQSGVPSRFSGSGSGTEFTLTISSLQPEDFATYYCLQHYSYPRTF
GQGTKVEVKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQ
WKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEV
THQGLSSPVTKSFNRGEC
5E5 Fab Heavy Chain (Post Cleavage) (SEQ ID NO:
32697):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSNYVMHWVRQAPGKGLEWVA
VIWYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCTR
EVYSSGWYDYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAA
LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPS
SSLGTQTYICNVNHKPSNTKVDKKVEPKSCGSDEVD
5E5 Fab Light Chain (Post Cleavage) (SEQ ID NO:
32698):
DIQMTQSPSSLSASVGDRVTITCRASQGIRNDLGWYQQKPGKAPKRLIY
AASSLQSGVPSRFSGSGSGTEFTLTISSLQPEDFATYYCLQHYSYPRTF
GQGTKVEVKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQ
WKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEV
THQGLSSPVTKSFNRGEC

Complex Formation and Crystallization

The ASGR-1 CBD/5E5 Fab complex was made by mixing a molar excess of ASGR-1 CBD with 5E5 Fab. The complex was separated from excess ASGR-1 by purification on a size exclusion chromatography column. The ASGR-1 CBD/5E5 Fab complex was concentrated to 10 mg/ml and crystallizes in 0.1 M Tris pH 8.5, 12% PEG 4000.

Data Collection and Structure Determination

The dataset for the ASGR-1 CBD/5E5 Fab complex crystal was collected on beamline 5.0.2 at the Berkeley synchrotron and processed with Mosflm¹/Aimless².

ASGR-1 CBD/5E5 Fab complex crystals grow in the P2₁ space group with unit cell dimensions a=62.93, b=41.75, c=118.89 Å and β=97.16 with one complex molecule per asymmetric unit, and diffract to 1.95 Å resolution. The ASGR-1 CBD/5E5 Fab complex structure was solved by molecular replacement with the program Molrep². The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=25.9/R_free=30.5. While the electron density for the ASGR-1 CBD and 5E5 Fab variable domain (along with the corresponding interface) is quite good, the electron density for the 5E5 constant domain is poor (most likely due to poor packing within the crystal lattice). This likely explains the higher R/R_free observed from this structure refinement.

Core interaction interface amino acids were determined as being all amino acid residues with at least one non-hydrogen atom less than or equal to 5 Å from the partner protein. 5 Å was chosen as the core region cutoff distance to allow for atoms within a van der Waals radius plus a possible water-mediated hydrogen bond. Boundary interaction interface amino acids were determined as all amino acid residues with at least one non-hydrogen atom less than or equal to 8 Å from the partner protein but not included in the core interaction list. Less than or equal to 8 Å was chosen as the boundary region cutoff distance to allow for the length of an extended arginine amino acid. Amino acids that met these distance criteria were calculated with the program PyMOL⁵.

REFERENCES

• 1. Battye, T. G., Kontogiannis, L., Johnson, O., Powell, H. R. & Leslie, A. G. iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta Crystallogr D Biol Crystallogr 67, 271-81 (2011).
• 2. CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-3 (1994).
• 3. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66, 486-501 (2010).
• 4. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213-21 (2010).
• 5. DeLano, W. L. The PyMOL Molecular Graphics System. (Palo Alto, 2002).

C. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 22G5

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 22G5, determined to 2.1 Å resolution (the conditions of which are described above in B). This structure, depicted in FIGS. 23A&B, shows that when 22G5 binds to/interacts with ASGR-1, a conformational rearrangement of the carbohydrate binding loop occurs, impairing the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). This demonstrates that the 22G5 Fab indirectly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 22G5 with ASGR-1. This was defined as residues that are within 5 Å of the 22G5 protein. The core residues are as follows: W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, Q270, P272, W275 (SEQ ID N0:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 22G5. These residues were ASGR-1 residues that were from 5-8 Å of the 22G5 protein. The boundary residues are as follows: P155, N157, W158, F168, S169, R170, W175, A178, D179, C182, A187, W211, C269, R271, Y273, R274, C277, T279 (SEQ ID N0:5).

Specific core 22G5 amino acid residues of the interaction interface with ASGR-1 were defined as 22G5 residues that are within 5 Å of the ASGR-1 protein. The core 22G5 Heavy Chain residues include: A33, V50, I51, S52, R53, S54, G55, G56, Y57, Y59, R99, A101, A103, G104, E106; and the core 22G5 Light Chain residues include: 22G5 Light Chain: Y32, S91, Y92, R93, Thr94, Pro95, F97.

Boundary 22G5 amino acid residues of the interaction interface with ASGR-1 were defined as 22G5 residues that are 5-8 Å from the ASGR-1 protein. The boundary 22G5 Heavy Chain residues include: S30, S31, Y32, M34, N35, W47, S49, T58, R72, N74, L100, V102, S105; and the boundary 22G5 Light Chain residues include: I2, Q27, N28, NAG100, I29, S30, S31, Q90, L96.

Methods:

The same methods were followed as described above in Example 10B except for the following changes:

The 22G5 Fab fragment was generated by cleaving the 22G5-IgG4 mAb with papain;

The ASGR-1 CBD/22G5 Fab complex was concentrated to 8 mg/ml and crystallized in 0.1 Bis-Tris pH 6.5, 0.2 sodium malonate, 20% PEG 3350;

The dataset was processed with XDS/Aimless;

ASGR-1 CBD/22G5 Fab complex crystals grow in the P212121 space group with unit cell dimensions a=46.04, b=80.34, c=169.14 Å with one complex molecule per asymmetric unit, and diffract to 2.1 Å resolution; and

The structure was improved with multiple rounds of model building with Coot3 and refinement with Phenix4, to a final R=17.8/Rfree=22.5.

D. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 4A2

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 4A2, determined to 2.15 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 24, 25 and 26, shows that when 4A2 binds to/interacts with ASGR-1, a conformational rearrangement of the carbohydrate binding loop occurs, impairing the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). This demonstrates that the 4A2 Fab indirectly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 4A2 with ASGR-1. This was defined as residues that are within 5 Å of the 4A2 protein. The core residues are as follows: R170, W195, E196, K199, Q202, H203, H204, I205, G206, P207, V208, F233, K234, N235, W236, P238, D260, D261, G262, R263, R274 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 4A2. These residues were ASGR-1 residues that were from 5-8 Å of the 4A2 protein. The boundary residues are as follows: N157, V159, F168, S169, S171, S194, Q198, F200, V201, T210, R237, E239, Q240, F258, T259, W264 (SEQ ID NO:5).

Specific core 4A2 amino acid residues of the interaction interface with ASGR-1 were defined as 4A2 residues that are within 5 Å of the ASGR-1 protein. The core 4A2 Heavy Chain residues include: T28, F29, T30, N31, Y32, D33, W50, H52, S55, N57, S99, S100, G101, W102, Y103; and the core 4A2 Light Chain residues include: 4A2 Light Chain: H31, S33, N34, N36, Y38, W56, Y97, Y98.

Boundary 4A2 amino acid residues of the interaction interface with ASGR-1 were defined as 4A2 residues that are 5-8 Å from the ASGR-1 protein. The boundary 4A2 Heavy Chain residues include: Y27, 134, N35, W47, M51, P53, N54, G56, T58, G59, Y104, D106; and the boundary 4A2 Light Chain residues include: 129, S32, N35, N37, Y55, T59, Q96, N99, T100.

The coordinates for the ASGR-1 CBD/4A2 crystal structure complex are presented in Table 10.2.

Methods:

The same methods were followed as described above in part B of this Example except for the following changes:

1. For this antibody only, a double stop codon was inserted at the end of CH1 domain that allowed for expression of a 4A2 Fab. The Fab purification was carried out via an affinity and a cation exchanger column. The final sequence of 4A2 Fab is:

Heavy Chain (SEQ ID NO: 32650):
QVQLVQSGTEVKKPGASVKVSCKASGYTFTNYDINWVRQATGQGLEWMGW
MHPNSGNTGYAQKFQGRVTLTRDTSISTAYMELSSLRSEDTAVYYCASSS
GWYYFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDY
FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYI
CNVNHKPSNTKVDKKVEPKSCGSDEVDGGD
Light Chain (SEQ ID NO: 32651):
DIVMTQSPDSLAVSLGERATINCKSSQSILHSSNNNNYLAWFQQKPGQPP
KLLLYWASTRESGVPDRFSGSGSGTDFTLTISSLQPEDVAVYYCQQYYNT
PVTFGPGTKVGIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREA
KVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYAC
EVTHQGLSSPVTKSFNRGEC

1. The ASGR-1 CBD/4A2 Fab complex was concentrated to 20 mg/ml and crystallized in 0.2 M Tri-Lithium citrate and 20% PEG3350;

2. The ASGR-1 CBD/4A2 Fab complex crystals grow in the P2₁2₁2₁ space group with unit cell dimensions a=63.42, b=76.37, c=156.67 Å with one complex molecule per asymmetric unit, and diffract to 2.15 Å resolution; and

3. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=17.9/R_free=21.8.

Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 7E11

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 7E11, determined to 2.0 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 27 and 28, shows that when 7E11 binds to/interacts with ASGR-1, a conformational rearrangement of the carbohydrate binding loop occurs, impairing the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). This demonstrates that the 7E11 Fab indirectly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 7E11 with ASGR-1. This was defined as residues that are within 5 Å of the 7E11 protein. The core residues are as follows: H161, S194, W195, E196, Q198, K199, F200, Q202, H203, F233, K234, N235, W236, R237, P238, R263 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 7E11. These residues were ASGR-1 residues that were from 5-8 Å of the 7E11 protein. The boundary residues are as follows: E160, E162, V192, T193, E197, V201, H204, Y229, E230, T231, G232, E239, Q240, P241, D261, G262, W264 (SEQ ID NO:5).

Specific core 7E11 amino acid residues of the interaction interface with ASGR-1 were defined as 7E11 residues that are within 5 Å of the ASGR-1 protein. The core 7E11 Heavy Chain residues include: S30, S31, I50, W52, H53, S56, N57, Y59, S01, M102, G103; and the core 7E11 Light Chain residues include: 130, Y32, T91, Y92, S93, T94, 196.

Boundary 7E11 amino acid residues of the interaction interface with ASGR-1 were defined as 7E11 residues that are 5-8 Å from the ASGR-1 protein. The boundary 7E11 Heavy Chain residues include: T28, F29, F32, G33, H35, W47, I51, D54, K58, D99, L100, G104; and the boundary 7E11 Light Chain residues include: I2, Q27, N28, I29, S31, L33, N34, T50, S67, Q89, Q90, P95.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

The 7E11 Fab fragment was generated by cleaving the 7E11 mAb with caspase 3:

7E11 mAb Heavy Chain (SEQ ID NO: 32652):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSFGMHWVRQAPGKGLEW
VAIIWHDGSNKYYADSVKGRFTISRDNSNNTLYLQMSSLRAEDTAVYY
CARDLSMGGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAAL
GCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPS
SSLGTQTYICNVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCP
APELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY
VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNK
ALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYP
SDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNV
FSCS VMHEALHNHYTQKSLSLSPGHHHHHH
7E11 mAb Light Chain (SEQ ID NO: 32653):
DIQMTQSPSSLSASVGDRVTIACRASQNIISYLNWYQQKPGKAPKFLI
YTASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQTYSTPL
TFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREA
KVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVY
ACEVTHQGLSSPVTKSFNRGEC
7E11 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32654):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSFGMHWVRQAPGKGLEWVAI
IWHDGSNKYYADSVKGRFTISRDNSNNTLYLQMSSLRAEDTAVYYCARDL
SMGGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDY
FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYI
CNVNHKPSNTKVDKKVEPKSCGSDEVD
7E11 Fab Light Chain (Post-Cleavage) (SEQ ID NO:
32655):
DIQMTQSPSSLSASVGDRVTIACRASQNIISYLNWYQQKPGKAPKFLIYT
ASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQTYSTPLTFGG
GTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV
DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG
LSSPVTKSFNRGEC

• • 1. The ASGR-1 CBD/7E11 Fab complex was concentrated to 20 mg/ml and crystallized in 0.2 M Potassium Phosphate monobasic and 20% PEG3350;
  • 2. The ASGR-1 CBD/7E11 Fab complex crystals grow in the P6222 space group with unit cell dimensions a=105.75, b=105.75, c=193.75 Å and γ=120.0° with one complex molecule per asymmetric unit, and diffract to 2.0 Å resolution;
  • 3. The dataset was processed with XDS/CCP4;
  • 4. The ASGR-1 CBD/7E11 Fab complex structure was solved by molecular replacement with the program Phaser; and
  • 5. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=21.4/R_free=26.9.

E. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 4H6

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 4H6, determined to 2.6 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 29 and 30, shows that when 4H6 binds to/interacts with ASGR-1, a conformational rearrangement of the carbohydrate binding loop occurs, impairing the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). This demonstrates that the 4H6 Fab indirectly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 4H6 with ASGR-1. This was defined as residues that are within 5 Å of the 4H6 protein. The core residues are as follows: H161, E162, T193, S194, W195, E196, K199, Q202, T231, G232, F233, K234, N235, P238, D261, R263 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 4H6. These residues were ASGR-1 residues that were from 5-8 Å of the 4H6 protein. The boundary residues are as follows: R163, V192, E197, Q198, H203, P207, D228, E230, W236, R237, D260, G262, W264 (SEQ ID NO:5).

Specific core 4H6 amino acid residues of the interaction interface with ASGR-1 were defined as 4H6 residues that are within 5 Å of the ASGR-1 protein. The core 4H6 Heavy Chain residues include: Y33, H35, W50, H52, S55, G57, T58, N59, D99, G100, T101, S102; and the core 4H6 Light Chain residues include: Q27, W32, A91, N92, S93, F94, F96.

Boundary 4H6 amino acid residues of the interaction interface with ASGR-1 were defined as 4H6 residues that are 5-8 Å from the ASGR-1 protein. The boundary 4H6 Heavy Chain residues include: D31, Y32, L34, W47, I51, N54, G56, Y60, Q65, S103, F104; and the boundary 4H6 Light Chain residues include: D1, I2, G28, I29, S30, R31, Y49, G50, Q89, Q90, P95.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. The 4H6 Fab fragment was generated by cleaving the 4H6 mAb with caspase 3.

4H6 mAb Heavy Chain (SEQ ID NO: 32656):
QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYLHWVRQAPGQGLEWMGW
IHPNSGGTNYAQKFQGRVTMTRDTSISTAYMGLSSLRSDDTAVYYCARDG
TSSFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF
PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC
NVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPAPELLGGPSVFL
FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR
EEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQ
PREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK
TTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLS
LSPGHHHHHH
4H6 mAb Light Chain (SEQ ID NO: 32657):
DIQMTQSPSSVSASVGDRVTITCRASQGISRWLAWYQQKPGKAPKLLIYG
ASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQANSFPFTFGP
GTKVDIKGTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV
DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG
LSSPVTKSFNRGEC
4H6 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32658):
QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYLHWVRQAPGQGLEWMGW
IHPNSGGTNYAQKFQGRVTMTRDTSISTAYMGLSSLRSDDTAVYYCARDG
TSSFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF
PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC
NVNHKPSNTKVDKKVEPKSCGSDEVD
4H6 Fab Light Chain (Post-Cleavage) (SEQ ID NO:
32659):
DIQMTQSPSSVSASVGDRVTITCRASQGISRWLAWYQQKPGKAPKLLIYG
ASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQANSFPFTFGP
GTKVDIKGTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV
DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG
LSSPVTKSFNRGEC

2. The ASGR-1 CBD/4H6 Fab complex was concentrated to 20 mg/ml and crystallized in 0.2M Sodium fluoride, 0.1 M Bis Tris propane pH8.5, 20% PEG3350;

3. The dataset was collected on beamline ID22 at the APS synchrotron and processed with HKL2000/CCP4;

4. The ASGR-1 CBD/4H6 Fab complex crystals grow in the P12₁1 space group with unit cell dimensions a=57.20, b=43.58, c=131.65 Å and β=90.7° with one complex molecule per asymmetric unit, and diffract to 2.6 Å resolution;

5. The ASGR-1 CBD/4H6 Fab complex structure was solved by molecular replacement with the program Phaser; and

6. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=17.9/R_free=22.5.

F. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 72G9

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 72G9, determined to 2.55 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 31 and 32A and 32B, shows that when 72G9 binds to/interacts with ASGR-1, the CDR H2 loop of the Fab fragment appears to directly block the ligand (i.e., carbohydrate) binding/interacting to ASGR-1 CBD. This demonstrates that the 72G9 Fab directly inhibits the ASGR-1 CBD/Ligand binding.

The deicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 72G9 with ASGR-1. This was defined as residues that are within 5 Å of the 72G9 protein. The core residues are as follows: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270 ((SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 72G9. These residues were ASGR-1 residues that were from 5-8 Å of the 72G9 protein. The boundary residues are as follows: H215, K222, T231, G232, R237, P238, H247, G248, E253, C255, D266, V268, C269 (SEQ ID NO:5).

Specific core 72G9 amino acid residues of the interaction interface with ASGR-1 were defined as 72G9 residues that are within 5 Å of the ASGR-1 protein. The core 72G9 Heavy Chain residues include: G26, F27, T28, S30, S31, Y32, S33, S52, G53, S54, S56, Y57, Y59, R98, G100, S101, R102; and the core 72G9 Light Chain residues include: Y32, Y49, T50, Q55, S91, H92, S93, F94, F96.

Boundary 72G9 amino acid residues of the interaction interface with ASGR-1 were defined as 72G9 residues that are 5-8 Å from the ASGR-1 protein. The boundary 72G9 Heavy Chain residues include: V2, F29, N35, S50, T51, S55, I58, R72, G99, G103, F104, D105; and the boundary 72G9 Light Chain residues include: S28, I29, T30, N33, L46, S53, L54, S56, Q89, Q90, P95.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. The 72G9 Fab fragment was generated by cleaving the 72G9 mAb with caspase 3.

72G9 mAb Heavy Chain (SEQ ID NO: 32660):
EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
ISGSSSYIYYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYFCARGG
SRGFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF
PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC
NVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPAPELLGGPSVFL
FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR
EEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQ
PREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK
TTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLS
LSPGHHHHHH
72G9 mAb Light Chain (SEQ ID NO: 32661):
DIQMTQSPSSLSASVGDRVTITCRASQSITSYLNWYQQKPGKAPKLLIYT
ASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSHSFPFTFGP
GTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV
DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG
LSSPVTKSFNRGEC
72G9 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32662):
EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
ISGSSSYIYYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYFCARGG
SRGFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF
PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC
NVNHKPSNTKVDKKVEPKSCGS DEVD
72G9 Fab Light Chain (Post-Cleavage) (SEQ ID NO:
32663):
DIQMTQSPSSLSASVGDRVTITCRASQSITSYLNWYQQKPGKAPKLLIYT
ASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSHSFPFTFGP
GTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV
DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG
LSSPVTKSFNRGEC

2. The 72G9 Fab/ASGR-1 CBD complex was concentrated to 0.2 M Magnesium Sulfate heptahydrate, 20% PEG3350;

3. The ASGR-1 CBD/72G9 Fab complex crystals grew in the P2₁ space group with unit cell dimensions a=100.98, b=64.95, c=100.68 Å and β=96.43° with one complex molecule per asymmetric unit, and diffract to 2.55 Å resolution;

4. The dataset was processed with XDS/CCP4;

5. The ASGR-1 CBD/72G9 Fab complex structure was solved by molecular replacement with the program Phaser; and

6. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=20.4/R_free=23.4.

G. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 194A4

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 194A4, determined to 2.6 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 33 and 34, shows that when 194A4 binds to/interacts with ASGR-1, a conformational rearrangement of the carbohydrate binding loop occurs, impairing the carbohydrate binding loop from binding to/interacting with ligand (i.e., carbohydrates). This demonstrates that the 194A4 Fab indirectly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 194A4 with ASGR-1. This was defined as residues that are within 5 Å of the 194A4 protein. The core residues are as follows: T193, S194, W195, E196, P220, W221, G226, T227, D228, Y229, E230, T231, G232, F233, K234, N235, W236, R237, P238, E239, G252 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 194A4. These residues were ASGR-1 residues that were from 5-8 Å of the 194A4 protein. The boundary residues are as follows: H161, E162, V191, V192, E197, Q198, D216, G219, K222, W223, D225, R263, W264 (SEQ ID NO:5).

Specific core 194A4 amino acid residues of the interaction interface with ASGR-1 were defined as 194A4 residues that are within 5 Å of the ASGR-1 protein. The core 194A4 Heavy Chain residues include: V31, Y32, Y33, W50, N52, S55, G57, R98, G99, Y100, D101, I102, T204; and the core 194A4 Light Chain residues include: V29, S30, I32, Y33, L47, Y50, R55, A56, T57, Y94.

Boundary 194A4 amino acid residues of the interaction interface with ASGR-1 were defined as 194A4 residues that are 5-8 Å from the ASGR-1 protein. The boundary 194A4 Heavy Chain residues include: V2, Y27, T30, L34, N35, P53, N54, G56, T58, N59, A97, L103, G105; and the boundary 194A4 Light Chain residues include: G28, N31, L48, I49, G51, N54, G58, I59, S68, G69, D93, S95.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. The 194A4 Fab fragment was generated by cleaving the 194A4 mAb with caspase 3.

194A4 mAb Heavy Chain (SEQ ID NO: 32664):
QVQLVQSGTEVKKPGASLKVSCKASGYTFTVYYLNWVRQAPGQGLEWMGW
INPNSGGTNYAQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARGY
DILTGWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFP
EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICN
VNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPAPELLGGPSVFLF
PPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPRE
EQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQP
REPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKT
TPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSL
SPGHHHHHH
194A4 mAb Light Chain (SEQ ID NO: 32665):
EIVLTQSPGTLSLSPGERATLSCRASRGVSNIYLAWYQQKPGQAPRLLIY
GASNRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQHNDYSMFTFG
PGTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWK
VDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQ
GLSSPVTKSFNRGEC
194A4 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32666):
QVQLVQSGTEVKKPGASLKVSCKASGYTFTVYYLNWVRQAPGQGLEWMGW
INPNSGGTNYAQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARGY
DILTGWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFP
EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICN
VNHKPSNTKVDKKVEPKSCGSDEVD
194A4 Fab Light Chain (Post-Cleavage) (SEQ ID NO:
32667):
EIVLTQSPGTLSLSPGERATLSCRASRGVSNIYLAWYQQKPGQAPRLLIY
GASNRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQHNDYSMFTFG
PGTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWK
VDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQ
GLSSPVTKSFNRGEC

2. The 194A4 Fab/ASGR-1 CBD complex was concentrated to 13.1 mg/mL and crystallized with 0.2 M Sodium chloride, 0.1M MES pH6.0, 20% PEG2000 MME;

3. The dataset was processed with XDS/CCP4;

4. The 194A4 Fab/ASGR-1 CBD complex crystals grow in the P2₁2₁2₁ space group with unit cell dimensions a=52.23, b=66.40, c=177.75 Å with one complex molecule per asymmetric unit, and diffract to 2.6 Å resolution;

5. The ASGR-1 CBD/194A4 Fab complex structure was solved by molecular replacement with the program Phaser; and

6. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=20.1/R_free=24.6.

H. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 54E9

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 54E9, determined to 2.6 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIG. 35 and FIG. 36A and FIG. 36B, shows that when 54E9 binds to/interacts with ASGR-1, the CDR H3 loop of the Fab fragment appears to directly block the ligand (i.e., carbohydrate) from binding/interacting to ASGR-1 CBD. This demonstrates that the 54E9 Fab directly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 54E9 with ASGR-1. This was defined as residues that are within 5 Å of the 54E9 protein. The core residues are as follows: W195, N209, N235, R237, P238, E239, Q240, D242, H257, T259, D260, D261, R263, N265, D267, R271, Y273 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 54E9. These residues were ASGR-1 residues that were from 5-8 Å of the 54E9 protein. The boundary residues are as follows: Q198, Q202, P207, V208, F233, W236, D243, E253, F258, G262, W264, D266 (SEQ ID NO:5).

Specific core 54E9 amino acid residues of the interaction interface with ASGR-1 were defined as 54E9 residues that are within 5 Å of the ASGR-1 protein. The core 54E9 Heavy Chain residues include: N30, S31, Y32, S52, Y54, N55, K59, R98, D100, F101, W102, S103, G104, Y105, K107, D110; and the core 54E9 Light Chain residues include: none.

Boundary 54E9 amino acid residues of the interaction interface with ASGR-1 were defined as 54E9 residues that are 5-8 Å from the ASGR-1 protein. The boundary 54E9 Heavy Chain residues include: V2, Y27, T28, F29, G33, W50, A53, G56, N57, H99, Y106, G108; and the boundary 54E9 Light Chain residues include: N31, Y50, V51, Q54.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. The 54E9 Fab fragment was generated by cleaving the 54E9 mAb with caspase 3.

54E9 mAb Heavy Chain (SEQ ID NO: 32668):
QVQLVQSGAEVKKPGASVKVSCKASGYTFNSYGISWVRLAPGQGLEWMGW
ISAYNGNTKNAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARHD
FWSGYYKGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCL
VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGT
QTYICNVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPAPELLGG
PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNA
KTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTIS
KAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQP
ENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
QKSLSLSPGHHHHHH
54E9 mAb Light Chain (SEQ ID NO: 32669):
QSVLTQPPSASGTPGQRVTISCSGSNSNIGNNIVTWYQQLPGTAPKLLIY
VNDQRPSGVPDRFSGSKSGTSASLAISGLQSEDEADYYCAAWDDSLNGWV
FGGGTTLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTV
AWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVT
HEGSTVEKTVAPTECS
54E9 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32670):
QVQLVQSGAEVKKPGASVKVSCKASGYTFNSYGISWVRLAPGQGLEWMGW
ISAYNGNTKNAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARHD
FWSGYYKGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCL
VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGT
QTYICNVNHKPSNTKVDKKVEP
KSCGSDEVD
54E9 Fab Light Chain (Post-Cleavage) (SEQ ID NO:
32671):
QSVLTQPPSASGTPGQRVTISCSGSNSNIGNNIVTWYQQLPGTAPKLLIY
VNDQRPSGVPDRFSGSKSGTSASLAISGLQSEDEADYYCAAWDDSLNGWV
FGGGTTLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTV
AWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVT
HEGSTVEKTVAPTECS

1. The 54E9 Fab/ASGR-1 CBD complex was concentrated to 14.8 mg/mL and crystallized with 0.2 M Magnesium Chloride hexahydrate, 20% PEG3350;

2. The dataset was processed with XDS/CCP4;

3. The 54E9 Fab/ASGR-1 CBD complex crystals grow in the 12 space group with unit cell dimensions a=64.66, b=41.65, c=224.59 Å and β=97.60° with one complex molecule per asymmetric unit, and diffract to 2.6 Å resolution;

4. The 54E9 Fab/ASGR-1 CBD complex structure was solved by molecular replacement with the program Phaser; and

5. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R=19.1/R_free=25.9

I. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 218G4

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 218G4, determined to 2.4 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 37 and 38, shows that when 218G4 binds to/interacts with ASGR-1, it impairs its ability to bind to ligand (e.g., carbohydrate). This demonstrates that the 218G4 Fab directly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 218G4 with ASGR-1. This was defined as residues that are within 5 Å of the 218G4 protein. The core residues are as follows: R170, S171, G172, A174, H204, I205, G206, P207, V208, N209, H257, D260, N265, D267, Q270, R271, P272, Y273, R274 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 218G4. These residues were ASGR-1 residues that were from 5-8 Å of the 218G4 protein. The boundary residues are as follows: W167, F168, S169, K173, W175, D177, Y181, Q202, H203, T210, W211, R237, F258, T259, D261, D266, V268, C269, W275 (SEQ ID NO:5).

Specific core 218G4 amino acid residues of the interaction interface with ASGR-1 were defined as 218G4 residues that are within 5 Å of the ASGR-1 protein. The core 218G4 Heavy Chain residues include: Q1, V2, F27, S30, S31, Y32, Y53, D54, W99, Y100, Y101, Y102; and the core 218G4 Light Chain residues include: Y33, Y50, D51, N53, K54, S57.

Boundary 218G4 amino acid residues of the interaction interface with ASGR-1 were defined as 218G4 residues that are 5-8 Å from the ASGR-1 protein. The boundary 218G4 Heavy Chain residues include: G26, T28, F29, G33, W52, G55, R72, N74, N98, Y103, Y104, D107, V108; and the boundary 218G4 Light Chain residues include: V34, S52, R55, P56, G58, G65.

The coordinates for the ASGR-1 CBD/GalNAc crystal structure complex are presented in Table 10.3.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. The 218G4 Fab fragment was generated by cleaving the 218G4 mAb with caspase 3.

218G4 mAb Heavy Chain (SEQ ID NO: 32672):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGLHWVRQAPGKGLEWVAV
IWYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRVEDTAVYYCANWY
YYYYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKD
YFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTY
ICNVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPAPELLGGPSV
FLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTK
PREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAK
GQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN
YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKS
LSLSPGHHHHHH
218G4 mAb Light Chain (SEQ ID NO: 32673):
QSVLTQPPSVSAAPGQKVTISCSGSSSNIGNNYVSWYQQLPGTAPKLLLY
DSNKRPSGIPARFSGSKSGTSATLGITGLQTGDEADYYCGTWDSSLNTVV
FGGGTKLTVLSQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTV
AWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVT
HEGSTVEKTVAPTECS
218G4 Fab Heavy Chain (Post-Cleavage)(SEQ ID NO:
32674):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGLHWVRQAPGKGLEWVAV
IWYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRVEDTAVYYCANWY
YYYYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKD
YFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTY
ICNVNHKPSNTKVDKKVEPKSCGSDEVD
218G4 Fab Light Chain (Post-Cleavage):
Same sequence as 218G4 mAb Light chain

1. The 218G4 Fab/ASGR-1 CBD complex was concentrated to 16.4 mg/mL and crystallized with 0.1M Tris pH8 and 1.6M Lithium Sulfate;

2. The dataset was collected from a single crystal on beamline ID22 at the Argonne National Laboratory and processed with XDS/CCP4;

3. The 218G4 Fab/ASGR-1 CBD complex crystals grow in the C222 space group with unit cell dimensions a=137.24, b=245.26, c=118.91 Å with two complex molecules per asymmetric unit and diffract to 2.6 Å resolution;

4. The 218G4 Fab/ASGR-1 CBD complex structure was solved by molecular replacement with the program Phaser; and

5. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R_factor=18.4/R_free=21.6

J. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 176H4

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 176H5, determined to 2.3 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 39 and 40, show that when 176H4 binds to/interacts with ASGR-1, it appears to block ligand (e.g., carbohydrate) binding by ASGR-1 CBD, with the paratope of the 176H4 antibody located directly on top of the carbohydrate binding pocket. This demonstrates that the 174H4 Fab directly inhibits the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 176H4 with ASGR-1. This was defined as residues that are within 5 Å of the 176H4 protein. The core residues are as follows: R170, S171, G172, K173, A174, D177, P207, V208, N209, R237, Q240, W244, G246, H247, G248, L249, E253, H257, T259, D260, N265, D267, Q270, R271, P272, Y273, R274 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 176H4. These residues were ASGR-1 residues that were from 5-8 Å of the 176H4 protein. The boundary residues are as follows: S169, W175, A176, A178, T210, W211, W236, P238, E239, D242, Y245, G250, G251, F258, D261, G262, R263, W264, D266, V268, C269, W275 (SEQ ID NO:5).

Specific core 176H4 amino acid residues of the interaction interface with ASGR-1 were defined as 176H4 residues that are within 5 Å of the ASGR-1 protein. The core 176H4 Heavy Chain residues include: S31, W52, Y53, D54, Y57, Y59, D102, F103, W104; and the core 176H4 Light Chain residues include: H31, G32, D33, G34, K35, Y37, 197, Q98, 199.

Boundary 176H4 amino acid residues of the interaction interface with ASGR-1 were defined as 176H4 residues that are 5-8 Å from the ASGR-1 protein. The boundary 176H4 Heavy Chain residues include: T28, S30, Y32, G33, W47, I50, I51, S56, K58, Y60, K65, D99, H101, S105, G106; and the boundary 176H4 Light Chain residues include: I2, Q27, S28, L29, L30, T36, E55, Q95, S96, P100, W101.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. The 176H4 Fab fragment was generated by cleaving the 176H4 mAb with caspase 3.

176H4 mAb Heavy Chain (SEQ ID NO: 32675):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAI
IWYDGSYKYYADSVKGRFTISRDNSKNTLYLQMSSLRAEDTAVYYCARDA
HDFWSGYFAYWGQGALVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLV
KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQ
TYICNVNHKPSNTKVDKKVEPKSCGSDEVDGGDKTHTCPPCPAPELLGGP
SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAK
TKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISK
AKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPE
NNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQ
KSLSLSPGHHHHHH
176H4 mAb Light Chain (SEQ ID NO: 32676):
DIVMTQTPLSLSVTPGQPASISCKSSQSLLHGDGKTYLYWYLQKPGQPPQ
LLIYEVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDVGIYYCMQSIQIP
WTFGQGTRVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK
VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACE
VTHQGLSSPVTKSFNRGEC
176H4 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32677):
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAI
IWYDGSYKYYADSVKGRFTISRDNSKNTLYLQMSSLRAEDTAVYYCARDA
HDFWSGYFAYWGQGALVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLV
KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQ
TYICNVNHKPSNTKVDKKVEPKSCGSDEVD
176H4 Fab Light Chain (Post-Cleavage):
Same sequence as 176H4 mAb Light chain

1. The 176H4 Fab/ASGR-1 CBD complex was concentrated to 14.9 mg/mL and crystallized 1 with 0.2 M Sodium Nitrate, 20% PEG3350;

2. The dataset was collected from a single crystal on beamline ID22 at the Argonne National Laboratory and processed with XDS/CCP4;

3. The 176H4 Fab/ASGR-1 CBD complex crystals grow in the I121 space group with unit cell dimensions a=68.31, b=126.31, c=134.13 Å and β=101.6° with two complex molecules per asymmetric unit, and diffract to 2.3 Å resolution;

4. The 176H4 Fab/ASGR-1 CBD complex structure was solved by molecular replacement with the program Phaser; and

5. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R_factor=17.9/R_free=23.3

K. Crystal Structure of ASGR-1 Carbohydrate Binding Domain (CBD) with 194C10

The present example presents the crystal structure of the ASGR-1 CBD bound to the Fab fragment of 194C10, determined to 2.6 Å resolution (the conditions of which are described above in section B of this Example). This structure, depicted in FIGS. 41 and 42, shows that when 194C10 binds to/interacts with ASGR-1, it likely induces a conformational rearrangement of the carbohydrate binding loop, impairing ASGR-1 CBD from binding to ligand (e.g., carbohydrate), as well as possibly blocking the ligand (e.g., carbohydrate) binding by ASGR-1 CBD, with the paratope of the 194C10 Fab. These data indicate that the 174H4 Fab may directly and/or indirectly inhibit the ASGR-1 CBD/Ligand binding.

The depicted structure also allows one to identify specific core ASGR amino acid residues for the interaction interface of 194C10 with ASGR-1. This was defined as residues that are within 5 Å of the 194C10 protein. The core residues are as follows: N157, R170, S171, G172, Q202, H203, H204, I205, G206, P207, V208, N209, T210, D260, R271, P272, Y273, R274 (SEQ ID NO:5).

The structures were also used to identify boundary ASGR-1 amino acid residues for the interaction interface with 194C10. These residues were ASGR-1 residues that were from 5-8 Å of the 194C10 protein. The boundary residues are as follows: V156, W158, V159, H161, W167, F168, S169, K173, K199, F200, V201, W211, R237, H257, F258, T259, D261, D267, V268, Q270, W275 (SEQ ID NO:5).

Specific core 194C10 amino acid residues of the interaction interface with ASGR-1 were defined as 194C10 residues that are within 5 Å of the ASGR-1 protein. The core 194C10 Heavy Chain residues include: R30, Y31, Y33, E50, S54, S56, N58, D98, Y99, G100; and the core 194C10 Light Chain residues include: N30, S31, Y33, F50, S54, S68, Y92, E93, W97.

Boundary 194C10 amino acid residues of the interaction interface with ASGR-1 were defined as 194C10 residues that are 5-8 Å from the ASGR-1 protein. The boundary 194C10 Heavy Chain residues include: S28, Y32, W34, S35, W47, G49, I51, S52, H53, G55, T57, R97, A101, F102, D103; and the boundary 194C10 Light Chain residues include: S28, V29, G32, L47, G51, A52, S53, R55, A56, G69, Q90, Q91, S94, S95.

The coordinates for the ASGR-1 CBD/GalNAc crystal structure complex are presented in Table 10.4.

Methods:

The same methods were followed as described above in part B of this example except for the following changes:

1. 194C10 Fab fragment was generated by cleaving the 194C10 mAb with caspase 3.

194C10 mAb Heavy Chain (SEQ ID NO: 32678):
QVQLQQWGAGLLKPSETLSLTCAVSGGSFRYYYWSWIRQPPGKGLEWFGE
INHAGSTNYNPSLKSRVTISIDTSKNQFSLKLRSVTAADTAVYYCARDYG
AFDIWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPE
PVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNV
NHKPSNTKVDKKVEPKSCG
194C10 mAb Light Chain (SEQ ID NO: 32679):
EIVLTQSPGTLSLSPGERATLSCRASPSVNSGYLAWYQQKPGQTPRLLIF
GASSRATGIPDRFSASGSGADFTLTISRLEPEDFAVYFCQQYESSPWTFG
QGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWK
VDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQ
GLSSPVTKSFNRGEC*
194C10 Fab Heavy Chain (Post-Cleavage) (SEQ ID NO:
32680):
QVQLQQWGAGLLKPSETLSLTCAVSGGSFRYYYWSWIRQPPGKGLEWFGE
INHAGSTNYNPSLKSRVTISIDTSKNQFSLKLRSVTAADTAVYYCARDYG
AFDIWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPE
PVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNV
NHKPSNTKVDKKVEPKSCGSDEVD
194C10 Fab Light Chain (Post-Cleavage):

Same sequence as 194C10 mAb Light chain

1. The 194C10 Fab/ASGR-1 CBD complex was concentrated to 13.6 mg/mL and crystallized with 0.2 M Ammonium Sulfate, 0.1 M Tris pH7.5, 20% PEG5000MME;

2. The dataset was collected from a single crystal on beamline ID22 at the Argonne National Laboratory and processed with XDS/CCP4;

3. The 194C10 Fab/ASGR-1 CBD complex crystals grow in the P12₁1 space group with unit cell dimensions a=65.62, b=130.44, c=85.93 Å and β=111.6° with two complex molecules per asymmetric unit, and diffract to 2.6 Å resolution;

4. The 194C10 Fab/ASGR-1 CBD complex structure was solved by molecular replacement with the program Phaser; and

5. The structure was improved with multiple rounds of model building with Coot³ and refinement with Phenix⁴, to a final R_factor=17.1/R_free=22.8.

L. Interaction Between GalNAc, ASGR-1 and Certain Antibodies

The structure of the 72G9/ASGR-1 complex (Item G above) was overlaid on the ASGR-1/ligand (GalNac) structure (Item A above) and the result of this combination is depicted in FIG. 31B. The structure of the 54E9/ASGR-1 complex (Item I above) was also overlaid on the ASGR-1/ligand (GalNac) structure (Item A above) and the result of this combination is depicted in FIG. 35B. The structure of the 218G4/ASGR-1 complex (Item J above) was overlaid on the ASGR-1/ligand (GalNac) structure (Item A above) and the result of this combination is depicted in FIG. 38. The structure of the 176H4/ASGR-1 complex (Item K above) was overlaid on the ASGR-1/ligand (GalNac) structure (Item A above) and the result of this combination is depicted in FIG. 40. These figures demonstrate areas on ASGR-1 which can be usefully targeted to inhibit ASGR-1 interaction with a ligand, e.g., GalNac. These figures show that 72G9, 54E9, 218G4 and 176H4 directly interact with a subset of amino acid residues that are specifically involved in binding to the ligand (e.g., GalNAc).

As noted above, analysis of the crystal structures identified specific amino acids involved in the interaction between ASGR-1 and the partner proteins (the core and boundary regions of the interface on the ASGR-1 surface) and the spatial requirements of these partner proteins to interact with ASGR-1. The structures suggest ways to inhibit the interaction between ASGR-1 and a ligand, GalNAc. First, as noted above, binding an agent to ASGR-1 where it shares residues in common with the binding site of a ligand such as GalNAc would inhibit the interaction between ASGR-1 and the ligand. Second, an agent that binds outside of the residues in common can sterically interfere with the ligand that are either N- or C-terminal to the ligand to prevent the interaction between ASGR-1 and a ligand.

In some embodiments, the residues that are involved in both ligand binding and are close to the areas where the above noted antigen binding proteins bind are especially useful for manipulating ASGR-1 binding to ligand. For example, amino acid residues from interfaces in common in both the core region and boundary region for the different binding partners are listed in Table 10.5 below.

TABLE 10.5
Parameters                      Amino acid position(s)
72G9/GalNAc both under 5 Å      Q240, D242, W244
72G9 under 5 Å/GalNAc 5-8 Å     E239, P241, D243, Y245, G246,
                                G252
72G9 at 5-8 Å/GalNAc under 5 Å  R237, E253
72G9/GalNAc both at 5-8 Å       P238, H247, C255, V268
54E9/GalNAc both under 5 Å      N209, R237, Q240, D242, H257,
                                T259, N265, D267, Y273
54E9 under 5 Å/GalNAc 5-8 Å     P238, E239, D260, R263, R271
54E9 at 5-8 Å/GalNAc under 5 Å  E253, D266
54E9/GalNAc both at 5-8 Å       D243, F258, W264
218G4/GalNAc both under 5 Å     N209, H257, N265, D267, Y273
218G4 under 5 Å/GalNAc 5-8 Å    D260, R271
218G4 at 5-8 Å/GalNAc under 5 Å R237, T259, D266
218G4/GalNAc both at 5-8 Å      F258, V268
176H4/GalNAc both under 5 Å     N209, R237, Q240, W244, E253,
                                H257, T259, N265, D267, Y273
176H4 under 5 Å/GalNAc 5-8 Å    G246, H247, D260, R271
176H4 at 5-8 Å/GalNAc under 5 Å D266
176H4/GalNAc both at 5-8 Å      P238, E239, Y245, F258, R263,
                                W264, V268

As will be appreciated by one of skill in the art, in some embodiments, the antigen binding proteins bind to and/or block at least one of the above noted residues.

Antigen binding proteins and molecules that interact with the relevant areas or residues of the structure of ASGR-1 (including those areas or residues within 15, 15-8, 8, 8-5, 5, or fewer angstroms from where ligands, such as GalNAc, or the antibodies, interact with ASGR-1) depicted in the figures (e.g., FIGS. 19-42) and/or their corresponding positions on the structures from the coordinates are also contemplated.

Example 11: Determination of the Binding Affinity of ASGR-1 Specific Antibodies

To quantitate the binding affinity of specific antibodies for ASGR-1 (either purified from hybridoma supernatants or made recombinantly), association and dissociation rates can be measured using a ForteBio Octet instrument. The antibodies were covalently coupled to AR2G tips to load levels close to 2 nm and then bound to the soluble human ASGR-1 carbohydrate binding domain (CBD; amino acid residues 154-281; N-terminal 6×His tag) in a 3-fold serial dilution series starting typically at 30 nM with either 3-point or 6-point dilution series. Experimental kinetic results were globally fit to a 1:1 binding model in order to determine the association and dissociation rate constants as well as the equilibrium dissociation constant. Association and dissociation times were chosen to ensure that curvature was present during association curves and measured dissociation levels dropped at least 5% from starting levels. All Octet buffers contained 10 mM Tris (pH7.5), 150 mM NaCl, 1 mM CaCl₂, 0.10 mg/ml BSA and 0.13% Triton X-100. Octet assays were run at 27° C. Because this assay only measures binding to the ASGR-1 CBD, antibodies that recognize epitopes partially or entirely outside the CBD and/or recognize ASGR-1 in the context of a native ASGR complex, for example, as could occur on cell membranes, may not score as positive in this assay. Data provided for representative antibodies in TABLE 11.1.

	TABLE 11.1
		Octet		Octet
		binding		binding
	Ab name	KD (nM)	Ab name	KD (nM)
	4H6	4.8	194A4	0.7
	4B1	>30	194C1	1.3
	4A2	0.06	194C10	4
	5E5	7.6	197G3	0.8
	6G7	2.0	198D2	>30
	7G4	0.9	198G3	0.04
	7F4	1.2	202A3	>30
	7E11	1.6	218G4	2.6
	12D2	>30	4A2.001	0.06
	22G5	1.4	4A2.001.003	0.04
	25A4	0.03	4A2.001.004	0.03
	26C4	0.4	4A2.001.005	0.02
	29H8	1.0	4A2.001.010	0.04
	48B12	0.3	4A2.001.012	0.04
	54E9	>30	25A4.001	0.06
	56E5	0.5	25A4.001.021	0.04
	72G9	0.5	4H6.009	0.28
	75G3	1.0	7E11.001	0.71
	176H4	0.8	7E11.001.005	0.42
	184E7	0.3	7E11.001.007	0.62
	190F8	0.6	5E5.016	1.46
	191G1	2.4	5E5.019	1.80
	191G10	0.5	5E5.005	2.00
	193E7	3.5

Example 12: CHO—S:huASGR-1 Cell Binding Assay

CHO—S stable high-expressing cell line were developed for both human ASGR-1 as well as mouse ASGR-1. A typical 384 well plate multiplex flow cytometery-based cell binding method is described as followed: Parental CHO—S cells and CHO—S:huASGR-1 cells were respectively labeled using a CellTrace CFSE Cell Proliferation Kit (ThermoFisher Catalog #C34554) and CellTrace Violet Cell Proliferation Kit (ThermoFisher Catalog#C34557) CHO—S:muASGR-1 were not labeled. 20 ul of cells at 4 C were added to duplicate wells of the 384 well plate. The cells were equally mixed from all three cell lines (30K cells/well). Then 20 ul of the ASGR-1 antibodies (either purified from hybridoma supernatants or made recombinantly) were added in an 11-point dose response using a 1:2 fold serial dilution starting at 100 nM. The cells and antibodies were incubated for 30 min at 4 C and then spun down and washed twice with FACS buffer containing 1 mM CaCl2. 30 ul of anti-huIgG-APC secondary antibodies were then added at a 1:1000 dilution) for 30 min at 4 C and then washed once with the same buffer. 60 ul of PI (1:1000) was added and then the cells were read by a core flow cytometry facility. The cells were gated first for live cells, then for single cells and finally for the cell dyes to separate the mixed cells into the three different cell populations. Histograms of signal vs count representing the binding profile of each antibody at each antibody concentration were automatically analyzed for the median of the binding signal and then a binding graph was made with log 10 antibody concentration in nM on the X axis with standard deviation of the median signals from the duplicate wells on the Y-axis. The binding curves were fit with a standard four parameter sigmoidal binding curve and EC50's reported for all graphs with full curves. Data provided for representative antibodies in TABLE12.1.

	TABLE 12.1
		Cell binding		Cell binding
	Ab name	EC50 (nM)	Ab name	EC50 (nM)
	4H6	1.70	56E5	1.1
	4B1	4.1	72G9	0.41
	4A2	0.82	75G3	1
	4A2.001	1.8	176H4	1
	5E5	3.80	184E7	1
	6G7	0.6	190F8	9
	7G4	0.69	191G1	0.16
	7F4	5.40	191G10	0.31
	7E11	1.40	193E7	0.13
	7E11.001	3.2	194A4	25
	12D2	3.2	194C1	0.11
	22G5	7.2	194C10	0.56
	25A4	1.6	197G3	0.25
	25A4.001	1.2	198D2	0.14
	26C4	11	198G3	0.21
	29H8	1.9	202A3	0.8
	48B12	38	218G4	2.2
	54E9	5

For human ASGR-2, CHO—S stable cells expressing C-terminal His-tagged human ASGR-2 were resuspended in cold flow buffer (10 mM Tris, pH 7.5, 137 mM NaCl, 1 mM CaCl2 and 2% fetal bovine serum) and 1.5×10e6 cells per well were added to a 96-well, v-bottom plate in a volume of 80 ul. 80 ul of antibody at 400 nM was then added to each well. After incubation on ice for 30 min, the cells were centrifuged at 1400 rpm for 3 min and then washed twice in cold flow buffer. The cells were then resuspended in 120 ul of anti-human IgG-APC (diluted 1:1000 in flow buffer) and incubated on ice for 30 minutes, centrifuged and washed twice as before, and resuspended in 200 ul cold flow buffer, and then analyzed on a BD-LSR II flow cytometer. Data provided for antibody 7F4 in FIG. 43.

Example 13: CHO—S:huASGR-1 Ligand Blocking Assay

All ASGR-1 antibodies that bound either human or mouse ASGR-1 stable CHO—S cells were then tested for ligand blocking using both a protein ligand and a synthetic sugar ligand. The method in brief is as follows: first, 20 ul of either CHO-Shuman or mouse ASGR-1 cells were added to wells of a 384 well plate (30 k cells/well) followed by spin and discarding the supernatant. Second, 10 ul of the antibodies (either purified from hybridoma supernatants or made recombinantly) were added in duplicate to the cells in a dilution series (200 nM top concentration, 1:2 serial dilution, 11 point curve) and were incubated for 30 min at 4 C. Third, 10 ul of the minimally biotinylated ligands were added at 2× their binding EC05, so that the wells contained a final 20 ul volume with Ab starting at 100 nM and the ligand at their EC50. After 30 min incubation at 4 C, the plate was spun and washed twice with FACS buffer+1 mM CaCl2 followed by the detection streptavidin-AF647 at 1:1000 dilution. After 30 min at 4 C, the cells were spun and washed once and then 60 ul PI added at 1:1000 dilution and the plates delivered to a core flow cytometry facility. The plates were read and processed similarly to the cell binding method except the signal now represents an inhibition curve and typically decreases a function of increasing antibody concentration. IC50 nM potency and % Inhibition were reported. The desialylated, biotinylated asialofetuin (see Example 9A) and biotinylated GALNAc-PAA (Fisher #NC9024754) were used as ligands with measured binding EC50s of 10.7 and 5.4 nM. Differences in the ability of antibodies to block these two ligands could occur as a result of differences in, for example, avidity stemming from differences in the number and/or orientation of the ASGR binding terminal sugar residues of each ligand, steric hindrance between antibody and each ligand, and/or changes in the conformation of ASGR induced by antibody binding that selectively alters the binding of each ligand. Data provided for representative antibodies in TABLE 13.1.

	TABLE 13.1
	Ligand Blocking
	bn-GalNAc-PAA	bn-asialofetuin
Ab name	IC50 (nM)	% Inhibition	IC50 (nM)	% Inhibition
4H6	8.1	20%	12	85%
4B1	42	36%	64	75%
4A2	54	70%	11	99%
4A2.001	28	75	12	99
5E5	>200	0%	16	95%
6G7	>200	0%	11	99%
7G4	20	−30%	14	96%
7F4	0.24	30%	2.6	99%
7E11	40	37%	13	99%
7E11.001	>100	50	13	99
12D2	2.1	10%	10	20%
22G5	11	93%	3.4	99%
25A4	40	77%	11	99%
25A4.001	31	68	8.1	99
26C4	36	83%	6.6	99%
29H8	17	99%	7	99%
48B12	86	94%	19	99%
54E9	100	19%	50	75%
56E5	45	99%	23	99%
72G9	24	20%	53	20%
75G3	115	99%	29	99%
176H4	73	79%	59	99%
184E7	10	99%	23	99%
190F8	44	83%	34	98%
191G1	62	78%	24	99%
191G10	56	99%	27	99%
193E7	33	60%	30	99%
194A4	48	60%	57	99%
194C1	72	89%	34	99%
194C10	87	99%	30	99%
197G3	15	74%	29	90%
198D2	55	99%	22	99%
198G3	5	81%	26	99%
202A3	32	96%	16	98%
218G4	71	99%	28	99%

Example 14: ASGR-1 Specific Antibody Optimization (Chemical Degradation Site Engineering)

Variable domain sequence motifs having a high risk of sidechain degradation were engineered out of ASGR-1 specific antibodies. See for example, ASGR-1 specific antibody sequences in Tables 6 and 7.

Certain high risk motifs included: (1) CDR ‘NG’ and ‘NT’ sequences prone to asparagine deamidation, (2) CDR ‘DG,’ ‘DH’, ‘DS,’ and ‘DT’ sequences prone to aspartic acid isomerization, (3) and CDR3 tryptohphans prone to oxidation. Bioinformatics and structural analyses were used to identify substitutions likely to retain binding affinity to the ASGR-1 CBD. Typically, substitution identities were derived from germline sequences or from sequence-related ASGR-1 CBD-binding mAbs. These substitutions were then modeled into a homology model of the unbound mAb using the software MOE (CCG)¹ to predict structural fitness. For cases in which the bioinformatics or structural analyses did not provide a clear substitution identity, residue types chemically similar to the parent residue were identified.

Variable domain sequence motifs violating multiple sequence alignment-based pair-wise residue covariance trends² were also engineered out of ASGR-1 specific antibodies. Substitution identities for covariance violators were identified using a hybrid bioinformatics/structural approach similar to that used to remediate degradation sites.

• 1. Molecular Operating Environment (MOE), 2013.08; Chemical Computing Group, Inc., 1010 Sherbooke St. West, Suit #910, Montreal, QC, Canada, H3A 2R7, 2016.
• 2. Kannan, G. Method of Correlated Mutational Analysis to Improve Therapeutic Antibodies. US Patent Application PCT/US2012/028596 filed Mar. 9, 2012.

Example 15: Epitope Mapping Using Peptide Arrays

Custom peptide microarrays were obtained commercially (PEPperPRINT GmbH). For epitope mapping using linear arrays, the antigen (ASGR-1) was translated into 291 different overlapping 15 amino acid (aa) peptides printed in duplicate (582 peptide spots per array copy). For epitope mapping using cyclized arrays, the antigen (ASGR-1) was translated into 888 different overlapping 7 aa, 10 aa and 13 aa peptides printed in duplicate (1,776 peptide spots per array copy). Peptide cyclization was accomplished using N- to C-terminal thioether formation with and without an additional scaffold for varying conformational restriction. Each PEPperCHIP® Peptide array is framed by Flag (DYKDDDDKAS) and HA (YPYDVPDYAG) control peptides. Assay buffer was PBS-T (PBS, pH7.4, 0.05% Tween 20), blocking buffer was Rockland Blocking Buffer (Rockland Immunochemicals), staining buffer was assay buffer+10% Rockland Blocking buffer. Secondary antibody was goat anti-human IRDye680LT (Li-Cor). Control antibodies were anti-FLAG M2 DyLight800, anti-HA DyLight680. Arrays were scanned on Li-Cor Odyssey with an offset of 0.65 mm, 21 um resolution.

Array staining and detection was per manufacturer's instructions. Briefly, arrays were pre-stained with secondary antibodies for 30 minutes, washed and scanned to detect background binding. Arrays were then stained with commercially available primary antibodies overnight, followed by washing and 30 minute incubation with labeled secondary antibodies. Arrays were scanned to detect binding of anti-ASGR-1 antibodies. Finally, arrays were stained with control antibodies for 45 minutes prior to washing and scanning to detect control peptides.

Antigen binding proteins with desired binding properties can be identified using this assay.

Example 16: In Vivo Studies

RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 and/or antigen binding proteins, such as monoclonal antibodies, that inhibit ligand binding to ASGR, ASGR-1, and/or ASGR-2 in vitro can be administered in vivo to a relevant animal model and levels and/or activity of endogenous blood proteins like alkaline phosphatase measured. In addition, the clearance of exogenously administered ASGR ligands (for example asialoglycoproteins, certain non-asialylated proteins, synthetic ligands, etc.) can be inhibited by pre-treatment with RNAi or a co- or pre-administered antibody.

Additionally, physiologic effects of the antigen binding proteins or RNAi can be evaluated in relevant animal models of cardiovascular disease using readouts including blood pressure, primary and secondary hemostasis, heart function and morphology, endothelial function, LDL cholesterol levels, non-HDL cholesterol levels, inflammation, and atherosclerosis.

Example 17: Effect of ASGR-1 Antibody 4A2 on Serum LDL Cholesterol and Alkaline Phosphatase in Normal and Obese Cynomolgus Monkeys

The purpose of the study was to evaluate the LDL cholesterol (LDL-C)-lowering activity of anti-ASGR inhibitors. In general, cynomolgus monkeys do not have high levels of total cholesterol, HDL-C or LDL-C. Therefore, both normal and dyslipidemic models were utilized in this example. In the dyslipidemic model, monkeys were selected if their LDL levels were at least 100 mg/dL (normal is 40-60 mg/dL), and if there body mass index was over 41 kg/m² (normal is below 35 kg/m²). Animals that met these criterea on standard diet were classified as spontaneously obese dylipidemic. Other animals were fed a high-fat diet (HFD; 4.15 kcal/gm, 32% fat) prior to inclusion in the study and were classified as HFD obese dyslipidemic.

Naive male spontaneous obese dyslipidemic and HFD obese dyslipidemic cynolgous monkeys were given a single subcutaneous injection of anti-ASGR-1 antibody 4A2.001 (IgG1z-SEFL2) (10 mg/kg in 10 mM sodium acetate, 9% sucrose, 0.01% polysorbate-80, pH 5.2). Naïve male and female normal cynomolgus monkeys were given a single intravenous injection of anti-ASGR-1 antibody 4A2.001 (IgG1z-SEFL2)(100 mg/kg in 10 mM sodium acetate, 9% sucrose, 0.01% polysorbate-80, pH 5.2). Blood was collected from overnight fasted animals to monitor LDL-C and alkaline phosphatase (ALP) levels post-antibody injection. Blood was collected 70, 118, 190 and 268 hours post-injection (dyslipidemic models) and at 0.05, 0.25, 0.5, 1, 4, 8, 24, 48, 72, 168, 240, 336, 504, 672, 840, 1008, and 1176 hours post-injection (normal). LDL-C decrease (%) and ALP increase (%) were the main endpoints of the study and were measured on Roche C311 and C501 chemistry analyzers. Baseline levels of LDL-C and ALP were established from blood collected 7 days prior to antibody administration.

Dyslipidemic Model:

• Species: Macaca fascicularis
• Weight Range: >7.0 kg
• BMI Range: >41 kg/m²
• Age range: 12-17 years
• Time on HFD: 6 months
• Source: KBI monkey colony
• Number and Sex: 3 male spontaneous obese monkeys and 3 male HFD induced obese monkeys (BMI>41, LDL>80 mg/dL)). Animals were selected from a larger pool based on similar baseline LDL and ALP levels

Normal Model:

• Species: Macaca fascicularis
• Weight Range: 2.6-4.2 kg
• Age range: 2.5-4 years
• Number and Sex: 2 male and 1 female fed normal laboratory diet
  Data for this study is provided in FIG. 44 (dyslipidemic model) and FIG. 45 (normal model).

Example 18: Proteomic Profiling of Serum Samples from Human ASGR1 Carriers and Controls

Introduction

As described above in Example 1, ASGR1 loss-of-function (LOF) was found to be associated with a beneficial phenotype (protected from coronary artery disease, lower LDL cholesterol and longer life span) in human.¹. To understand the mechanism of action underlying this association and find potential biomarkers, proteomic measurement of human serum samples were performed and compared to changes in circulating protein levels between the ASGR1 LOF variant carriers and controls.

Materials and Methods

Sample Collection and Proteomic Profiling

A total of 333 human serum samples were acquired from the deCODE Icelandic population study, including 100 ASGR1 del12 heterozygous carriers (cases group) and 233 non-carriers (controls group). The Case/Control Groups are well matched by sex, age and collection time/freezer storage time. 150 ul serum samples were shipped to SomaLogic Inc, where 1310 proteins were measured by the SOMAscan Assay 1.3 k. The 1310 proteins were SOMAmer® Reagents Generated to Human Proteins, the complete list of tested proteins are summarized in the SOMAscan Assay 1.3K Content, Rev 1 (Effective: Sep. 21, 2015) which is incorpored by reference herein in its entirety.

The SOMAscan assay measured serum protein concentration using a Slow Off-rate Modified DNA Aptamer (SOMAmer)-based capture array. Each of the 1310 proteins is bond by its respective fluorescently labeled SOMAmer in the assay and their concentrations are reflected by the respective SOMAmer's relative fluorescence units (RFU).

Data Analysis

2 Samples were removed due to low volume that did not meet Somascan requirements and 13 samples were removed because they had been treated with EDTA. The RFU data of each measured protein was log transformed, then centered and scaled to calculate standardized RFU values for this protein. Principle components (PCs) were derived from 1310 standardized RFU values by principle components analysis. An outlier removal based on Hotellings T2 distribution of PC1 and PC2 was applied and excluded another 8 samples from further analysis.

After QC, the remaining 93 ASGR1 Del12 heterozygous Carriers (cases group) and 217 samples without the Del12 allele (controls group) and their standardized RFU values of each protein were analyzed by a linear model adjusting for Age, Sex, FreezerTime and the first 10 PCs,

Yi=β0+β1Gi+β2AGEi+β3SEXi+β4FTi+β5PC1i+ . . . +β15PC10i+εi

where Yi is the standardized RFU value for the i th sample for a particular protein, Gi is the Del12 genotype the i th sample and β1 capture the estimates of the mean difference between human samples with Del12 and without Del12. Since 1310 tests were performed for the proteins on Somascan platform, we calculated the significant threshold by Bonferroni method (0.05/1310=3.82×10⁻⁵) assuming these are independent tests. However, the Bonferroni correction is likely too stringent because proteins are often correlated with each other therefore these tests are not independent. Thus a realistic threshold of significance (5.19×10⁻⁵) was obtained by performing 100,000 permutations using the method by Sham and Purcell 2014³.

Results and Discussion

Using the permutation threshold, 41 Proteins were identified to have significant serum levels between human ASGR1 del12 carriers and non-carriers (P<5.19×10⁻⁵). Of those, 26 show significant increase in the carriers (Table 18.1) and 15 decrease significantly in the carriers (Table 18.2). These changes are likely to mediate the beneficial effects resulting from ASGR1 loss of function seen in the del12 carriers. The levels of these proteins in blood can serve as biomarkers for ASGR1 loss of function and be used to assess ASGR1-targeted therapy during drug development.

TABLE 18.1
Proteins with significant increase
in serum of ASGR1 del12 carriers.
	Estimate
p value	(SD)	Gene	Full Name
3.71E−54	1.34	TNFSF8	Tumor necrosis factor ligand
			superfamily member 8
1.33E−52	1.45	CD163	Scavenger receptor cysteine-rich
			type 1 protein M130
2.07E−25	1.09	CSF1R	Macrophage colony-stimulating
			factor 1 receptor
1.44E−24	1.16	LYVE1	Lymphatic vessel endothelial
			hyaluronic acid receptor 1
1.03E−22	0.65	IL6ST	Interleukin-6 receptor subunit beta
4.56E−15	0.67	IL18BP	Interleukin-18-binding protein
1.16E−12	0.74	CD300C	CMRF35-like molecule 6
2.47E−12	0.59	TYRO3	Tyrosine-protein kinase receptor
			TYRO3
8.85E−12	0.80	LRP8	Low-density lipoprotein receptor-
			related protein 8
1.76E−09	0.66	IL1RL1	Interleukin-1 receptor-like 1
2.62E−09	0.61	ISLR2	Immunoglobulin superfamily
			containing leucine-rich repeat
			protein 2
4.01E−09	0.55	SIGLEC7	Sialic acid-binding Ig-like lectin 7
4.47E−09	0.48	NRXN3	Neurexin-3-beta
1.03E−07	0.58	PLAU	Urokinase-type plasminogen
			activator
2.96E−07	0.37	CD55	Complement decay-accelerating
			factor
8.27E−07	0.53	CD48	CD48 antigen
1.22E−06	0.31	TNFRSF21	Tumor necrosis factor receptor
			superfamily member 21
1.62E−06	0.36	MRC2	C-type mannose receptor 2
3.82E−06	0.57	KLK13	Kallikrein-13
4.95E−06	0.33	IGF1R	Insulin-like growth factor 1
			receptor
1.46E−05	0.45	ANGPT2	Angiopoietin-2
2.02E−05	0.39	CNTN4	Contactin-4
2.57E−05	0.47	FCGR3B	Low affinity immunoglobulin
			gamma Fc region receptor
			III-B
2.93E−05	0.38	C1S	Complement C1s subcomponent
3.92E−05	0.40	LY9	T-lymphocyte surface antigen Ly-9
4.48E−05	0.46	CD200R1	Cell surface glycoprotein
			CD200 receptor 1

TABLE 18.2
Proteins with significant decrease
in serum of ASGR1 del12 carriers.
	Estimate
p value	(SD)	Gene	Target Full Name
1.08E−09	−0.52	CD93	Complement component C1q
			receptor
6.32E−09	−0.50	IDS	Iduronate 2-sulfatase
1.56E−07	−0.34	RGMB	RGM domain family member B
2.91E−07	−0.44	TGFBI	Transforming growth factor-beta-
			induced protein ig-h3
5.56E−07	−0.48	LUM	Lumican
6.67E−07	−0.46	MMP2	72 kDa type IV collagenase
1.36E−06	−0.38	FLRT2	Leucine-rich repeat transmembrane
			protein FLRT2
2.18E−06	−0.48	AHSG	Alpha-2-HS-glycoprotein
2.44E−06	−0.37	CSH1	Chorionic somatomammotropin
		CSH2	hormone
3.16E−06	−0.54	ESM1	Endothelial cell-specific
			molecule 1
1.36E−05	−0.52	AFM	Afamin
1.67E−05	−0.48	TNFRSF17	Tumor necrosis factor receptor
			superfamily member 17
2.68E−05	−0.46	OMD	Osteomodulin
4.69E−05	−0.23	GDI2	Rab GDP dissociation inhibitor
			beta
5.09E−05	−0.45	SPOCK2	Testican-2

REFERENCES

• 1 See also, Nioi, P. et al. Variant ASGR1 Associated with a Reduced Risk of Coronary Artery Disease. The New England journal of medicine 374, 2131-2141, doi:10.1056/NEJMoa1508419 (2016).
• 2 Gold, L. et al. Aptamer-based multiplexed proteomic technology for biomarker discovery. PLoS One 5, e15004, doi:10.1371/journal.pone. 0015004 (2010).
• 3 Sham, P. C. & Purcell, S. M. Statistical power and significance testing in large-scale genetic studies. Nature reviews. Genetics 15, 335-346, doi:10.1038/nrg3706 (2014).

Example 19: Proteomic Profiling of Serum Samples from ASGR1 Cyno PK-PD Study

Introduction

As decribed above in Example 1, ASGR1 loss-of-function (LOF) was found to be associated with a beneficial phenotype (protected from coronary artery disease, lower LDL cholesterol and longer life span) in human¹. Certain ASGR-1 antigen binding proteins disclosed herein were found to mimic the LOF effects, and can be useful in the treatment of coronary artery disease. In brief, cynomolgus monkeys were treated with certain ASGR-1 specific, ligand blocking antibodies in order to study the PK-PD profile of these antibodies. Moreover, a dose-dependent elevation of alkaline phosphatase (ALP) levels was observed in the Ab-treated cynos, which resembles the ALP elevation seen in human ASGR1 LOF carriers. In addition to ALP, proteomic profiling in human serum identified 41 proteins that potentially underlie the beneficial effects caused by ASGR1 LOF as described above in Example 18. To compare effects of anti-ASGR1 antibody treatment with the human ASGR1 LOF and identify comparable signatures in cynomolgus monkey, proteomic measurement of the serum samples from this study was conducted. The list of proteins with altered levels in the antibody-treated animals is compared to the ones identified in human LOF carriers.

Materials and Methods

Sample Selection and Proteomic Profiling

6 animal groups with 3 animals in each group were selected for proteomic profiling. The 6 groups include 5 antibody-treated groups (mAb1/25A4, mAb2/4A2, mAb3/7E11, mAb4/5E5 and mAb8/4H6) and a vehicle control group (mAb6). The animals were dosed once at 100 mg/kg. Serum samples from time points 0, 168, 336, 504, 672 and 1176 hours were collected for each animal (Table 19.1 & 19.2). The only exception is group mAb8/4H6, where time point 1008 hour is used instead of 1176 hour. 120 ul serum samples were shipped to SomaLogic Inc, where 1310 proteins (see table 18.0) were measured by the SOMAscan Assay 1.3 k.

The SOMAscan assay measures serum protein concentration using a Slow Off-rate Modified DNA Aptamer (SOMAmer)-based capture array. Each of the 1310 proteins is bond by its respective fluorescently labeled SOMAmer in the assay and their concentrations are reflected by the respective SOMAmer's relative fluorescence units (RFU).

TABLE 19.1
Serum sample selection.
	Time points
Animal		D0	D8	D15	D22	D29	D50
group	Animal Number	0 hr	168 hr	336 hr	504 hr	672 hr	1176 hr
25A4	701, 702, 703	✓	✓	✓	✓	✓	✓
4A2	704, 705, 706	✓	✓	✓	✓	✓	✓
7E11	707, 708, 711	✓	✓	✓	✓	✓	✓
5E5	709, 710, 712	✓	✓	✓	✓	✓	✓
SEFL2-	716, 717, 718	✓	✓	✓	✓	✓	✓
control
4H6	204, 205, 206	✓	✓	✓	✓	✓	✓*
*4H6 was collected at D43 (1008 hr).

TABLE 19.2
List of all sample groups by treatment and time points.
	Treatment
Sample	(e.g., drug,	Time	# of Samples
group	vehicle, etc.)	point	in Group	Subject ID
25A4_D0	mAb1	0	Hr	3	701, 702, 703
25A4_D8	mAb1	168	Hr	3	701, 702, 703
25A4_D15	mAb1	336	Hr	3	701, 702, 703
25A4_D22	mAb1	504	Hr	3	701, 702, 703
25A4_D29	mAb1	672	Hr	3	701, 702, 703
25A4_D50	mAb1	1176	Hr	3	701, 702, 703
4A2_D0	mAb2	0	Hr	3	704, 705, 706
4A2_D8	mAb2	168	Hr	3	704, 705, 706
4A2_D15	mAb2	336	Hr	3	704, 705, 706
4A2_D22	mAb2	504	Hr	3	704, 705, 706
4A2_D29	mAb2	672	Hr	3	704, 705, 706
4A2_D50	mAb2	1176	Hr	3	704, 705, 706
7E11_D0	mAb3	0	Hr	3	707, 708, 711
7E11_D8	mAb3	168	Hr	3	707, 708, 711
7E11_D15	mAb3	336	Hr	3	707, 708, 711
7E11_D22	mAb3	504	Hr	3	707, 708, 711
7E11_D29	mAb3	672	Hr	3	707, 708, 711
7E11_D50	mAb3	1176	Hr	3	707, 708, 711
5E5_D0	mAb4	0	Hr	3	709, 710, 712
5E5_D8	mAb4	168	Hr	3	709, 710, 712
5E5_D15	mAb4	336	Hr	3	709, 710, 712
5E5_D22	mAb4	504	Hr	3	709, 710, 712
5E5_D29	mAb4	672	Hr	3	709, 710, 712
5E5_D50	mAb4	1176	Hr	3	709, 710, 712
CTL_D0	mAb6	0	Hr	3	716, 717, 718
CTL_D8	mAb6	168	Hr	3	716, 717, 718
CTL_D15	mAb6	336	Hr	3	716, 717, 718
CTL_D22	mAb6	504	Hr	3	716, 717, 718
CTL_D29	mAb6	672	Hr	3	716, 717, 718
CTL_D50	mAb6	1176	Hr	3	716, 717, 718
4H6_D0	mAb8	0	Hr	3	204, 205, 206
4H6_D8	mAb8	168	Hr	3	204, 205, 206
4H6_D15	mAb8	336	Hr	3	204, 205, 206
4H6_D22	mAb8	504	Hr	3	204, 205, 206
4H6_D29	mAb8	672	Hr	3	204, 205, 206
4H6_D43	mAb8	1008	Hr	3	204, 205, 206

Data Analysis

As the SOMAscan assay was developed for humans, some proteins in cynomolgus monkey may not be recognized by the SOMAmer reagents. As a result, SOMAscan measurements of these proteins would have low credibility and may not reflect the true protein levels. A simple criterion was defined to determine the credibility of the measurements, assuming the serum levels of a given protein are in relatively close range in human and cynomolgus monkey. The mean and range of each protein level in human are calculated based on the 217 human control samples from the human proteomic study described in Example 18. The mean and range of each protein level in cynomolgus monkey are calculated based on a total of 48 samples including measurements of all time points for the SEFL-2 control group and the pre-treatment (D0) and washout period (D50) measurements of all the other groups. A protein measurement would be assigned low credibility if (1) its range in cynomolgus monkey is not overlapping with human; and (2) there is a 5 fold difference between the mean level of this protein in human and cynomolgus monkey. A total of 162 proteins were determined as low-credibility by these criteria and were excluded (FIG. 58, which depicts a summary of the credibility of protein measurements in cynomolgus monkey). In FIG. 58, log 10 RFU of mean protein levels in the two species are plotted and the ones with low credibility (light shading) and high credibility (black) are marked.

One sample in the 4H6 group was removed due to low volume that did not meet the requirements for the SOMAscan assay. No outliers were found in the principle components analysis. A linear mixed model adjusting for potential confounding factors was used to test whether the ASGR1 antibody treatment changes each protein level differently from the control group over time points,

Y_ti=β₀+β₁TREATGROUP_i+β₂TIME_ti+β₃(TREATGROUP_i)(TIME_ti)+β₄COV_ti+ . . . +β_m+4COV_ti+b_0i+ε_ti

which is determined by the p-value for β₃ (i.e., treatment by time interaction; mean difference in slopes between treatment conditions). The random effect b_0i captures individual animal heterogeneity. The TREATGROUP is coded as (25A4=4A2=7E11=5E5=4H6=1; SELF-2=0) and TIME is coded as (D8=D15=D22=D29=1; D0=D50=0) to test for the ASGR1 antibodies effect after treatment comparing to pre-treatment and washout period. Since multiple tests were performed for the proteins on SOMAscan platform, a Bonferroni corrected significant threshold (5×10⁻⁵) was used.

Results and Discussion

33 proteins were identified to have significant serum level changes after ASGR1 antibody treatment (Table 19.3; P<5×10⁻⁵). Interestingly, all the 33 proteins show increased levels (1.36˜10.18 fold) after ASGR1 antibody treatment.

TABLE 19.3
Proteins with significant changes after ASGR1
antibody treatment in Cynomolgus monkey.
	Estimated
	Fold
P-value	Change	Gene	Full Name
1.87E−13	10.18	TNFSF8	Tumor necrosis factor ligand
			superfamily member 8
1.01E−06	8.56	ASGR1	Asialoglycoprotein receptor 1
1.35E−10	3.93	ADGRE2	Adhesion G protein-coupled
			receptor E2
2.74E−11	2.86	CD86	T-lymphocyte activation
			antigen CD86
1.46E−11	2.81	TNFRSF21	Tumor necrosis factor receptor
			superfamily member 21
7.48E−10	2.57	L1CAM	Neural cell adhesion molecule L1
6.09E−12	2.42	PLXNC1	Plexin-C1
1.22E−07	2.11	MRC2	C-type mannose receptor 2
1.18E−06	2.10	AMIGO2	Amphoterin-induced protein 2
2.28E−11	2.02	ANGPT2	Angiopoietin-2
6.68E−09	1.99	INSR	Insulin receptor
1.02E−10	1.93	IL17RA	Interleukin-17 receptor A
7.12E−12	1.90	NRXN3	Neurexin-3-beta
5.95E−06	1.85	GPNMB	Transmembrane glycoprotein NMB
2.03E−06	1.74	IGF1R	Insulin-like growth factor 1
			receptor
3.91E−09	1.73	PLAUR	Urokinase plasminogen activator
			surface receptor
3.58E−09	1.69	FGFR1	Fibroblast growth factor receptor 1
1.26E−06	1.60	LRP8	Low-density lipoprotein receptor-
			related protein 8
3.87E−09	1.55	LYPD3	Ly6/PLAUR domain-containing
			protein 3
3.17E−06	1.55	GRN	Granulins
4.27E−05	1.54	CNTN4	Contactin-4
4.59E−07	1.54	KDR	Vascular endothelial growth factor
			receptor 2
4.99E−06	1.53	IL12RB2	Interleukin-12 receptor subunit
			beta-2
5.85E−06	1.52	ROBO3	Roundabout homolog 3
1.44E−06	1.50	ALCAM	CD 166 antigen
3.83E−05	1.46	TYRO3	Tyrosine-protein kinase receptor
			TYRO3
3.09E−05	1.45	CADM1	Cell adhesion molecule 1
1.53E−08	1.44	JAG1	Protein jagged-1
2.58E−09	1.43	ISLR2	Immunoglobulin superfamily
			containing leucine-rich
			repeat protein 2
3.11E−05	1.39	SET	Protein SET
4.64E−05	1.38	IL20RA	Interleukin-20 receptor subunit
			alpha
2.15E−06	1.36	KLRK1	NKG2-D type II integral
			membrane protein
2.39E−05	1.36	GFRA2	GDNF family receptor alpha-2

To compare results from this study with the human proteomic study, a list of proteins made by the 33 proteins in Table 19.3 and the top 41 proteins identified in human was compiled. This results in a list of 64 proteins total. The estimates of protein level change and p-value of the changes in the studies were compared (Table 19.4). Based on concordance of change in the cyno (in response to ASGR1 antibody treatment) and human (in response to ASGR1 LOF) studies, the proteins are classified into 5 tiers. Tier 1 includes 10 proteins that pass the stringent Bonferroni corrected significance level (p<5×10⁻⁵) in both studies with the same direction of changes. The number of proteins supported by strong evidence in both studies are much higher than the number one would expect by chance (p=1.58×10⁻⁸; Fisher's exact test). It indicates that ASGR1 Ab treatment can induce a serum protein levels change in cyno that is similar to the effect of del12 LOF variant in Human. Therefore, these proteins are the core biomarkers. For example, the strongest biomarker TNFSF8 had more than 10 fold increase after ASGR1 Antibody treatment (FIGS. 59A-59D, which depict the results of serum protein levels of TNFSF8 in cyno and human studies).

Tier 2 contains 12 proteins with strong evidence (p<5×10⁻⁵) in the cyno study and suggestive evidence (p<0.05) in human with the same direction of changes. Both Tier 1 and 2 proteins have increased levels in both studies. Tier 3 includes 11 proteins that are found significant only in the cyno study but not human. These proteins are likely to be biomarkers specific for the drug modality or for cynomolgus monkeys. For example, the soluble secreted form of ASGR1 increased more than 10 fold after antibody treatment but no significant difference was observed in human between the ASGR1 del12 carriers and non-carriers. Tier 4 contains 17 proteins with significant evidence (p<5×10⁻⁵) in the human study but not supported by the cyno study. Majority of the proteins in Tier 4 has decrease levels in human del12 carriers. This observation may indicate a difference between antibody treatment and constitutive gene LOF. It could also possibly be due to species difference or simply caused by lower statistical power in the cyno study.

Lastly, there are 14 proteins with significant changes in human classified as Tier 5 because they were excluded in the cyno study due to the low credibility of their SOMAmer reagents.

In summary, the two studies show high degree of concordance between the antibody treatment in cynomolgus monkey and ASGR1 LOF in humans, with 10 proteins (Tier 1) showing very significant changes in the same direction in both studies. The ASGR-1 antibody treatment is working well as a way of mimicking the effects of ASGR1 LOF in humans and can be useful in the treatment of coronary artery disease.

TABLE 19.4
Five tiers of protein biomarkers and comparison of the estimates
of protein level change and p-value between the two studies.
	human	Cyno
		Estimate		Estimate
Target Full Name	Gene	(SD)	P-value	log2FC	P-value	Tier
Tumor necrosis factor ligand superfamily member 8	TNFSF8	1.34	3.7E−54	3.35	1.87E−13	1
Tumor necrosis factor receptor superfamily	TNFRSF21	0.31	1.2E−06	1.49	1.46E−11	1
member 21
C-type mannose receptor 2	MRC2	0.36	1.6E−06	1.08	1.22E−07	1
Angiopoietin-2	ANGPT2	0.45	1.5E−05	1.01	2.28E−11	1
Neurexin-3-beta	NRXN3	0.48	4.5E−09	0.93	7.12E−12	1
Insulin-like growth factor 1 receptor	IGF1R	0.33	5.0E−06	0.80	2.03E−06	1
Low-density lipoprotein receptor-related protein 8	LRP8	0.80	8.9E−12	0.68	1.26E−06	1
Contactin-4	CNTN4	0.39	2.0E−05	0.63	4.27E−05	1
Tyrosine-protein kinase receptor TYRO3	TYRO3	0.59	2.5E−12	0.55	3.83E−05	1
Immunoglobulin superfamily containing leucine-	ISLR2	0.61	2.6E−09	0.52	2.58E−09	1
rich repeat protein 2
T-lymphocyte activation antigen CD86	CD86	0.39	2.1E−03	1.52	2.74E−11	2
Neural cell adhesion molecule L1	L1CAM	0.30	5.5E−03	1.36	7.48E−10	2
Plexin-C1	PLXNC1	0.40	1.0E−04	1.28	6.09E−12	2
Amphoterin-induced protein 2	AMIGO2	0.44	1.9E−04	1.07	1.18E−06	2
Interleukin-17 receptor A	IL17RA	0.29	0.03	0.95	1.02E−10	2
Urokinase plasminogen activator surface receptor	PLAUR	0.35	3.3E−04	0.79	3.91E−09	2
Fibroblast growth factor receptor 1	FGFR1	0.30	2.3E−03	0.75	3.58E−09	2
Granulins	GRN	0.27	5.7E−03	0.63	3.17E−06	2
CD166 antigen	ALCAM	0.20	9.1E−03	0.58	1.44E−06	2
Protein jagged-1	JAG1	0.17	0.01	0.53	1.53E−08	2
Protein SET	SET	0.28	2.1E−03	0.47	3.11E−05	2
GDNF family receptor alpha-2	GFRA2	0.39	9.2E−05	0.44	2.39E−05	2
Asialoglycoprotein receptor 1	ASGR1	0.00	0.99	3.10	1.01E−06	3
Adhesion G protein-coupled receptor E2	ADGRE2	0.04	0.70	1.97	1.35E−10	3
Insulin receptor	INSR	0.20	0.06	1.00	6.68E−09	3
Transmembrane glycoprotein NMB	GPNMB	−0.22	0.01	0.89	5.95E−06	3
Ly6/PLAUR domain-containing protein 3	LYPD3	−0.06	0.26	0.63	3.87E−09	3
Vascular endothelial growth factor receptor 2	KDR	0.19	0.09	0.63	4.59E−07	3
Interleukin-12 receptor subunit beta-2	IL12RB2	0.11	0.38	0.61	4.99E−06	3
Roundabout homolog 3	ROB03	0.08	0.55	0.61	5.85E−06	3
Cell adhesion molecule 1	CADM1	−0.17	0.02	0.53	3.09E−05	3
Interleukin-20 receptor subunit alpha	IL20RA	0.05	0.69	0.47	4.64E−05	3
NKG2-D type II integral membrane protein	KLRK1	−0.14	0.25	0.44	2.15E−06	3
Lymphatic vessel endothelial hyaluronic acid	LYVE1	1.16	1.44E−24	0.00	0.96	4
receptor 1
CMRF35-like molecule 6	CD300C	0.74	1.16E−12	0.03	0.39	4
Interleukin-1 receptor-like 1	IL1RL1	0.66	1.76E−09	0.75	0.10	4
Kallikrein-13	KLK13	0.57	3.82E−06	0.08	0.42	4
CD48 antigen	CD48	0.53	8.27E−07	−0.06	0.81	4
Rab GDP dissociation inhibitor beta	GDI2	−0.23	4.69E−05	−0.27	0.09	4
Chorionic somatomammotropin hormone	CSH1 CSH2	−0.37	2.44E−06	0.19	9.4E−03	4
Leucine-rich repeat transmembrane protein	FLRT2	−0.38	1.36E−06	0.30	0.03	4
FLRT2
Transforming growth factor-beta-induced protein	TGFBI	−0.44	2.91E−07	0.13	0.46	4
ig-h3
Testican-2	SPOCK2	−0.45	5.09E−05	0.10	0.96	4
72 kDa type IV collagenase	MMP2	−0.46	6.67E−07	0.13	0.48	4
Osteomodulin	OMD	−0.46	2.68E−05	0.12	0.78	4
Alpha-2-HS-glycoprotein	AHSG	−0.48	2.18E−06	0.00	0.97	4
Iduronate 2-sulfatase	IDS	−0.50	6.32E−09	0.05	0.33	4
Complement component C1q receptor	CD93	−0.52	1.08E−09	0.19	0.15	4
Afamin	AFM	−0.52	1.36E−05	0.02	0.94	4
Endothelial cell-specific molecule 1	ESM1	−0.54	3.16E−06	0.09	0.56	4
Scavenger receptor cysteine-rich type 1 protein	CD163	1.45	1.33E−52	NA	NA	5
M130
Macrophage colony-stimulating factor 1 receptor	CSF1R	1.09	2.07E−25	NA	NA	5
Interleukin-18-binding protein	IL18BP	0.67	4.56E−15	NA	NA	5
Interleukin-6 receptor subunit beta	IL6ST	0.65	1.03E−22	NA	NA	5
Urokinase-type plasminogen activator	PLAU	0.58	1.03E−07	NA	NA	5
Sialic acid-binding Ig-like lectin 7	SIGLEC7	0.55	4.01E−09	NA	NA	5
Low affinity immunoglobulin gamma Fc region	FCGR3B	0.47	2.57E−05	NA	NA	5
receptor III-B
Cell surface glycoprotein CD200 receptor 1	CD200R1	0.46	4.48E−05	NA	NA	5
T-lymphocyte surface antigen Ly-9	LY9	0.40	3.92E−05	NA	NA	5
Complement C1s subcomponent	C1S	0.38	2.93E−05	NA	NA	5
Complement decay-accelerating factor	CD55	0.37	2.96E−07	NA	NA	5
RGM domain family member B	RGMB	−0.34	1.56E−07	NA	NA	5
Lumican	LUM	−0.48	5.56E−07	NA	NA	5
Tumor necrosis factor receptor superfamily	TNFRSF17	−0.48	1.67E−05	NA	NA	5
member 17

REFERENCES

• 1 See also, Nioi, P. et al. Variant ASGR1 Associated with a Reduced Risk of Coronary Artery Disease. The New England journal of medicine 374, 2131-2141, doi:10.1056/NEJMoa1508419 (2016).
• 2 Gold, L. et al. Aptamer-based multiplexed proteomic technology for biomarker discovery. PLoS One 5, e15004, doi:10.1371/journal.pone. 0015004 (2010).

Example 20: Method of Reducing a Risk of Cardiovascular Disease

A subject at risk of cardiovascular disease is identified. One or more antibodies as provided herein (see Example 7, as well as Tables A, B and C) and/or RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 (as outlined in Example 3), are administered to a subject at risk of cardiovascular disease. The antibody and/or RNAi construct reduces the level of expression of ASGR, ASGR-1 and/or ASGR-2. Subsequent rounds of antibodies and/or RNAi are administered to the subject. One or more of the markers in Example 19 (e.g., Tier 1) is monitored to make certain that an adequate amount of the antibody and/or RNAi construct is administered and is functioning as desired. The risk that the subject will experience cardio vascular disease is decreased.

Additionally, as a further option, physiologic effects of the antibody and/or RNAi can be evaluated in relevant animal models of cardiovascular disease using readouts including blood pressure, primary and secondary hemostasis, heart function and morphology, endothelial function, LDL cholesterol levels, non-HDL cholesterol levels, inflammation, and/or atherosclerosis.

Example 21: Method of Reducing a Risk of Myocardial Infarction or Coronary Artery Disease

A subject at risk of a myocardial infarction or coronary artery disease is identified. One or more antibodies as provided herein (see Example 7, as well as Tables A, B and C) and/or RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 (as outlined in Example 3), are administered to a subject at risk of a myocardial infarction or coronary artery disease. The antibody and/or RNAi construct reduces the level of expression of ASGR, ASGR-1 and/or ASGR-2. Subsequent rounds of antibodies and/or RNAi are administered to the subject. One or more of the markers in Example 19 (e.g., Tier 1) is monitored to make certain that an adequate amount of the antibody and/or RNAi construct is administered and is functioning as desired. The risk that the subject will experience a myocardial infarction or coronary artery disease is decreased.

Additionally, as a further option, physiologic effects of the antibody and/or RNAi can be evaluated in relevant animal models of myocardial infarction or coronary artery disease using readouts including blood pressure, primary and secondary hemostasis, heart function and morphology, endothelial function, LDL cholesterol levels, non-HDL cholesterol levels, inflammation, and/or atherosclerosis.

Example 22: Method of Reducing LDL Cholesterol

A subject having a LDL cholesterol level to be lowered is identified. One or more antibodies as provided herein (see Example 7, as well as Tables A, B and C) and/or RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 (as outlined in Example 3), are administered to the subject. The antibody and/or RNAi construct reduces the level of expression of ASGR, ASGR-1 and/or ASGR-2. Subsequent rounds of antibodies and/or RNAi are administered to the subject. One or more of the markers in Example 19 (e.g., tier 1) is monitored to make certain that an adequate amount of the antibody and/or RNAi construct is administered and is functioning as desired. The level of LDL cholesterol in the subject is thereby reduced.

Example 23: Method of Reducing Non-HDL Cholesterol

A subject having a non-HDL cholesterol level to be lowered is identified. One or more antibodies as provided herein (see Example 7, as well as Tables A, B and C) and/or RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 (as outlined in Example 3), are administered to the subject. The antibody and/or RNAi construct reduces the level of expression of ASGR, ASGR-1 and/or ASGR-2. Subsequent rounds of antibodies and/or RNAi are administered to the subject. One or more of the markers in Example 19 (e.g., Tier 1) is monitored to make certain that an adequate amount of the antibody and/or RNAi construct is administered and is functioning as desired. The level of non-HDL cholesterol in the subject is thereby reduced.

Example 24: Method of Increasing ALP Levels

One or more antibodies as provided herein (see Example 7, as well as Tables A, B, and C) and/or RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 (as outlined in Example 3), are administered to the subject. The antibody and/or RNAi construct reduces the level of expression of ASGR, ASGR-1 and/or ASGR-2. Subsequent rounds of antibodies and/or RNAi are administered to the subject. One or more of the markers in Example 19 (e.g., Tier 1) is monitored to make certain that an adequate amount of the antibody and/or RNAi construct is administered and is functioning as desired. The level of ALP in the subject is thereby increased.

Example 25: Method of Monitoring the Effectiveness of an ASGR-1 Therapy

One or more antibodies as provided herein (see Example 7, as well as Tables A, B and C) and/or RNAi constructs that reduce expression of ASGR-1 and/or ASGR-2 (as outlined in Example 3), are administered to the subject. One or more of the markers in Example 19 is monitored to make certain that an adequate amount of the antibody and/or RNAi construct is administered and is functioning as desired. When the marker level changes in a similar manner to those changes noted in Example 19 (e.g., Tier 1), it is evidence that the amount of the one or more antibody and/or RNAi is effective. Additionally, as a further option, the effectiveness of this biochemical change can be observed by its physiologic effects from the antibody and/or RNAi, which can be evaluated using readouts including blood pressure, primary and secondary hemostasis, heart function and morphology, endothelial function, LDL cholesterol levels, non-HDL cholesterol levels, inflammation, and/or atherosclerosis.

TABLE 10.1
ATOM	1	O	THR	A	151	−35.000	−25.802	13.973	1.00	41.82	O
ATOM	2	N	THR	A	151	−34.909	−27.403	11.804	1.00	40.99	N
ATOM	3	CA	THR	A	151	−34.274	−27.888	13.020	1.00	40.74	C
ATOM	4	C	THR	A	151	−34.232	−26.755	14.051	1.00	40.85	C
ATOM	5	CB	THR	A	151	−32.835	−28.381	12.758	1.00	37.81	C
ATOM	6	OG1	THR	A	151	−32.738	−28.919	11.438	1.00	46.22	O
ATOM	7	CG2	THR	A	151	−32.470	−29.491	13.725	1.00	44.52	C
ATOM	8	O	CYS	A	152	−30.928	−26.774	16.222	1.00	27.69	O
ATOM	9	N	CYS	A	152	−33.315	−26.861	15.005	1.00	43.00	N
ATOM	10	CA	CYS	A	152	−33.119	−25.852	16.027	1.00	32.33	C
ATOM	11	C	CYS	A	152	−31.621	−25.772	16.312	1.00	30.92	C
ATOM	12	CB	CYS	A	152	−33.900	−26.213	17.289	1.00	36.97	C
ATOM	13	SG	CYS	A	152	−34.435	−24.804	18.287	1.00	47.04	S
ATOM	14	N	CYS	A	153	−31.104	−24.590	16.620	1.00	26.78	N
ATOM	15	CA	CYS	A	153	−29.716	−24.493	17.055	1.00	24.74	C
ATOM	16	C	CYS	A	153	−29.577	−25.058	18.464	1.00	26.56	C
ATOM	17	O	CYS	A	153	−30.538	−25.026	19.235	1.00	25.88	O
ATOM	18	CB	CYS	A	153	−29.243	−23.040	17.017	1.00	21.46	C
ATOM	19	SG	CYS	A	153	−29.368	−22.304	15.376	1.00	33.20	S
ATOM	20	N	PRO	A	154	−28.379	−25.571	18.813	1.00	26.96	N
ATOM	21	CA	PRO	A	154	−28.146	−26.019	20.190	1.00	20.79	C
ATOM	22	C	PRO	A	154	−28.236	−24.848	21.163	1.00	22.57	C
ATOM	23	O	PRO	A	154	−28.081	−23.710	20.737	1.00	22.50	O
ATOM	24	CB	PRO	A	154	−26.715	−26.585	20.147	1.00	20.99	C
ATOM	25	CG	PRO	A	154	−26.432	−26.822	18.709	1.00	21.42	C
ATOM	26	CD	PRO	A	154	−27.183	−25.760	17.974	1.00	19.94	C
ATOM	27	N	VAL	A	155	−28.499	−25.124	22.438	1.00	21.58	N
ATOM	28	CA	VAL	A	155	−28.490	−24.090	23.462	1.00	20.72	C
ATOM	29	C	VAL	A	155	−27.187	−23.287	23.412	1.00	25.13	C
ATOM	30	O	VAL	A	155	−26.109	−23.865	23.218	1.00	27.20	O
ATOM	31	CB	VAL	A	155	−28.664	−24.704	24.884	1.00	23.97	C
ATOM	32	CG1	VAL	A	155	−28.384	−23.669	25.957	1.00	27.90	C
ATOM	33	CG2	VAL	A	155	−30.062	−25.267	25.061	1.00	25.53	C
ATOM	34	N	ASN	A	156	−27.299	−21.968	23.586	1.00	20.81	N
ATOM	35	CA	ASN	A	156	−26.158	−21.050	23.634	1.00	24.68	C
ATOM	36	C	ASN	A	156	−25.568	−20.824	22.253	1.00	25.74	C
ATOM	37	O	ASN	A	156	−24.518	−20.206	22.106	1.00	25.52	O
ATOM	38	CB	ASN	A	156	−25.070	−21.552	24.603	1.00	30.21	C
ATOM	39	CG	ASN	A	156	−25.565	−21.628	26.041	1.00	38.75	C
ATOM	40	OD1	ASN	A	156	−26.494	−20.908	26.430	1.00	35.88	O
ATOM	41	ND2	ASN	A	156	−24.953	−22.502	26.835	1.00	33.84	N
ATOM	42	N	TRP	A	157	−26.247	−21.340	21.237	1.00	24.43	N
ATOM	43	CA	TRP	A	157	−25.928	−20.981	19.866	1.00	23.93	C
ATOM	44	C	TRP	A	157	−26.920	−19.930	19.389	1.00	26.16	C
ATOM	45	O	TRP	A	157	−28.032	−19.841	19.904	1.00	28.51	O
ATOM	46	CB	TRP	A	157	−25.965	−22.202	18.965	1.00	22.94	C
ATOM	47	CG	TRP	A	157	−24.818	−23.129	19.174	1.00	24.76	C
ATOM	48	CD1	TRP	A	157	−24.459	−23.752	20.336	1.00	20.94	C
ATOM	49	CD2	TRP	A	157	−23.887	−23.562	18.180	1.00	19.03	C
ATOM	50	NE1	TRP	A	157	−23.355	−24.540	20.126	1.00	23.79	N
ATOM	51	CE2	TRP	A	157	−22.983	−24.440	18.809	1.00	21.53	C
ATOM	52	CE3	TRP	A	157	−23.717	−23.273	16.828	1.00	15.83	C
ATOM	53	CZ2	TRP	A	157	−21.927	−25.043	18.124	1.00	16.56	C
ATOM	54	CZ3	TRP	A	157	−22.667	−23.866	16.152	1.00	18.56	C
ATOM	55	CH2	TRP	A	157	−21.790	−24.746	16.798	1.00	13.77	C
ATOM	56	N	VAL	A	158	−26.520	−19.120	18.420	1.00	25.61	N
ATOM	57	CA	VAL	A	158	−27.394	−18.058	17.951	1.00	23.85	C
ATOM	58	C	VAL	A	158	−27.857	−18.367	16.536	1.00	26.75	C
ATOM	59	O	VAL	A	158	−27.048	−18.589	15.642	1.00	24.47	O
ATOM	60	CB	VAL	A	158	−26.698	−16.690	17.998	1.00	26.10	C
ATOM	61	CG1	VAL	A	158	−27.691	−15.587	17.690	1.00	21.15	C
ATOM	62	CG2	VAL	A	158	−26.076	−16.469	19.368	1.00	27.52	C
ATOM	63	N	GLU	A	159	−29.170	−18.411	16.351	1.00	30.02	N
ATOM	64	CA	GLU	A	159	−29.751	−18.659	15.043	1.00	28.56	C
ATOM	65	C	GLU	A	159	−29.824	−17.359	14.272	1.00	25.78	C
ATOM	66	O	GLU	A	159	−30.140	−16.313	14.840	1.00	24.18	O
ATOM	67	CB	GLU	A	159	−31.145	−19.279	15.182	1.00	24.88	C
ATOM	68	CG	GLU	A	159	−31.764	−19.742	13.875	1.00	35.35	C
ATOM	69	CD	GLU	A	159	−33.213	−20.190	14.052	1.00	41.67	C
ATOM	70	OE1	GLU	A	159	−34.123	−19.392	13.733	1.00	44.61	O
ATOM	71	OE2	GLU	A	159	−33.441	−21.333	14.516	1.00	36.73	O
ATOM	72	N	HIS	A	160	−29.542	−17.432	12.977	1.00	25.27	N
ATOM	73	CA	HIS	A	160	−29.577	−16.257	12.118	1.00	31.03	C
ATOM	74	C	HIS	A	160	−29.525	−16.672	10.656	1.00	30.42	C
ATOM	75	O	HIS	A	160	−28.530	−17.261	10.205	1.00	26.33	O
ATOM	76	CB	HIS	A	160	−28.411	−15.317	12.426	1.00	29.99	C
ATOM	77	CG	HIS	A	160	−28.320	−14.150	11.493	1.00	28.06	C
ATOM	78	ND1	HIS	A	160	−29.043	−12.991	11.679	1.00	33.48	N
ATOM	79	CD2	HIS	A	160	−27.605	−13.970	10.359	1.00	29.69	C
ATOM	80	CE1	HIS	A	160	−28.770	−12.143	10.703	1.00	30.20	C
ATOM	81	NE2	HIS	A	160	−27.903	−12.713	9.887	1.00	29.37	N
ATOM	82	N	GLU	A	161	−30.593	−16.361	9.925	1.00	29.26	N
ATOM	83	CA	GLU	A	161	−30.696	−16.730	8.520	1.00	30.40	C
ATOM	84	C	GLU	A	161	−30.349	−18.188	8.278	1.00	30.86	C
ATOM	85	O	GLU	A	161	−29.548	−18.493	7.393	1.00	34.60	O
ATOM	86	CB	GLU	A	161	−29.788	−15.852	7.659	1.00	35.54	C
ATOM	87	CG	GLU	A	161	−30.197	−14.386	7.604	1.00	41.66	C
ATOM	88	CD	GLU	A	161	−31.526	−14.165	6.901	1.00	42.46	C
ATOM	89	OE1	GLU	A	161	−32.027	−15.108	6.252	1.00	47.99	O
ATOM	90	OE2	GLU	A	161	−32.070	−13.043	7.001	1.00	40.82	O
ATOM	91	N	ARG	A	162	−30.928	−19.068	9.092	1.00	24.36	N
ATOM	92	CA	ARG	A	162	−30.792	−20.516	8.931	1.00	31.86	C
ATOM	93	C	ARG	A	162	−29.374	−21.045	9.202	1.00	30.42	C
ATOM	94	O	ARG	A	162	−29.030	−22.166	8.814	1.00	31.05	O
ATOM	95	CB	ARG	A	162	−31.250	−20.930	7.528	1.00	38.14	C
ATOM	96	CG	ARG	A	162	−32.267	−22.051	7.540	1.00	48.13	C
ATOM	97	CD	ARG	A	162	−33.076	−22.071	6.261	1.00	59.39	C
ATOM	98	NE	ARG	A	162	−33.517	−23.423	5.921	1.00	73.66	N
ATOM	99	CZ	ARG	A	162	−34.365	−23.702	4.937	1.00	64.55	C
ATOM	100	NH1	ARG	A	162	−34.866	−22.720	4.200	1.00	53.99	N
ATOM	101	NH2	ARG	A	162	−34.711	−24.960	4.694	1.00	63.33	N
ATOM	102	N	SER	A	163	−28.556	−20.240	9.869	1.00	24.82	N
ATOM	103	CA	SER	A	163	−27.287	−20.728	10.379	1.00	27.06	C
ATOM	104	C	SER	A	163	−27.270	−20.611	11.897	1.00	28.98	C
ATOM	105	O	SER	A	163	−27.914	−19.730	12.474	1.00	28.00	O
ATOM	106	CB	SER	A	163	−26.110	−19.963	9.768	1.00	26.42	C
ATOM	107	OG	SER	A	163	−25.629	−20.605	8.596	1.00	27.29	O
ATOM	108	N	CYS	A	164	−26.548	−21.522	12.537	1.00	26.62	N
ATOM	109	CA	CYS	A	164	−26.342	−21.469	13.975	1.00	23.71	C
ATOM	110	C	CYS	A	164	−24.920	−20.996	14.249	1.00	23.70	C
ATOM	111	O	CYS	A	164	−23.980	−21.412	13.579	1.00	20.95	O
ATOM	112	CB	CYS	A	164	−26.591	−22.838	14.601	1.00	25.60	C
ATOM	113	SG	CYS	A	164	−28.228	−23.515	14.210	1.00	29.69	S
ATOM	114	N	TYR	A	165	−24.766	−20.116	15.227	1.00	23.47	N
ATOM	115	CA	TYR	A	165	−23.469	−19.539	15.507	1.00	21.97	C
ATOM	116	C	TYR	A	165	−23.139	−19.708	16.970	1.00	22.33	C
ATOM	117	O	TYR	A	165	−23.970	−19.473	17.835	1.00	21.92	O
ATOM	118	CB	TYR	A	165	−23.434	−18.055	15.141	1.00	17.23	C
ATOM	119	CG	TYR	A	165	−23.665	−17.761	13.679	1.00	18.76	C
ATOM	120	CD1	TYR	A	165	−24.949	−17.615	13.174	1.00	22.13	C
ATOM	121	CD2	TYR	A	165	−22.601	−17.602	12.813	1.00	21.90	C
ATOM	122	CE1	TYR	A	165	−25.169	−17.327	11.833	1.00	25.39	C
ATOM	123	CE2	TYR	A	165	−22.808	−17.317	11.470	1.00	23.30	C
ATOM	124	CZ	TYR	A	165	−24.096	−17.177	10.990	1.00	24.28	C
ATOM	125	OH	TYR	A	165	−24.295	−16.900	9.663	1.00	25.37	O
ATOM	126	N	TRP	A	166	−21.913	−20.111	17.243	1.00	17.81	N
ATOM	127	CA	TRP	A	166	−21.436	−20.129	18.601	1.00	20.06	C
ATOM	128	C	TRP	A	166	−20.213	−19.213	18.680	1.00	18.56	C
ATOM	129	O	TRP	A	166	−19.289	−19.307	17.870	1.00	18.84	O
ATOM	130	CB	TRP	A	166	−21.117	−21.554	19.040	1.00	18.95	C
ATOM	131	CG	TRP	A	166	−20.709	−21.665	20.486	1.00	22.40	C
ATOM	132	CD1	TRP	A	166	−21.533	−21.745	21.563	1.00	21.92	C
ATOM	133	CD2	TRP	A	166	−19.369	−21.697	21.001	1.00	22.78	C
ATOM	134	NE1	TRP	A	166	−20.797	−21.831	22.717	1.00	26.27	N
ATOM	135	CE2	TRP	A	166	−19.464	−21.805	22.400	1.00	22.51	C
ATOM	136	CE3	TRP	A	166	−18.098	−21.648	20.408	1.00	20.00	C
ATOM	137	CZ2	TRP	A	166	−18.343	−21.869	23.221	1.00	19.21	C
ATOM	138	CZ3	TRP	A	166	−16.989	−21.716	21.214	1.00	19.92	C
ATOM	139	CH2	TRP	A	166	−17.116	−21.820	22.616	1.00	20.77	C
ATOM	140	N	PHE	A	167	−20.233	−18.308	19.648	1.00	20.52	N
ATOM	141	CA	PHE	A	167	−19.189	−17.304	19.803	1.00	17.05	C
ATOM	142	C	PHE	A	167	−18.367	−17.589	21.039	1.00	23.11	C
ATOM	143	O	PHE	A	167	−18.847	−17.397	22.149	1.00	20.92	O
ATOM	144	CB	PHE	A	167	−19.794	−15.905	19.894	1.00	17.09	C
ATOM	145	CG	PHE	A	167	−20.649	−15.533	18.712	1.00	19.67	C
ATOM	146	CD1	PHE	A	167	−22.012	−15.806	18.710	1.00	20.06	C
ATOM	147	CD2	PHE	A	167	−20.087	−14.907	17.598	1.00	18.66	C
ATOM	148	CE1	PHE	A	167	−22.807	−15.457	17.615	1.00	21.81	C
ATOM	149	CE2	PHE	A	167	−20.860	−14.555	16.501	1.00	14.19	C
ATOM	150	CZ	PHE	A	167	−22.230	−14.836	16.502	1.00	20.28	C
ATOM	151	N	SER	A	168	−17.127	−18.039	20.853	1.00	20.07	N
ATOM	152	CA	SER	A	168	−16.296	−18.360	22.000	1.00	19.88	C
ATOM	153	C	SER	A	168	−16.073	−17.121	22.847	1.00	23.65	C
ATOM	154	O	SER	A	168	−16.105	−15.992	22.331	1.00	22.61	O
ATOM	155	CB	SER	A	168	−14.950	−18.952	21.570	1.00	13.34	C
ATOM	156	OG	SER	A	168	−14.018	−17.940	21.262	1.00	16.40	O
ATOM	157	N	ARG	A	169	−15.877	−17.339	24.149	1.00	18.01	N
ATOM	158	CA	ARG	A	169	−15.443	−16.284	25.038	1.00	22.03	C
ATOM	159	C	ARG	A	169	−14.033	−16.614	25.568	1.00	21.36	C
ATOM	160	O	ARG	A	169	−13.617	−16.124	26.615	1.00	24.92	O
ATOM	161	CB	ARG	A	169	−16.447	−16.082	26.182	1.00	26.09	C
ATOM	162	CG	ARG	A	169	−17.858	−15.584	25.733	1.00	33.24	C
ATOM	163	CD	ARG	A	169	−17.799	−14.586	24.532	1.00	35.48	C
ATOM	164	NE	ARG	A	169	−19.120	−14.199	24.007	1.00	41.60	N
ATOM	165	CZ	ARG	A	169	−19.315	−13.401	22.953	1.00	38.23	C
ATOM	166	NH1	ARG	A	169	−18.279	−12.905	22.281	1.00	28.72	N
ATOM	167	NH2	ARG	A	169	−20.550	−13.100	22.559	1.00	36.96	N
ATOM	168	N	SER	A	170	−13.303	−17.438	24.823	1.00	16.23	N
ATOM	169	CA	SER	A	170	−11.877	−17.660	25.065	1.00	16.00	C
ATOM	170	C	SER	A	170	−11.094	−17.698	23.742	1.00	17.67	C
ATOM	171	O	SER	A	170	−11.662	−17.537	22.663	1.00	16.96	O
ATOM	172	CB	SER	A	170	−11.652	−18.958	25.851	1.00	17.57	C
ATOM	173	OG	SER	A	170	−12.101	−20.084	25.121	1.00	18.85	O
ATOM	174	N	GLY	A	171	−9.783	−17.916	23.824	1.00	19.23	N
ATOM	175	CA	GLY	A	171	−8.947	−17.854	22.645	1.00	12.77	C
ATOM	176	C	GLY	A	171	−8.169	−19.115	22.334	1.00	16.65	C
ATOM	177	O	GLY	A	171	−7.701	−19.820	23.236	1.00	16.99	O
ATOM	178	N	LYS	A	172	−8.037	−19.389	21.039	1.00	15.85	N
ATOM	179	CA	LYS	A	172	−7.313	−20.542	20.533	1.00	13.77	C
ATOM	180	C	LYS	A	172	−6.509	−20.164	19.309	1.00	17.02	C
ATOM	181	O	LYS	A	172	−6.873	−19.224	18.576	1.00	17.20	O
ATOM	182	CB	LYS	A	172	−8.262	−21.678	20.148	1.00	16.06	C
ATOM	183	CG	LYS	A	172	−8.818	−22.506	21.281	1.00	17.04	C
ATOM	184	CD	LYS	A	172	−9.638	−23.666	20.687	1.00	17.13	C
ATOM	185	CE	LYS	A	172	−10.400	−24.441	21.766	1.00	16.06	C
ATOM	186	NZ	LYS	A	172	−9.439	−25.070	22.711	1.00	20.45	N
ATOM	187	N	ALA	A	173	−5.427	−20.902	19.074	1.00	13.08	N
ATOM	188	CA	ALA	A	173	−4.750	−20.834	17.792	1.00	14.02	C
ATOM	189	C	ALA	A	173	−5.758	−21.289	16.754	1.00	16.04	C
ATOM	190	O	ALA	A	173	−6.675	−22.056	17.064	1.00	15.29	O
ATOM	191	CB	ALA	A	173	−3.482	−21.720	17.766	1.00	14.17	C
ATOM	192	N	TRP	A	174	−5.591	−20.827	15.522	1.00	16.89	N
ATOM	193	CA	TRP	A	174	−6.571	−21.098	14.492	1.00	15.29	C
ATOM	194	C	TRP	A	174	−6.839	−22.598	14.329	1.00	17.24	C
ATOM	195	O	TRP	A	174	−8.000	−23.030	14.334	1.00	17.21	O
ATOM	196	CB	TRP	A	174	−6.111	−20.486	13.185	1.00	15.83	C
ATOM	197	CG	TRP	A	174	−7.133	−20.523	12.123	1.00	17.80	C
ATOM	198	CD1	TRP	A	174	−8.015	−19.532	11.795	1.00	14.69	C
ATOM	199	CD2	TRP	A	174	−7.375	−21.598	11.217	1.00	17.89	C
ATOM	200	NE1	TRP	A	174	−8.784	−19.926	10.732	1.00	13.89	N
ATOM	201	CE2	TRP	A	174	−8.416	−21.193	10.361	1.00	17.17	C
ATOM	202	CE3	TRP	A	174	−6.803	−22.865	11.036	1.00	20.13	C
ATOM	203	CZ2	TRP	A	174	−8.911	−22.013	9.353	1.00	17.46	C
ATOM	204	CZ3	TRP	A	174	−7.294	−23.675	10.039	1.00	18.74	C
ATOM	205	CH2	TRP	A	174	−8.338	−23.246	9.208	1.00	21.31	C
ATOM	206	N	ALA	A	175	−5.781	−23.395	14.229	1.00	14.70	N
ATOM	207	CA	ALA	A	175	−5.950	−24.829	13.999	1.00	16.88	C
ATOM	208	C	ALA	A	175	−6.707	−25.488	15.138	1.00	18.55	C
ATOM	209	O	ALA	A	175	−7.444	−26.448	14.921	1.00	18.63	O
ATOM	210	CB	ALA	A	175	−4.595	−25.512	13.803	1.00	20.43	C
ATOM	211	N	ASP	A	176	−6.530	−24.982	16.355	1.00	15.66	N
ATOM	212	CA	ASP	A	176	−7.267	−25.535	17.479	1.00	14.07	C
ATOM	213	C	ASP	A	176	−8.717	−25.047	17.471	1.00	17.62	C
ATOM	214	O	ASP	A	176	−9.621	−25.790	17.834	1.00	19.92	O
ATOM	215	CB	ASP	A	176	−6.566	−25.191	18.784	1.00	17.82	C
ATOM	216	CG	ASP	A	176	−5.169	−25.805	18.865	1.00	32.45	C
ATOM	217	OD2	ASP	A	176	−4.231	−25.127	19.349	1.00	29.94	O
ATOM	218	OD1	ASP	A	176	−5.003	−26.959	18.405	1.00	34.43	O
ATOM	219	N	ALA	A	177	−8.951	−23.811	17.036	1.00	15.88	N
ATOM	220	CA	ALA	A	177	−10.324	−23.342	16.867	1.00	15.36	C
ATOM	221	C	ALA	A	177	−11.000	−24.134	15.765	1.00	14.26	C
ATOM	222	O	ALA	A	177	−12.176	−24.472	15.856	1.00	17.76	O
ATOM	223	CB	ALA	A	177	−10.355	−21.866	16.550	1.00	12.43	C
ATOM	224	N	ASP	A	178	−10.250	−24.417	14.710	1.00	17.91	N
ATOM	225	CA	ASP	A	178	−10.776	−25.168	13.575	1.00	18.45	C
ATOM	226	C	ASP	A	178	−11.241	−26.540	14.045	1.00	20.72	C
ATOM	227	O	ASP	A	178	−12.390	−26.930	13.819	1.00	17.75	O
ATOM	228	CB	ASP	A	178	−9.714	−25.301	12.493	1.00	18.31	C
ATOM	229	CG	ASP	A	178	−10.161	−26.169	11.346	1.00	24.63	C
ATOM	230	OD1	ASP	A	178	−11.279	−25.949	10.829	1.00	26.01	O
ATOM	231	OD2	ASP	A	178	−9.388	−27.067	10.960	1.00	28.35	O
ATOM	232	N	ASN	A	179	−10.343	−27.251	14.729	1.00	18.35	N
ATOM	233	CA	ASN	A	179	−10.668	−28.541	15.329	1.00	20.73	C
ATOM	234	C	ASN	A	179	−11.839	−28.466	16.310	1.00	21.76	C
ATOM	235	O	ASN	A	179	−12.689	−29.359	16.343	1.00	22.85	O
ATOM	236	CB	ASN	A	179	−9.443	−29.130	16.037	1.00	19.26	C
ATOM	237	CG	ASN	A	179	−9.756	−30.435	16.752	1.00	24.98	C
ATOM	238	OD1	ASN	A	179	−9.955	−30.455	17.961	1.00	27.04	O
ATOM	239	ND2	ASN	A	179	−9.814	−31.528	16.002	1.00	24.23	N
ATOM	240	N	TYR	A	180	−11.897	−27.407	17.110	1.00	17.86	N
ATOM	241	CA	TYR	A	180	−13.001	−27.265	18.054	1.00	16.79	C
ATOM	242	C	TYR	A	180	−14.342	−27.266	17.313	1.00	19.82	C
ATOM	243	O	TYR	A	180	−15.287	−27.948	17.709	1.00	19.73	O
ATOM	244	CB	TYR	A	180	−12.861	−25.985	18.891	1.00	16.59	C
ATOM	245	CG	TYR	A	180	−14.056	−25.719	19.810	1.00	19.48	C
ATOM	246	CD2	TYR	A	180	−13.996	−26.024	21.162	1.00	24.26	C
ATOM	247	CD1	TYR	A	180	−15.245	−25.156	19.316	1.00	18.40	C
ATOM	248	CE2	TYR	A	180	−15.089	−25.789	22.008	1.00	20.67	C
ATOM	249	CE1	TYR	A	180	−16.328	−24.922	20.135	1.00	16.82	C
ATOM	250	CZ	TYR	A	180	−16.243	−25.239	21.483	1.00	23.60	C
ATOM	251	OH	TYR	A	180	−17.312	−25.009	22.311	1.00	27.99	O
ATOM	252	N	CYS	A	181	−14.416	−26.480	16.247	1.00	21.68	N
ATOM	253	CA	CYS	A	181	−15.634	−26.361	15.468	1.00	21.18	C
ATOM	254	C	CYS	A	181	−16.005	−27.691	14.816	1.00	22.39	C
ATOM	255	O	CYS	A	181	−17.173	−28.054	14.738	1.00	17.23	O
ATOM	256	CB	CYS	A	181	−15.479	−25.268	14.414	1.00	17.00	C
ATOM	257	SG	CYS	A	181	−15.347	−23.612	15.108	1.00	21.92	S
ATOM	258	N	ARG	A	182	−15.008	−28.435	14.366	1.00	22.70	N
ATOM	259	CA	ARG	A	182	−15.309	−29.699	13.720	1.00	25.40	C
ATOM	260	C	ARG	A	182	−15.881	−30.687	14.737	1.00	22.32	C
ATOM	261	O	ARG	A	182	−16.756	−31.489	14.417	1.00	21.62	O
ATOM	262	CB	ARG	A	182	−14.064	−30.255	13.031	1.00	22.43	C
ATOM	263	CG	ARG	A	182	−13.757	−29.535	11.727	1.00	27.35	C
ATOM	264	CD	ARG	A	182	−12.390	−29.887	11.188	1.00	27.56	C
ATOM	265	NE	ARG	A	182	−11.981	−28.956	10.139	1.00	34.68	N
ATOM	266	CZ	ARG	A	182	−12.311	−29.080	8.851	1.00	37.24	C
ATOM	267	NH1	ARG	A	182	−13.062	−30.100	8.446	1.00	30.09	N
ATOM	268	NH2	ARG	A	182	−11.900	−28.176	7.966	1.00	33.00	N
ATOM	269	N	LEU	A	183	−15.415	−30.609	15.975	1.00	22.21	N
ATOM	270	CA	LEU	A	183	−15.858	−31.565	16.980	1.00	20.10	C
ATOM	271	C	LEU	A	183	−17.289	−31.265	17.408	1.00	22.94	C
ATOM	272	O	LEU	A	183	−17.907	−32.076	18.096	1.00	23.53	O
ATOM	273	CB	LEU	A	183	−14.918	−31.577	18.182	1.00	19.03	C
ATOM	274	CG	LEU	A	183	−13.826	−32.651	18.153	1.00	24.47	C
ATOM	275	CD1	LEU	A	183	−13.119	−32.696	16.809	1.00	24.47	C
ATOM	276	CD2	LEU	A	183	−12.816	−32.407	19.258	1.00	24.08	C
ATOM	277	N	GLU	A	184	−17.809	−30.113	16.977	1.00	23.63	N
ATOM	278	CA	GLU	A	184	−19.222	−29.762	17.156	1.00	23.88	C
ATOM	279	C	GLU	A	184	−20.075	−29.971	15.910	1.00	22.40	C
ATOM	280	O	GLU	A	184	−21.110	−29.330	15.791	1.00	22.93	O
ATOM	281	CB	GLU	A	184	−19.372	−28.292	17.560	1.00	23.75	C
ATOM	282	CG	GLU	A	184	−18.635	−27.890	18.806	1.00	26.06	C
ATOM	283	CD	GLU	A	184	−19.139	−28.631	20.019	1.00	33.11	C
ATOM	284	OE1	GLU	A	184	−20.363	−28.913	20.075	1.00	34.32	O
ATOM	285	OE2	GLU	A	184	−18.305	−28.946	20.899	1.00	34.75	O
ATOM	286	N	ASP	A	185	−19.651	−30.834	14.989	1.00	21.89	N
ATOM	287	CA	ASP	A	185	−20.270	−30.908	13.664	1.00	25.50	C
ATOM	288	C	ASP	A	185	−20.452	−29.523	13.066	1.00	22.06	C
ATOM	289	O	ASP	A	185	−21.511	−29.206	12.547	1.00	21.39	O
ATOM	290	CB	ASP	A	185	−21.637	−31.606	13.701	1.00	40.42	C
ATOM	291	CG	ASP	A	185	−21.531	−33.104	13.910	1.00	51.64	C
ATOM	292	OD1	ASP	A	185	−20.401	−33.647	13.831	1.00	55.89	O
ATOM	293	OD2	ASP	A	185	−22.589	−33.745	14.116	1.00	52.07	O
ATOM	294	N	ALA	A	186	−19.419	−28.693	13.152	1.00	25.31	N
ATOM	295	CA	ALA	A	186	−19.521	−27.315	12.702	1.00	21.25	C
ATOM	296	C	ALA	A	186	−18.262	−26.920	11.989	1.00	18.66	C
ATOM	297	O	ALA	A	186	−17.353	−27.723	11.805	1.00	20.79	O
ATOM	298	CB	ALA	A	186	−19.779	−26.377	13.882	1.00	18.33	C
ATOM	299	N	HIS	A	187	−18.199	−25.658	11.603	1.00	18.96	N
ATOM	300	CA	HIS	A	187	−17.012	−25.135	10.969	1.00	17.14	C
ATOM	301	C	HIS	A	187	−16.810	−23.710	11.439	1.00	17.01	C
ATOM	302	O	HIS	A	187	−17.776	−23.033	11.778	1.00	19.70	O
ATOM	303	CB	HIS	A	187	−17.156	−25.191	9.450	1.00	15.59	C
ATOM	304	CG	HIS	A	187	−18.323	−24.414	8.940	1.00	15.47	C
ATOM	305	ND1	HIS	A	187	−18.281	−23.048	8.761	1.00	15.92	N
ATOM	306	CD2	HIS	A	187	−19.578	−24.800	8.606	1.00	18.70	C
ATOM	307	CE1	HIS	A	187	−19.456	−22.628	8.323	1.00	18.66	C
ATOM	308	NE2	HIS	A	187	−20.261	−23.671	8.223	1.00	21.90	N
ATOM	309	N	LEU	A	188	−15.560	−23.264	11.480	1.00	16.40	N
ATOM	310	CA	LEU	A	188	−15.256	−21.859	11.698	1.00	14.33	C
ATOM	311	C	LEU	A	188	−16.058	−20.996	10.738	1.00	16.82	C
ATOM	312	O	LEU	A	188	−16.141	−21.289	9.527	1.00	15.26	O
ATOM	313	CB	LEU	A	188	−13.761	−21.602	11.512	1.00	13.49	C
ATOM	314	CG	LEU	A	188	−12.853	−21.922	12.696	1.00	16.50	C
ATOM	315	CD1	LEU	A	188	−11.390	−21.816	12.290	1.00	18.24	C
ATOM	316	CD2	LEU	A	188	−13.163	−20.975	13.841	1.00	15.22	C
ATOM	317	N	VAL	A	189	−16.613	−19.915	11.271	1.00	15.19	N
ATOM	318	CA	VAL	A	189	−17.596	−19.127	10.543	1.00	13.95	C
ATOM	319	C	VAL	A	189	−17.130	−18.784	9.129	1.00	14.59	C
ATOM	320	O	VAL	A	189	−15.970	−18.432	8.894	1.00	13.02	O
ATOM	321	CB	VAL	A	189	−17.957	−17.836	11.316	1.00	15.19	C
ATOM	322	CG1	VAL	A	189	−16.788	−16.866	11.361	1.00	13.58	C
ATOM	323	CG2	VAL	A	189	−19.191	−17.168	10.700	1.00	19.68	C
ATOM	324	N	VAL	A	190	−18.041	−18.966	8.183	1.00	16.77	N
ATOM	325	CA	VAL	A	190	−17.814	−18.617	6.786	1.00	18.83	C
ATOM	326	C	VAL	A	190	−18.720	−17.429	6.469	1.00	18.58	C
ATOM	327	O	VAL	A	190	−19.925	−17.526	6.604	1.00	17.97	O
ATOM	328	CB	VAL	A	190	−18.113	−19.808	5.843	1.00	19.02	C
ATOM	329	CG1	VAL	A	190	−18.145	−19.357	4.367	1.00	16.14	C
ATOM	330	CG2	VAL	A	190	−17.092	−20.917	6.052	1.00	17.67	C
ATOM	331	N	VAL	A	191	−18.146	−16.297	6.086	1.00	16.96	N
ATOM	332	CA	VAL	A	191	−18.956	−15.094	5.909	1.00	16.61	C
ATOM	333	C	VAL	A	191	−19.163	−14.813	4.424	1.00	21.27	C
ATOM	334	O	VAL	A	191	−18.196	−14.541	3.705	1.00	19.05	O
ATOM	335	CB	VAL	A	191	−18.302	−13.887	6.589	1.00	19.68	C
ATOM	336	CG1	VAL	A	191	−19.161	−12.637	6.414	1.00	16.81	C
ATOM	337	CG2	VAL	A	191	−18.073	−14.187	8.076	1.00	17.57	C
ATOM	338	N	THR	A	192	−20.410	−14.895	3.960	1.00	17.29	N
ATOM	339	CA	THR	A	192	−20.686	−14.767	2.523	1.00	21.54	C
ATOM	340	C	THR	A	192	−21.558	−13.571	2.143	1.00	21.36	C
ATOM	341	O	THR	A	192	−21.854	−13.372	0.976	1.00	21.17	O
ATOM	342	CB	THR	A	192	−21.344	−16.046	1.963	1.00	19.51	C
ATOM	343	OG1	THR	A	192	−22.486	−16.392	2.755	1.00	23.52	O
ATOM	344	CG2	THR	A	192	−20.354	−17.193	2.007	1.00	19.60	C
ATOM	345	N	SER	A	193	−21.938	−12.744	3.107	1.00	18.59	N
ATOM	346	CA	SER	A	193	−22.678	−11.549	2.755	1.00	21.89	C
ATOM	347	C	SER	A	193	−22.432	−10.451	3.763	1.00	26.64	C
ATOM	348	O	SER	A	193	−21.913	−10.693	4.856	1.00	19.28	O
ATOM	349	CB	SER	A	193	−24.172	−11.847	2.681	1.00	23.78	C
ATOM	350	OG	SER	A	193	−24.655	−12.141	3.986	1.00	23.32	O
ATOM	351	N	TRP	A	194	−22.825	−9.241	3.378	1.00	27.24	N
ATOM	352	CA	TRP	A	194	−22.794	−8.087	4.260	1.00	24.77	C
ATOM	353	C	TRP	A	194	−23.633	−8.331	5.504	1.00	25.57	C
ATOM	354	O	TRP	A	194	−23.199	−8.061	6.624	1.00	26.59	O
ATOM	355	CB	TRP	A	194	−23.295	−6.845	3.519	1.00	28.68	C
ATOM	356	CG	TRP	A	194	−23.125	−5.572	4.283	1.00	38.36	C
ATOM	357	CD1	TRP	A	194	−24.116	−4.747	4.741	1.00	37.90	C
ATOM	358	CD2	TRP	A	194	−21.884	−4.976	4.696	1.00	44.56	C
ATOM	359	NE1	TRP	A	194	−23.569	−3.668	5.400	1.00	43.45	N
ATOM	360	CE2	TRP	A	194	−22.202	−3.785	5.388	1.00	46.98	C
ATOM	361	CE3	TRP	A	194	−20.538	−5.334	4.546	1.00	36.22	C
ATOM	362	CZ2	TRP	A	194	−21.219	−2.949	5.932	1.00	52.52	C
ATOM	363	CZ3	TRP	A	194	−19.560	−4.503	5.089	1.00	42.44	C
ATOM	364	CH2	TRP	A	194	−19.908	−3.325	5.773	1.00	54.05	C
ATOM	365	N	GLU	A	195	−24.848	−8.824	5.293	1.00	26.92	N
ATOM	366	CA	GLU	A	195	−25.764	−9.112	6.385	1.00	23.47	C
ATOM	367	C	GLU	A	195	−25.105	−9.996	7.433	1.00	23.12	C
ATOM	368	O	GLU	A	195	−25.175	−9.715	8.632	1.00	28.18	O
ATOM	369	CB	GLU	A	195	−27.037	−9.781	5.846	1.00	30.26	C
ATOM	370	CG	GLU	A	195	−27.820	−10.627	6.876	1.00	40.78	C
ATOM	371	CD	GLU	A	195	−27.676	−12.144	6.673	1.00	40.62	C
ATOM	372	OE1	GLU	A	195	−27.945	−12.645	5.559	1.00	43.62	O
ATOM	373	OE2	GLU	A	195	−27.294	−12.841	7.634	1.00	42.10	O
ATOM	374	N	GLU	A	196	−24.454	−11.059	6.975	1.00	20.16	N
ATOM	375	CA	GLU	A	196	−23.824	−12.005	7.884	1.00	25.02	C
ATOM	376	C	GLU	A	196	−22.610	−11.407	8.600	1.00	21.89	C
ATOM	377	O	GLU	A	196	−22.377	−11.689	9.775	1.00	18.44	O
ATOM	378	CB	GLU	A	196	−23.416	−13.265	7.136	1.00	20.96	C
ATOM	379	CG	GLU	A	196	−22.822	−14.312	8.049	1.00	22.24	C
ATOM	380	CD	GLU	A	196	−22.589	−15.613	7.337	1.00	22.15	C
ATOM	381	OE1	GLU	A	196	−22.492	−15.604	6.093	1.00	19.92	O
ATOM	382	OE2	GLU	A	196	−22.506	−16.645	8.028	1.00	24.74	O
ATOM	383	N	GLN	A	197	−21.851	−10.584	7.881	1.00	18.28	N
ATOM	384	CA	GLN	A	197	−20.751	−9.817	8.456	1.00	18.47	C
ATOM	385	C	GLN	A	197	−21.217	−8.914	9.600	1.00	24.91	C
ATOM	386	O	GLN	A	197	−20.639	−8.924	10.694	1.00	18.25	O
ATOM	387	CB	GLN	A	197	−20.084	−8.973	7.373	1.00	18.68	C
ATOM	388	CG	GLN	A	197	−19.167	−7.888	7.890	1.00	23.19	C
ATOM	389	CD	GLN	A	197	−17.832	−8.428	8.348	1.00	19.88	C
ATOM	390	OE1	GLN	A	197	−17.290	−9.361	7.758	1.00	19.94	O
ATOM	391	NE2	GLN	A	197	−17.289	−7.840	9.406	1.00	20.73	N
ATOM	392	N	LYS	A	198	−22.253	−8.118	9.334	1.00	26.27	N
ATOM	393	CA	LYS	A	198	−22.775	−7.197	10.330	1.00	20.44	C
ATOM	394	C	LYS	A	198	−23.308	−7.995	11.495	1.00	18.19	C
ATOM	395	O	LYS	A	198	−23.199	−7.578	12.637	1.00	20.09	O
ATOM	396	CB	LYS	A	198	−23.886	−6.312	9.757	1.00	26.97	C
ATOM	397	CG	LYS	A	198	−23.441	−5.226	8.806	1.00	32.65	C
ATOM	398	CD	LYS	A	198	−24.652	−4.387	8.368	1.00	47.94	C
ATOM	399	CE	LYS	A	198	−25.404	−3.782	9.568	1.00	44.86	C
ATOM	400	NZ	LYS	A	198	−26.475	−2.822	9.154	1.00	46.87	N
ATOM	401	N	PHE	A	199	−23.903	−9.142	11.196	1.00	16.78	N
ATOM	402	CA	PHE	A	199	−24.438	−9.981	12.248	1.00	18.71	C
ATOM	403	C	PHE	A	199	−23.319	−10.480	13.161	1.00	19.39	C
ATOM	404	O	PHE	A	199	−23.448	−10.481	14.383	1.00	19.46	O
ATOM	405	CB	PHE	A	199	−25.204	−11.163	11.669	1.00	15.44	C
ATOM	406	CG	PHE	A	199	−25.498	−12.218	12.675	1.00	18.84	C
ATOM	407	CD2	PHE	A	199	−24.739	−13.374	12.732	1.00	22.90	C
ATOM	408	CD1	PHE	A	199	−26.510	−12.045	13.596	1.00	23.16	C
ATOM	409	CE2	PHE	A	199	−24.998	−14.339	13.686	1.00	25.42	C
ATOM	410	CE1	PHE	A	199	−26.775	−13.011	14.557	1.00	24.25	C
ATOM	411	CZ	PHE	A	199	−26.023	−14.155	14.603	1.00	20.45	C
ATOM	412	N	VAL	A	200	−22.220	−10.923	12.568	1.00	20.88	N
ATOM	413	CA	VAL	A	200	−21.127	−11.461	13.366	1.00	19.97	C
ATOM	414	C	VAL	A	200	−20.361	−10.342	14.096	1.00	19.76	C
ATOM	415	O	VAL	A	200	−20.037	−10.494	15.267	1.00	18.57	O
ATOM	416	CB	VAL	A	200	−20.201	−12.301	12.496	1.00	20.92	C
ATOM	417	CG1	VAL	A	200	−18.898	−12.658	13.243	1.00	18.59	C
ATOM	418	CG2	VAL	A	200	−20.942	−13.551	12.046	1.00	16.54	C
ATOM	419	N	GLN	A	201	−20.126	−9.211	13.430	1.00	19.23	N
ATOM	420	CA	GLN	A	201	−19.564	−8.024	14.096	1.00	22.96	C
ATOM	421	C	GLN	A	201	−20.288	−7.714	15.403	1.00	25.56	C
ATOM	422	O	GLN	A	201	−19.649	−7.493	16.437	1.00	22.68	O
ATOM	423	CB	GLN	A	201	−19.648	−6.781	13.199	1.00	23.94	C
ATOM	424	CG	GLN	A	201	−18.493	−6.549	12.235	1.00	24.31	C
ATOM	425	CD	GLN	A	201	−18.865	−5.570	11.096	1.00	31.70	C
ATOM	426	OE1	GLN	A	201	−18.274	−5.595	10.007	1.00	25.36	O
ATOM	427	NE2	GLN	A	201	−19.856	−4.718	11.349	1.00	28.05	N
ATOM	428	N	HIS	A	202	−21.625	−7.687	15.349	1.00	19.95	N
ATOM	429	CA	HIS	A	202	−22.415	−7.330	16.514	1.00	20.60	C
ATOM	430	C	HIS	A	202	−22.126	−8.228	17.715	1.00	23.45	C
ATOM	431	O	HIS	A	202	−21.915	−7.742	18.822	1.00	26.55	O
ATOM	432	CB	HIS	A	202	−23.906	−7.382	16.207	1.00	22.12	C
ATOM	433	CG	HIS	A	202	−24.758	−7.236	17.425	1.00	21.72	C
ATOM	434	ND1	HIS	A	202	−25.123	−6.010	17.931	1.00	25.57	N
ATOM	435	CD2	HIS	A	202	−25.276	−8.160	18.267	1.00	25.38	C
ATOM	436	CE1	HIS	A	202	−25.846	−6.183	19.022	1.00	23.46	C
ATOM	437	NE2	HIS	A	202	−25.958	−7.481	19.244	1.00	23.52	N
ATOM	438	N	HIS	A	203	−22.128	−9.537	17.495	1.00	22.74	N
ATOM	439	CA	HIS	A	203	−21.920	−10.478	18.584	1.00	21.81	C
ATOM	440	C	HIS	A	203	−20.469	−10.633	19.043	1.00	21.12	C
ATOM	441	O	HIS	A	203	−20.243	−11.066	20.168	1.00	31.14	O
ATOM	442	CB	HIS	A	203	−22.455	−11.849	18.201	1.00	19.70	C
ATOM	443	CG	HIS	A	203	−23.947	−11.937	18.209	1.00	27.48	C
ATOM	444	ND1	HIS	A	203	−24.669	−12.220	19.349	1.00	27.80	N
ATOM	445	CD2	HIS	A	203	−24.855	−11.767	17.220	1.00	22.28	C
ATOM	446	CE1	HIS	A	203	−25.958	−12.223	19.061	1.00	21.84	C
ATOM	447	NE2	HIS	A	203	−26.097	−11.945	17.777	1.00	20.85	N
ATOM	448	N	ILE	A	204	−19.487	−10.319	18.206	1.00	19.01	N
ATOM	449	CA	ILE	A	204	−18.102	−10.491	18.664	1.00	24.65	C
ATOM	450	C	ILE	A	204	−17.506	−9.213	19.247	1.00	23.37	C
ATOM	451	O	ILE	A	204	−16.502	−9.262	19.956	1.00	29.46	O
ATOM	452	CB	ILE	A	204	−17.156	−10.992	17.550	1.00	19.60	C
ATOM	453	CG1	ILE	A	204	−17.032	−9.970	16.421	1.00	22.94	C
ATOM	454	CG2	ILE	A	204	−17.581	−12.351	17.037	1.00	18.69	C
ATOM	455	CD1	ILE	A	204	−15.981	−10.357	15.400	1.00	18.85	C
ATOM	456	N	GLY	A	205	−18.118	−8.075	18.954	1.00	21.26	N
ATOM	457	CA	GLY	A	205	−17.663	−6.811	19.504	1.00	22.73	C
ATOM	458	C	GLY	A	205	−16.273	−6.438	19.025	1.00	24.53	C
ATOM	459	O	GLY	A	205	−15.782	−6.990	18.041	1.00	29.29	O
ATOM	460	N	PRO	A	206	−15.614	−5.508	19.729	1.00	27.53	N
ATOM	461	CA	PRO	A	206	−14.313	−5.000	19.264	1.00	25.17	C
ATOM	462	C	PRO	A	206	−13.141	−5.982	19.496	1.00	23.26	C
ATOM	463	O	PRO	A	206	−12.078	−5.584	19.979	1.00	27.76	O
ATOM	464	CB	PRO	A	206	−14.137	−3.729	20.092	1.00	24.03	C
ATOM	465	CG	PRO	A	206	−14.809	−4.066	21.394	1.00	21.52	C
ATOM	466	CD	PRO	A	206	−16.016	−4.911	21.018	1.00	22.26	C
ATOM	467	N	VAL	A	207	−13.325	−7.240	19.114	1.00	21.78	N
ATOM	468	CA	VAL	A	207	−12.381	−8.298	19.464	1.00	22.06	C
ATOM	469	C	VAL	A	207	−11.844	−9.063	18.248	1.00	21.75	C
ATOM	470	O	VAL	A	207	−12.602	−9.464	17.361	1.00	16.31	O
ATOM	471	CB	VAL	A	207	−13.044	−9.308	20.425	1.00	18.92	C
ATOM	472	CG1	VAL	A	207	−12.057	−10.360	20.865	1.00	16.73	C
ATOM	473	CG2	VAL	A	207	−13.637	−8.587	21.612	1.00	15.45	C
ATOM	474	N	ASN	A	208	−10.532	−9.277	18.220	1.00	20.49	N
ATOM	475	CA	ASN	A	208	−9.922	−10.105	17.191	1.00	18.16	C
ATOM	476	C	ASN	A	208	−10.499	−11.507	17.256	1.00	15.84	C
ATOM	477	O	ASN	A	208	−10.423	−12.147	18.294	1.00	16.63	O
ATOM	478	CB	ASN	A	208	−8.413	−10.156	17.367	1.00	16.49	C
ATOM	479	CG	ASN	A	208	−7.741	−8.839	17.055	1.00	18.40	C
ATOM	480	OD1	ASN	A	208	−6.915	−8.354	17.828	1.00	21.56	O
ATOM	481	ND2	ASN	A	208	−8.067	−8.269	15.912	1.00	15.53	N
ATOM	482	N	THR	A	209	−11.073	−11.982	16.157	1.00	14.76	N
ATOM	483	CA	THR	A	209	−11.804	−13.251	16.157	1.00	13.30	C
ATOM	484	C	THR	A	209	−11.524	−14.065	14.892	1.00	14.80	C
ATOM	485	O	THR	A	209	−11.708	−13.581	13.778	1.00	13.11	O
ATOM	486	CB	THR	A	209	−13.330	−13.001	16.288	1.00	15.05	C
ATOM	487	OG1	THR	A	209	−13.573	−12.186	17.436	1.00	17.23	O
ATOM	488	CG2	THR	A	209	−14.102	−14.310	16.450	1.00	12.52	C
ATOM	489	N	TRP	A	210	−11.075	−15.300	15.058	1.00	12.28	N
ATOM	490	CA	TRP	A	210	−10.804	−16.146	13.905	1.00	13.62	C
ATOM	491	C	TRP	A	210	−12.057	−16.440	13.089	1.00	15.28	C
ATOM	492	O	TRP	A	210	−13.124	−16.679	13.649	1.00	14.02	O
ATOM	493	CB	TRP	A	210	−10.197	−17.482	14.330	1.00	13.45	C
ATOM	494	CG	TRP	A	210	−8.783	−17.472	14.852	1.00	12.79	C
ATOM	495	CD1	TRP	A	210	−8.352	−18.038	16.003	1.00	14.29	C
ATOM	496	CD2	TRP	A	210	−7.619	−16.907	14.223	1.00	12.57	C
ATOM	497	NE1	TRP	A	210	−6.992	−17.868	16.141	1.00	14.57	N
ATOM	498	CE2	TRP	A	210	−6.521	−17.177	15.057	1.00	12.81	C
ATOM	499	CE3	TRP	A	210	−7.401	−16.202	13.033	1.00	13.91	C
ATOM	500	CZ2	TRP	A	210	−5.225	−16.755	14.754	1.00	15.48	C
ATOM	501	CZ3	TRP	A	210	−6.107	−15.791	12.729	1.00	15.74	C
ATOM	502	CH2	TRP	A	210	−5.038	−16.076	13.582	1.00	14.80	C
ATOM	503	N	MET	A	211	−11.917	−16.443	11.763	1.00	14.46	N
ATOM	504	CA	MET	A	211	−12.972	−16.939	10.897	1.00	13.94	C
ATOM	505	C	MET	A	211	−12.389	−18.101	10.107	1.00	18.15	C
ATOM	506	O	MET	A	211	−11.183	−18.368	10.203	1.00	14.39	O
ATOM	507	CB	MET	A	211	−13.511	−15.843	9.973	1.00	14.29	C
ATOM	508	CG	MET	A	211	−12.639	−15.552	8.758	1.00	15.21	C
ATOM	509	SD	MET	A	211	−13.121	−14.063	7.849	1.00	15.99	S
ATOM	510	CE	MET	A	211	−12.617	−12.803	9.002	1.00	13.06	C
ATOM	511	N	GLY	A	212	−13.234	−18.800	9.348	1.00	16.19	N
ATOM	512	CA	GLY	A	212	−12.811	−20.001	8.645	1.00	14.73	C
ATOM	513	C	GLY	A	212	−12.179	−19.746	7.292	1.00	14.61	C
ATOM	514	O	GLY	A	212	−12.524	−20.367	6.306	1.00	14.25	O
ATOM	515	N	LEU	A	213	−11.231	−18.824	7.260	1.00	15.62	N
ATOM	516	CA	LEU	A	213	−10.589	−18.426	6.023	1.00	13.96	C
ATOM	517	C	LEU	A	213	−9.080	−18.461	6.261	1.00	16.13	C
ATOM	518	O	LEU	A	213	−8.604	−17.950	7.283	1.00	13.92	O
ATOM	519	CB	LEU	A	213	−11.069	−17.041	5.609	1.00	12.59	C
ATOM	520	CG	LEU	A	213	−10.425	−16.377	4.404	1.00	13.49	C
ATOM	521	CD1	LEU	A	213	−10.715	−17.173	3.139	1.00	12.34	C
ATOM	522	CD2	LEU	A	213	−10.899	−14.942	4.283	1.00	13.03	C
ATOM	523	N	HIS	A	214	−8.348	−19.107	5.356	1.00	14.35	N
ATOM	524	CA	HIS	A	214	−6.894	−19.291	5.509	1.00	16.41	C
ATOM	525	C	HIS	A	214	−6.244	−19.539	4.160	1.00	18.20	C
ATOM	526	O	HIS	A	214	−6.940	−19.874	3.207	1.00	16.31	O
ATOM	527	CB	HIS	A	214	−6.577	−20.464	6.440	1.00	13.36	C
ATOM	528	CG	HIS	A	214	−6.949	−21.797	5.874	1.00	17.43	C
ATOM	529	ND1	HIS	A	214	−6.016	−22.687	5.391	1.00	23.48	N
ATOM	530	CD2	HIS	A	214	−8.158	−22.382	5.690	1.00	19.34	C
ATOM	531	CE1	HIS	A	214	−6.630	−23.772	4.949	1.00	21.50	C
ATOM	532	NE2	HIS	A	214	−7.930	−23.613	5.122	1.00	22.11	N
ATOM	533	N	ASP	A	215	−4.920	−19.376	4.079	1.00	18.22	N
ATOM	534	CA	ASP	A	215	−4.188	−19.750	2.867	1.00	17.30	C
ATOM	535	C	ASP	A	215	−2.925	−20.539	3.240	1.00	19.55	C
ATOM	536	O	ASP	A	215	−1.834	−20.316	2.712	1.00	19.31	O
ATOM	537	CB	ASP	A	215	−3.849	−18.504	2.029	1.00	14.78	C
ATOM	538	CG	ASP	A	215	−2.730	−17.641	2.638	1.00	17.69	C
ATOM	539	OD1	ASP	A	215	−2.483	−17.688	3.869	1.00	15.15	O
ATOM	540	OD2	ASP	A	215	−2.095	−16.899	1.866	1.00	17.44	O
ATOM	541	N	GLN	A	216	−3.078	−21.470	4.167	1.00	21.06	N
ATOM	542	CA	GLN	A	216	−1.934	−22.227	4.657	1.00	24.33	C
ATOM	543	C	GLN	A	216	−1.340	−23.160	3.607	1.00	21.68	C
ATOM	544	O	GLN	A	216	−0.150	−23.452	3.649	1.00	24.43	O
ATOM	545	CB	GLN	A	216	−2.333	−23.029	5.886	1.00	23.90	C
ATOM	546	CG	GLN	A	216	−2.684	−22.189	7.079	1.00	20.99	C
ATOM	547	CD	GLN	A	216	−3.202	−23.036	8.215	1.00	30.17	C
ATOM	548	OE1	GLN	A	216	−4.266	−23.648	8.110	1.00	26.71	O
ATOM	549	NE2	GLN	A	216	−2.440	−23.098	9.305	1.00	40.70	N
ATOM	550	N	ASN	A	217	−2.162	−23.621	2.668	1.00	23.32	N
ATOM	551	CA	ASN	A	217	−1.685	−24.532	1.629	1.00	20.04	C
ATOM	552	C	ASN	A	217	−1.612	−23.852	0.283	1.00	24.86	C
ATOM	553	O	ASN	A	217	−1.540	−24.510	−0.756	1.00	27.21	O
ATOM	554	CB	ASN	A	217	−2.588	−25.759	1.517	1.00	28.11	C
ATOM	555	CG	ASN	A	217	−2.888	−26.378	2.852	1.00	32.30	C
ATOM	556	OD1	ASN	A	217	−4.055	−26.547	3.218	1.00	38.88	O
ATOM	557	ND2	ASN	A	217	−1.841	−26.715	3.600	1.00	27.42	N
ATOM	558	N	GLY	A	218	−1.658	−22.529	0.295	1.00	22.21	N
ATOM	559	CA	GLY	A	218	−1.460	−21.777	−0.918	1.00	20.14	C
ATOM	560	C	GLY	A	218	−2.428	−20.632	−1.068	1.00	22.88	C
ATOM	561	O	GLY	A	218	−2.165	−19.536	−0.571	1.00	23.78	O
ATOM	562	N	PRO	A	219	−3.534	−20.871	−1.791	1.00	26.59	N
ATOM	563	CA	PRO	A	219	−4.537	−19.838	−2.062	1.00	23.67	C
ATOM	564	C	PRO	A	219	−5.541	−19.712	−0.933	1.00	20.80	C
ATOM	565	O	PRO	A	219	−5.700	−20.647	−0.143	1.00	21.41	O
ATOM	566	CB	PRO	A	219	−5.216	−20.342	−3.341	1.00	21.68	C
ATOM	567	CG	PRO	A	219	−5.134	−21.823	−3.228	1.00	22.20	C
ATOM	568	CD	PRO	A	219	−3.775	−22.087	−2.592	1.00	27.98	C
ATOM	569	N	TRP	A	220	−6.210	−18.564	−0.867	1.00	19.23	N
ATOM	570	CA	TRP	A	220	−7.281	−18.357	0.093	1.00	20.89	C
ATOM	571	C	TRP	A	220	−8.394	−19.370	−0.119	1.00	18.11	C
ATOM	572	O	TRP	A	220	−8.890	−19.549	−1.237	1.00	16.24	O
ATOM	573	CB	TRP	A	220	−7.818	−16.924	0.000	1.00	20.98	C
ATOM	574	CG	TRP	A	220	−6.855	−15.955	0.591	1.00	19.44	C
ATOM	575	CD1	TRP	A	220	−6.071	−15.058	−0.079	1.00	22.05	C
ATOM	576	CD2	TRP	A	220	−6.519	−15.825	1.977	1.00	16.53	C
ATOM	577	NE1	TRP	A	220	−5.286	−14.361	0.811	1.00	14.72	N
ATOM	578	CE2	TRP	A	220	−5.539	−14.815	2.077	1.00	13.97	C
ATOM	579	CE3	TRP	A	220	−6.958	−16.456	3.143	1.00	12.82	C
ATOM	580	CZ2	TRP	A	220	−4.997	−14.422	3.295	1.00	16.02	C
ATOM	581	CZ3	TRP	A	220	−6.422	−16.062	4.347	1.00	15.01	C
ATOM	582	CH2	TRP	A	220	−5.449	−15.060	4.418	1.00	18.72	C
ATOM	583	N	LYS	A	221	−8.744	−20.038	0.979	1.00	18.43	N
ATOM	584	CA	LYS	A	221	−9.784	−21.059	1.030	1.00	20.12	C
ATOM	585	C	LYS	A	221	−10.651	−20.866	2.269	1.00	17.14	C
ATOM	586	O	LYS	A	221	−10.133	−20.648	3.354	1.00	17.85	O
ATOM	587	CB	LYS	A	221	−9.169	−22.463	1.059	1.00	22.71	C
ATOM	588	CG	LYS	A	221	−8.599	−22.928	−0.263	1.00	30.31	C
ATOM	589	CD	LYS	A	221	−7.862	−24.250	−0.113	1.00	39.91	C
ATOM	590	CE	LYS	A	221	−7.419	−24.776	−1.471	1.00	44.01	C
ATOM	591	NZ	LYS	A	221	−6.601	−26.016	−1.336	1.00	58.69	N
ATOM	592	N	TRP	A	222	−11.965	−20.938	2.096	1.00	20.05	N
ATOM	593	CA	TRP	A	222	−12.893	−21.059	3.220	1.00	18.07	C
ATOM	594	C	TRP	A	222	−12.973	−22.520	3.658	1.00	15.25	C
ATOM	595	O	TRP	A	222	−12.883	−23.404	2.821	1.00	22.45	O
ATOM	596	CB	TRP	A	222	−14.280	−20.553	2.827	1.00	18.47	C
ATOM	597	CG	TRP	A	222	−14.383	−19.074	2.639	1.00	15.11	C
ATOM	598	CD1	TRP	A	222	−14.384	−18.397	1.458	1.00	15.59	C
ATOM	599	CD2	TRP	A	222	−14.536	−18.090	3.667	1.00	12.30	C
ATOM	600	NE1	TRP	A	222	−14.525	−17.045	1.686	1.00	17.01	N
ATOM	601	CE2	TRP	A	222	−14.621	−16.834	3.037	1.00	14.83	C
ATOM	602	CE3	TRP	A	222	−14.607	−18.148	5.058	1.00	15.63	C
ATOM	603	CZ2	TRP	A	222	−14.774	−15.651	3.749	1.00	14.19	C
ATOM	604	CZ3	TRP	A	222	−14.750	−16.975	5.761	1.00	14.82	C
ATOM	605	CH2	TRP	A	222	−14.833	−15.741	5.103	1.00	16.93	C
ATOM	606	N	VAL	A	223	−13.160	−22.781	4.948	1.00	18.67	N
ATOM	607	CA	VAL	A	223	−13.104	−24.154	5.453	1.00	21.37	C
ATOM	608	C	VAL	A	223	−14.214	−25.092	4.955	1.00	19.54	C
ATOM	609	O	VAL	A	223	−14.002	−26.293	4.883	1.00	26.83	O
ATOM	610	CB	VAL	A	223	−13.127	−24.195	7.000	1.00	20.27	C
ATOM	611	CG1	VAL	A	223	−11.823	−23.684	7.550	1.00	16.93	C
ATOM	612	CG2	VAL	A	223	−14.323	−23.424	7.546	1.00	13.22	C
ATOM	613	N	ASP	A	224	−15.391	−24.575	4.627	1.00	20.49	N
ATOM	614	CA	ASP	A	224	−16.455	−25.453	4.129	1.00	28.05	C
ATOM	615	C	ASP	A	224	−16.450	−25.610	2.592	1.00	31.47	C
ATOM	616	O	ASP	A	224	−17.344	−26.231	2.017	1.00	34.41	O
ATOM	617	CB	ASP	A	224	−17.832	−24.956	4.606	1.00	26.17	C
ATOM	618	CG	ASP	A	224	−18.313	−23.720	3.861	1.00	30.40	C
ATOM	619	OD1	ASP	A	224	−17.480	−22.971	3.288	1.00	27.86	O
ATOM	620	OD2	ASP	A	224	−19.548	−23.486	3.866	1.00	41.83	O
ATOM	621	N	GLY	A	225	−15.442	−25.060	1.930	1.00	26.37	N
ATOM	622	CA	GLY	A	225	−15.325	−25.234	0.495	1.00	24.35	C
ATOM	623	C	GLY	A	225	−15.828	−24.060	−0.325	1.00	26.11	C
ATOM	624	O	GLY	A	225	−15.605	−24.021	−1.532	1.00	30.45	O
ATOM	625	N	THR	A	226	−16.512	−23.114	0.322	1.00	28.38	N
ATOM	626	CA	THR	A	226	−16.991	−21.894	−0.346	1.00	26.57	C
ATOM	627	C	THR	A	226	−15.853	−21.219	−1.107	1.00	27.23	C
ATOM	628	O	THR	A	226	−14.732	−21.105	−0.602	1.00	25.68	O
ATOM	629	CB	THR	A	226	−17.587	−20.886	0.669	1.00	26.04	C
ATOM	630	OG1	THR	A	226	−18.644	−21.511	1.408	1.00	31.78	O
ATOM	631	CG2	THR	A	226	−18.109	−19.649	−0.025	1.00	22.83	C
ATOM	632	N	ASP	A	227	−16.131	−20.791	−2.331	1.00	25.74	N
ATOM	633	CA	ASP	A	227	−15.101	−20.198	−3.157	1.00	24.58	C
ATOM	634	C	ASP	A	227	−14.769	−18.774	−2.724	1.00	27.29	C
ATOM	635	O	ASP	A	227	−15.658	−17.943	−2.523	1.00	23.84	O
ATOM	636	CB	ASP	A	227	−15.523	−20.199	−4.625	1.00	31.00	C
ATOM	637	CG	ASP	A	227	−14.712	−19.226	−5.447	1.00	33.32	C
ATOM	638	OD1	ASP	A	227	−13.509	−19.502	−5.653	1.00	36.87	O
ATOM	639	OD2	ASP	A	227	−15.261	−18.175	−5.849	1.00	32.69	O
ATOM	640	N	TYR	A	228	−13.480	−18.485	−2.609	1.00	25.74	N
ATOM	641	CA	TYR	A	228	−13.055	−17.195	−2.090	1.00	22.35	C
ATOM	642	C	TYR	A	228	−13.186	−16.074	−3.109	1.00	22.96	C
ATOM	643	O	TYR	A	228	−13.706	−15.006	−2.779	1.00	21.88	O
ATOM	644	CB	TYR	A	228	−11.610	−17.272	−1.590	1.00	17.43	C
ATOM	645	CG	TYR	A	228	−10.989	−15.928	−1.261	1.00	18.06	C
ATOM	646	CD2	TYR	A	228	−10.176	−15.269	−2.181	1.00	19.30	C
ATOM	647	CD1	TYR	A	228	−11.208	−15.316	−0.019	1.00	18.53	C
ATOM	648	CE2	TYR	A	228	−9.602	−14.021	−1.886	1.00	18.76	C
ATOM	649	CE1	TYR	A	228	−10.630	−14.081	0.293	1.00	15.99	C
ATOM	650	CZ	TYR	A	228	−9.826	−13.436	−0.643	1.00	20.11	C
ATOM	651	OH	TYR	A	228	−9.245	−12.212	−0.342	1.00	16.25	O
ATOM	652	N	GLU	A	229	−12.717	−16.293	−4.339	1.00	24.84	N
ATOM	653	CA	GLU	A	229	−12.560	−15.153	−5.244	1.00	26.92	C
ATOM	654	C	GLU	A	229	−13.890	−14.532	−5.653	1.00	27.92	C
ATOM	655	O	GLU	A	229	−13.958	−13.314	−5.816	1.00	23.76	O
ATOM	656	CB	GLU	A	229	−11.744	−15.529	−6.482	1.00	31.64	C
ATOM	657	CG	GLU	A	229	−12.229	−16.734	−7.265	1.00	42.79	C
ATOM	658	CD	GLU	A	229	−11.112	−17.346	−8.115	1.00	43.21	C
ATOM	659	OE1	GLU	A	229	−10.142	−16.627	−8.448	1.00	39.47	O
ATOM	660	OE2	GLU	A	229	−11.196	−18.552	−8.440	1.00	52.24	O
ATOM	661	N	THR	A	230	−14.945	−15.341	−5.782	1.00	26.03	N
ATOM	662	CA	THR	A	230	−16.276	−14.802	−6.087	1.00	26.83	C
ATOM	663	C	THR	A	230	−17.120	−14.519	−4.847	1.00	30.75	C
ATOM	664	O	THR	A	230	−18.233	−14.006	−4.945	1.00	30.18	O
ATOM	665	CB	THR	A	230	−17.090	−15.754	−6.977	1.00	27.80	C
ATOM	666	OG1	THR	A	230	−17.113	−17.052	−6.378	1.00	25.69	O
ATOM	667	CG2	THR	A	230	−16.472	−15.855	−8.362	1.00	25.73	C
ATOM	668	N	GLY	A	231	−16.610	−14.872	−3.678	1.00	25.26	N
ATOM	669	CA	GLY	A	231	−17.362	−14.653	−2.463	1.00	27.26	C
ATOM	670	C	GLY	A	231	−17.154	−13.274	−1.878	1.00	26.63	C
ATOM	671	O	GLY	A	231	−16.290	−12.519	−2.321	1.00	25.15	O
ATOM	672	N	PHE	A	232	−17.973	−12.959	−0.882	1.00	23.85	N
ATOM	673	CA	PHE	A	232	−17.839	−11.763	−0.056	1.00	25.36	C
ATOM	674	C	PHE	A	232	−16.433	−11.627	0.530	1.00	22.51	C
ATOM	675	O	PHE	A	232	−15.815	−12.623	0.898	1.00	24.64	O
ATOM	676	CB	PHE	A	232	−18.875	−11.820	1.062	1.00	23.46	C
ATOM	677	CG	PHE	A	232	−18.859	−10.645	1.971	1.00	24.65	C
ATOM	678	CD1	PHE	A	232	−19.395	−9.429	1.564	1.00	19.49	C
ATOM	679	CD2	PHE	A	232	−18.354	−10.760	3.254	1.00	17.94	C
ATOM	680	CE1	PHE	A	232	−19.391	−8.337	2.414	1.00	21.52	C
ATOM	681	CE2	PHE	A	232	−18.350	−9.671	4.102	1.00	20.16	C
ATOM	682	CZ	PHE	A	232	−18.870	−8.457	3.678	1.00	22.04	C
ATOM	683	N	LYS	A	233	−15.923	−10.400	0.576	1.00	24.28	N
ATOM	684	CA	LYS	A	233	−14.642	−10.099	1.224	1.00	22.92	C
ATOM	685	C	LYS	A	233	−14.782	−8.799	1.978	1.00	22.84	C
ATOM	686	O	LYS	A	233	−15.471	−7.891	1.516	1.00	22.56	O
ATOM	687	CB	LYS	A	233	−13.495	−9.991	0.212	1.00	17.41	C
ATOM	688	CG	LYS	A	233	−13.227	−11.274	−0.560	1.00	20.00	C
ATOM	689	CD	LYS	A	233	−12.285	−11.032	−1.710	1.00	21.13	C
ATOM	690	CE	LYS	A	233	−12.419	−12.105	−2.767	1.00	26.26	C
ATOM	691	NZ	LYS	A	233	−13.753	−12.082	−3.453	1.00	23.06	N
ATOM	692	N	ASN	A	234	−14.132	−8.705	3.134	1.00	17.57	N
ATOM	693	CA	ASN	A	234	−14.165	−7.467	3.910	1.00	21.38	C
ATOM	694	C	ASN	A	234	−12.791	−7.112	4.486	1.00	19.87	C
ATOM	695	O	ASN	A	234	−12.683	−6.685	5.629	1.00	23.24	O
ATOM	696	CB	ASN	A	234	−15.212	−7.571	5.033	1.00	18.47	C
ATOM	697	CG	ASN	A	234	−15.554	−6.222	5.643	1.00	19.07	C
ATOM	698	OD1	ASN	A	234	−15.762	−6.106	6.848	1.00	22.84	O
ATOM	699	ND2	ASN	A	234	−15.579	−5.191	4.817	1.00	21.10	N
ATOM	700	N	TRP	A	235	−11.742	−7.311	3.697	1.00	19.16	N
ATOM	701	CA	TRP	A	235	−10.390	−6.975	4.135	1.00	22.32	C
ATOM	702	C	TRP	A	235	−10.264	−5.498	4.467	1.00	20.90	C
ATOM	703	O	TRP	A	235	−10.730	−4.642	3.719	1.00	27.44	O
ATOM	704	CB	TRP	A	235	−9.354	−7.319	3.063	1.00	20.49	C
ATOM	705	CG	TRP	A	235	−9.281	−8.753	2.684	1.00	20.76	C
ATOM	706	CD1	TRP	A	235	−9.712	−9.314	1.523	1.00	19.71	C
ATOM	707	CD2	TRP	A	235	−8.736	−9.816	3.467	1.00	18.48	C
ATOM	708	NE1	TRP	A	235	−9.475	−10.663	1.532	1.00	18.33	N
ATOM	709	CE2	TRP	A	235	−8.869	−10.998	2.713	1.00	17.93	C
ATOM	710	CE3	TRP	A	235	−8.135	−9.883	4.730	1.00	17.04	C
ATOM	711	CZ2	TRP	A	235	−8.427	−12.236	3.180	1.00	18.19	C
ATOM	712	CZ3	TRP	A	235	−7.703	−11.102	5.193	1.00	14.22	C
ATOM	713	CH2	TRP	A	235	−7.855	−12.269	4.423	1.00	16.87	C
ATOM	714	N	ARG	A	236	−9.630	−5.198	5.585	1.00	23.85	N
ATOM	715	CA	ARG	A	236	−9.169	−3.842	5.826	1.00	25.84	C
ATOM	716	C	ARG	A	236	−8.260	−3.466	4.669	1.00	25.73	C
ATOM	717	O	ARG	A	236	−7.521	−4.318	4.166	1.00	27.18	O
ATOM	718	CB	ARG	A	236	−8.428	−3.743	7.159	1.00	24.94	C
ATOM	719	CG	ARG	A	236	−8.108	−2.312	7.586	1.00	32.25	C
ATOM	720	CD	ARG	A	236	−7.436	−2.288	8.947	1.00	30.42	C
ATOM	721	NE	ARG	A	236	−6.217	−3.084	8.934	1.00	38.54	N
ATOM	722	CZ	ARG	A	236	−5.711	−3.700	10.000	1.00	39.09	C
ATOM	723	NH1	ARG	A	236	−6.327	−3.608	11.176	1.00	39.28	N
ATOM	724	NH2	ARG	A	236	−4.588	−4.409	9.889	1.00	27.72	N
ATOM	725	N	PRO	A	237	−8.333	−2.210	4.212	1.00	25.65	N
ATOM	726	CA	PRO	A	237	−7.412	−1.747	3.167	1.00	31.88	C
ATOM	727	C	PRO	A	237	−5.951	−2.048	3.497	1.00	27.32	C
ATOM	728	O	PRO	A	237	−5.531	−1.839	4.638	1.00	28.86	O
ATOM	729	CB	PRO	A	237	−7.678	−0.242	3.122	1.00	33.60	C
ATOM	730	CG	PRO	A	237	−9.149	−0.156	3.436	1.00	32.49	C
ATOM	731	CD	PRO	A	237	−9.367	−1.203	4.515	1.00	29.17	C
ATOM	732	N	GLU	A	238	−5.231	−2.563	2.501	1.00	21.38	N
ATOM	733	CA	GLU	A	238	−3.843	−3.022	2.608	1.00	23.04	C
ATOM	734	C	GLU	A	238	−3.741	−4.424	3.231	1.00	19.36	C
ATOM	735	O	GLU	A	238	−2.648	−4.901	3.526	1.00	20.85	O
ATOM	736	CB	GLU	A	238	−2.978	−2.022	3.397	1.00	26.89	C
ATOM	737	CG	GLU	A	238	−2.828	−0.651	2.740	1.00	31.80	C
ATOM	738	CD	GLU	A	238	−2.337	0.424	3.713	1.00	51.15	C
ATOM	739	OE1	GLU	A	238	−2.205	0.128	4.926	1.00	50.89	O
ATOM	740	OE2	GLU	A	238	−2.101	1.573	3.269	1.00	56.05	O
ATOM	741	N	GLN	A	239	−4.872	−5.089	3.427	1.00	20.11	N
ATOM	742	CA	GLN	A	239	−4.840	−6.495	3.825	1.00	21.60	C
ATOM	743	C	GLN	A	239	−5.501	−7.317	2.736	1.00	19.53	C
ATOM	744	O	GLN	A	239	−6.332	−6.792	2.011	1.00	21.20	O
ATOM	745	CB	GLN	A	239	−5.543	−6.726	5.166	1.00	17.31	C
ATOM	746	CG	GLN	A	239	−5.020	−5.893	6.310	1.00	21.03	C
ATOM	747	CD	GLN	A	239	−3.565	−6.156	6.618	1.00	18.65	C
ATOM	748	OE1	GLN	A	239	−3.045	−7.232	6.343	1.00	17.67	O
ATOM	749	NE2	GLN	A	239	−2.897	−5.165	7.184	1.00	18.18	N
ATOM	750	N	PRO	A	240	−5.132	−8.601	2.601	1.00	16.46	N
ATOM	751	CA	PRO	A	240	−4.108	−9.345	3.337	1.00	20.08	C
ATOM	752	C	PRO	A	240	−2.696	−8.938	2.901	1.00	19.97	C
ATOM	753	O	PRO	A	240	−2.486	−8.679	1.708	1.00	19.33	O
ATOM	754	CB	PRO	A	240	−4.412	−10.806	2.966	1.00	15.73	C
ATOM	755	CG	PRO	A	240	−4.999	−10.714	1.622	1.00	20.40	C
ATOM	756	CD	PRO	A	240	−5.783	−9.438	1.580	1.00	18.17	C
ATOM	757	N	ASP	A	241	−1.744	−8.882	3.830	1.00	16.04	N
ATOM	758	CA	ASP	A	241	−0.399	−8.446	3.472	1.00	12.88	C
ATOM	759	C	ASP	A	241	0.663	−9.491	3.732	1.00	12.48	C
ATOM	760	O	ASP	A	241	1.842	−9.234	3.490	1.00	15.24	O
ATOM	761	CB	ASP	A	241	−0.035	−7.164	4.212	1.00	15.52	C
ATOM	762	CG	ASP	A	241	−0.053	−7.332	5.733	1.00	19.38	C
ATOM	763	OD1	ASP	A	241	−0.451	−8.416	6.231	1.00	19.33	O
ATOM	764	OD2	ASP	A	241	0.293	−6.358	6.430	1.00	17.43	O
ATOM	765	N	ASP	A	242	0.249	−10.652	4.237	1.00	17.41	N
ATOM	766	CA	ASP	A	242	1.166	−11.774	4.527	1.00	16.54	C
ATOM	767	C	ASP	A	242	2.465	−11.313	5.190	1.00	16.20	C
ATOM	768	O	ASP	A	242	3.572	−11.552	4.700	1.00	18.85	O
ATOM	769	CB	ASP	A	242	1.487	−12.530	3.261	1.00	16.74	C
ATOM	770	CG	ASP	A	242	2.053	−13.888	3.538	1.00	21.40	C
ATOM	771	OD1	ASP	A	242	1.481	−14.576	4.413	1.00	17.68	O
ATOM	772	OD2	ASP	A	242	3.066	−14.253	2.887	1.00	16.85	O
ATOM	773	N	TRP	A	243	2.301	−10.617	6.299	1.00	15.83	N
ATOM	774	CA	TRP	A	243	3.382	−9.929	6.960	1.00	16.80	C
ATOM	775	C	TRP	A	243	4.390	−10.913	7.545	1.00	16.03	C
ATOM	776	O	TRP	A	243	4.020	−11.905	8.153	1.00	15.06	O
ATOM	777	CB	TRP	A	243	2.799	−9.041	8.043	1.00	19.08	C
ATOM	778	CG	TRP	A	243	3.727	−8.029	8.570	1.00	24.75	C
ATOM	779	CD1	TRP	A	243	4.591	−7.248	7.857	1.00	21.85	C
ATOM	780	CD2	TRP	A	243	3.888	−7.665	9.942	1.00	19.00	C
ATOM	781	NE1	TRP	A	243	5.274	−6.417	8.707	1.00	20.11	N
ATOM	782	CE2	TRP	A	243	4.858	−6.653	9.993	1.00	17.79	C
ATOM	783	CE3	TRP	A	243	3.296	−8.092	11.133	1.00	19.98	C
ATOM	784	CZ2	TRP	A	243	5.259	−6.067	11.189	1.00	19.26	C
ATOM	785	CZ3	TRP	A	243	3.697	−7.508	12.321	1.00	19.32	C
ATOM	786	CH2	TRP	A	243	4.666	−6.508	12.338	1.00	14.64	C
ATOM	787	N	TYR	A	244	5.671	−10.643	7.350	1.00	19.42	N
ATOM	788	CA	TYR	A	244	6.694	−11.486	7.945	1.00	20.57	C
ATOM	789	C	TYR	A	244	7.295	−10.760	9.140	1.00	19.06	C
ATOM	790	O	TYR	A	244	8.022	−11.353	9.930	1.00	17.76	O
ATOM	791	CB	TYR	A	244	7.784	−11.833	6.932	1.00	18.60	C
ATOM	792	CG	TYR	A	244	7.501	−13.035	6.056	1.00	24.25	C
ATOM	793	CD1	TYR	A	244	6.568	−12.970	5.020	1.00	17.33	C
ATOM	794	CD2	TYR	A	244	8.189	−14.228	6.244	1.00	24.36	C
ATOM	795	CE1	TYR	A	244	6.321	−14.070	4.203	1.00	18.22	C
ATOM	796	CE2	TYR	A	244	7.945	−15.342	5.436	1.00	21.75	C
ATOM	797	CZ	TYR	A	244	7.016	−15.257	4.415	1.00	19.74	C
ATOM	798	OH	TYR	A	244	6.776	−16.367	3.620	1.00	14.89	O
ATOM	799	N	GLY	A	245	6.958	−9.478	9.265	1.00	19.02	N
ATOM	800	CA	GLY	A	245	7.658	−8.568	10.152	1.00	20.36	C
ATOM	801	C	GLY	A	245	7.367	−8.768	11.621	1.00	19.87	C
ATOM	802	O	GLY	A	245	7.941	−8.086	12.475	1.00	21.29	O
ATOM	803	N	HIS	A	246	6.463	−9.696	11.910	1.00	19.33	N
ATOM	804	CA	HIS	A	246	6.150	−10.062	13.277	1.00	17.48	C
ATOM	805	C	HIS	A	246	7.284	−10.899	13.844	1.00	18.02	C
ATOM	806	O	HIS	A	246	7.418	−11.015	15.053	1.00	22.65	O
ATOM	807	CB	HIS	A	246	4.825	−10.823	13.340	1.00	15.31	C
ATOM	808	CG	HIS	A	246	4.719	−11.907	12.316	1.00	19.52	C
ATOM	809	ND1	HIS	A	246	5.326	−13.134	12.467	1.00	16.40	N
ATOM	810	CD2	HIS	A	246	4.101	−11.937	11.112	1.00	16.23	C
ATOM	811	CE1	HIS	A	246	5.085	−13.875	11.400	1.00	17.63	C
ATOM	812	NE2	HIS	A	246	4.343	−13.172	10.564	1.00	16.33	N
ATOM	813	N	GLY	A	247	8.098	−11.482	12.968	1.00	18.78	N
ATOM	814	CA	GLY	A	247	9.295	−12.193	13.394	1.00	17.32	C
ATOM	815	C	GLY	A	247	9.030	−13.544	14.022	1.00	19.13	C
ATOM	816	O	GLY	A	247	9.904	−14.116	14.677	1.00	21.71	O
ATOM	817	N	LEU	A	248	7.828	−14.074	13.811	1.00	20.58	N
ATOM	818	CA	LEU	A	248	7.427	−15.330	14.447	1.00	17.12	C
ATOM	819	C	LEU	A	248	7.676	−16.527	13.537	1.00	14.44	C
ATOM	820	O	LEU	A	248	7.656	−17.670	13.977	1.00	17.33	O
ATOM	821	CB	LEU	A	248	5.951	−15.270	14.852	1.00	19.74	C
ATOM	822	CG	LEU	A	248	5.635	−14.119	15.804	1.00	17.23	C
ATOM	823	CD1	LEU	A	248	4.193	−14.202	16.254	1.00	17.05	C
ATOM	824	CD2	LEU	A	248	6.599	−14.120	17.007	1.00	16.08	C
ATOM	825	N	GLY	A	249	7.920	−16.261	12.263	1.00	17.53	N
ATOM	826	CA	GLY	A	249	8.159	−17.332	11.315	1.00	16.74	C
ATOM	827	C	GLY	A	249	7.032	−17.381	10.316	1.00	15.59	C
ATOM	828	O	GLY	A	249	5.874	−17.344	10.708	1.00	17.37	O
ATOM	829	N	GLY	A	250	7.370	−17.451	9.029	1.00	14.92	N
ATOM	830	CA	GLY	A	250	6.370	−17.435	7.982	1.00	19.03	C
ATOM	831	C	GLY	A	250	5.672	−16.090	7.891	1.00	20.35	C
ATOM	832	O	GLY	A	250	6.054	−15.119	8.549	1.00	18.82	O
ATOM	833	N	GLY	A	251	4.646	−16.022	7.057	1.00	21.60	N
ATOM	834	CA	GLY	A	251	3.910	−14.787	6.880	1.00	17.04	C
ATOM	835	C	GLY	A	251	2.691	−14.851	7.752	1.00	16.59	C
ATOM	836	O	GLY	A	251	2.778	−15.115	8.952	1.00	22.55	O
ATOM	837	N	GLU	A	252	1.539	−14.636	7.137	1.00	16.53	N
ATOM	838	CA	GLU	A	252	0.272	−14.664	7.846	1.00	15.39	C
ATOM	839	C	GLU	A	252	−0.760	−15.400	7.016	1.00	17.17	C
ATOM	840	O	GLU	A	252	−1.021	−15.027	5.864	1.00	14.07	O
ATOM	841	CB	GLU	A	252	−0.201	−13.253	8.143	1.00	15.30	C
ATOM	842	CG	GLU	A	252	0.748	−12.448	8.970	1.00	16.44	C
ATOM	843	CD	GLU	A	252	0.242	−11.045	9.189	1.00	18.48	C
ATOM	844	OE1	GLU	A	252	0.261	−10.579	10.340	1.00	16.20	O
ATOM	845	OE2	GLU	A	252	−0.159	−10.400	8.200	1.00	15.99	O
ATOM	846	N	ASP	A	253	−1.355	−16.437	7.590	1.00	15.10	N
ATOM	847	CA	ASP	A	253	−2.163	−17.337	6.787	1.00	16.04	C
ATOM	848	C	ASP	A	253	−3.600	−17.499	7.243	1.00	15.46	C
ATOM	849	O	ASP	A	253	−4.310	−18.320	6.713	1.00	17.45	O
ATOM	850	CB	ASP	A	253	−1.519	−18.719	6.745	1.00	15.26	C
ATOM	851	CG	ASP	A	253	−0.090	−18.683	6.258	1.00	18.84	C
ATOM	852	OD1	ASP	A	253	0.337	−17.664	5.670	1.00	19.76	O
ATOM	853	OD2	ASP	A	253	0.605	−19.703	6.423	1.00	24.71	O
ATOM	854	N	CYS	A	254	−4.029	−16.745	8.238	1.00	15.58	N
ATOM	855	CA	CYS	A	254	−5.321	−17.012	8.818	1.00	13.38	C
ATOM	856	C	CYS	A	254	−6.083	−15.715	9.012	1.00	17.24	C
ATOM	857	O	CYS	A	254	−5.577	−14.778	9.643	1.00	17.90	O
ATOM	858	CB	CYS	A	254	−5.161	−17.762	10.147	1.00	17.64	C
ATOM	859	SG	CYS	A	254	−4.659	−19.487	9.965	1.00	15.82	S
ATOM	860	N	ALA	A	255	−7.298	−15.672	8.474	1.00	10.34	N
ATOM	861	CA	ALA	A	255	−8.134	−14.474	8.555	1.00	15.36	C
ATOM	862	C	ALA	A	255	−8.863	−14.334	9.886	1.00	16.38	C
ATOM	863	O	ALA	A	255	−9.420	−15.293	10.424	1.00	15.65	O
ATOM	864	CB	ALA	A	255	−9.153	−14.460	7.430	1.00	13.09	C
ATOM	865	N	HIS	A	256	−8.886	−13.116	10.401	1.00	15.41	N
ATOM	866	CA	HIS	A	256	−9.712	−12.834	11.552	1.00	16.09	C
ATOM	867	C	HIS	A	256	−10.427	−11.512	11.367	1.00	14.49	C
ATOM	868	O	HIS	A	256	−9.986	−10.664	10.599	1.00	17.03	O
ATOM	869	CB	HIS	A	256	−8.874	−12.816	12.841	1.00	11.61	C
ATOM	870	CG	HIS	A	256	−7.844	−11.733	12.885	1.00	15.00	C
ATOM	871	ND1	HIS	A	256	−7.979	−10.609	13.673	1.00	13.69	N
ATOM	872	CD2	HIS	A	256	−6.657	−11.605	12.245	1.00	13.08	C
ATOM	873	CE1	HIS	A	256	−6.915	−9.840	13.522	1.00	15.34	C
ATOM	874	NE2	HIS	A	256	−6.098	−10.423	12.661	1.00	15.12	N
ATOM	875	N	PHE	A	257	−11.543	−11.357	12.065	1.00	16.75	N
ATOM	876	CA	PHE	A	257	−12.147	−10.057	12.229	1.00	14.34	C
ATOM	877	C	PHE	A	257	−11.246	−9.225	13.119	1.00	16.09	C
ATOM	878	O	PHE	A	257	−10.752	−9.703	14.142	1.00	16.99	O
ATOM	879	CB	PHE	A	257	−13.541	−10.159	12.844	1.00	13.50	C
ATOM	880	CG	PHE	A	257	−14.430	−11.166	12.176	1.00	21.06	C
ATOM	881	CD2	PHE	A	257	−14.462	−12.477	12.618	1.00	16.97	C
ATOM	882	CD1	PHE	A	257	−15.233	−10.803	11.098	1.00	18.50	C
ATOM	883	CE2	PHE	A	257	−15.277	−13.410	12.003	1.00	17.90	C
ATOM	884	CE1	PHE	A	257	−16.049	−11.729	10.487	1.00	16.37	C
ATOM	885	CZ	PHE	A	257	−16.066	−13.029	10.928	1.00	14.28	C
ATOM	886	N	THR	A	258	−11.039	−7.979	12.734	1.00	15.18	N
ATOM	887	CA	THR	A	258	−10.337	−7.053	13.597	1.00	19.93	C
ATOM	888	C	THR	A	258	−11.351	−6.356	14.465	1.00	22.34	C
ATOM	889	O	THR	A	258	−12.557	−6.616	14.356	1.00	28.29	O
ATOM	890	CB	THR	A	258	−9.553	−6.014	12.814	1.00	18.33	C
ATOM	891	OG1	THR	A	258	−10.468	−5.213	12.058	1.00	17.14	O
ATOM	892	CG2	THR	A	258	−8.569	−6.692	11.876	1.00	19.40	C
ATOM	893	N	ASP	A	259	−10.869	−5.459	15.316	1.00	20.10	N
ATOM	894	CA	ASP	A	259	−11.735	−4.749	16.250	1.00	23.59	C
ATOM	895	C	ASP	A	259	−12.909	−4.037	15.572	1.00	23.64	C
ATOM	896	O	ASP	A	259	−13.984	−3.947	16.148	1.00	24.14	O
ATOM	897	CB	ASP	A	259	−10.911	−3.747	17.079	1.00	22.86	C
ATOM	898	CG	ASP	A	259	−10.205	−2.685	16.223	1.00	30.45	C
ATOM	899	OD1	ASP	A	259	−10.086	−2.851	14.987	1.00	32.11	O
ATOM	900	OD2	ASP	A	259	−9.736	−1.679	16.808	1.00	36.17	O
ATOM	901	N	ASP	A	260	−12.710	−3.542	14.351	1.00	27.68	N
ATOM	902	CA	ASP	A	260	−13.762	−2.778	13.673	1.00	24.53	C
ATOM	903	C	ASP	A	260	−14.544	−3.664	12.716	1.00	23.69	C
ATOM	904	O	ASP	A	260	−15.474	−3.208	12.055	1.00	27.59	O
ATOM	905	CB	ASP	A	260	−13.177	−1.551	12.934	1.00	23.65	C
ATOM	906	CG	ASP	A	260	−12.279	−1.920	11.738	1.00	31.18	C
ATOM	907	OD1	ASP	A	260	−12.578	−2.896	11.008	1.00	25.05	O
ATOM	908	OD2	ASP	A	260	−11.267	−1.206	11.514	1.00	30.59	O
ATOM	909	N	GLY	A	261	−14.138	−4.927	12.617	1.00	24.03	N
ATOM	910	CA	GLY	A	261	−14.898	−5.908	11.863	1.00	18.76	C
ATOM	911	C	GLY	A	261	−14.236	−6.262	10.550	1.00	17.99	C
ATOM	912	O	GLY	A	261	−14.459	−7.331	10.004	1.00	13.89	O
ATOM	913	N	ARG	A	262	−13.392	−5.373	10.048	1.00	19.30	N
ATOM	914	CA	ARG	A	262	−12.709	−5.649	8.791	1.00	19.10	C
ATOM	915	C	ARG	A	262	−11.659	−6.749	8.989	1.00	19.94	C
ATOM	916	O	ARG	A	262	−11.216	−7.016	10.120	1.00	12.26	O
ATOM	917	CB	ARG	A	262	−12.115	−4.356	8.232	1.00	20.66	C
ATOM	918	CG	ARG	A	262	−13.219	−3.351	7.897	1.00	25.30	C
ATOM	919	CD	ARG	A	262	−12.667	−2.017	7.453	1.00	28.34	C
ATOM	920	NE	ARG	A	262	−11.765	−1.459	8.449	1.00	25.73	N
ATOM	921	CZ	ARG	A	262	−11.035	−0.367	8.254	1.00	29.19	C
ATOM	922	NH1	ARG	A	262	−11.114	0.278	7.100	1.00	24.96	N
ATOM	923	NH2	ARG	A	262	−10.229	0.079	9.208	1.00	29.61	N
ATOM	924	N	TRP	A	263	−11.307	−7.432	7.903	1.00	14.26	N
ATOM	925	CA	TRP	A	263	−10.517	−8.648	8.041	1.00	16.50	C
ATOM	926	C	TRP	A	263	−9.043	−8.337	8.000	1.00	15.53	C
ATOM	927	O	TRP	A	263	−8.627	−7.337	7.443	1.00	16.65	O
ATOM	928	CB	TRP	A	263	−10.851	−9.661	6.946	1.00	13.91	C
ATOM	929	CG	TRP	A	263	−12.290	−10.013	6.862	1.00	16.25	C
ATOM	930	CD1	TRP	A	263	−13.273	−9.643	7.721	1.00	13.40	C
ATOM	931	CD2	TRP	A	263	−12.918	−10.804	5.846	1.00	17.03	C
ATOM	932	NE1	TRP	A	263	−14.473	−10.156	7.314	1.00	15.19	N
ATOM	933	CE2	TRP	A	263	−14.284	−10.870	6.160	1.00	14.98	C
ATOM	934	CE3	TRP	A	263	−12.456	−11.455	4.697	1.00	13.09	C
ATOM	935	CZ2	TRP	A	263	−15.196	−11.577	5.378	1.00	19.78	C
ATOM	936	CZ3	TRP	A	263	−13.360	−12.154	3.922	1.00	16.68	C
ATOM	937	CH2	TRP	A	263	−14.716	−12.206	4.261	1.00	16.08	C
ATOM	938	N	ASN	A	264	−8.262	−9.226	8.588	1.00	15.51	N
ATOM	939	CA	ASN	A	264	−6.816	−9.162	8.521	1.00	14.14	C
ATOM	940	C	ASN	A	264	−6.313	−10.573	8.398	1.00	14.75	C
ATOM	941	O	ASN	A	264	−6.994	−11.503	8.817	1.00	18.31	O
ATOM	942	CB	ASN	A	264	−6.239	−8.490	9.768	1.00	17.34	C
ATOM	943	CG	ASN	A	264	−4.721	−8.499	9.794	1.00	18.04	C
ATOM	944	OD1	ASN	A	264	−4.070	−8.128	8.820	1.00	13.84	O
ATOM	945	ND2	ASN	A	264	−4.151	−8.917	10.923	1.00	16.66	N
ATOM	946	N	ASP	A	265	−5.146	−10.757	7.795	1.00	18.48	N
ATOM	947	CA	ASP	A	265	−4.527	−12.072	7.800	1.00	18.19	C
ATOM	948	C	ASP	A	265	−3.499	−11.991	8.902	1.00	17.54	C
ATOM	949	O	ASP	A	265	−2.811	−10.980	9.030	1.00	18.38	O
ATOM	950	CB	ASP	A	265	−3.912	−12.455	6.438	1.00	15.50	C
ATOM	951	CG	ASP	A	265	−2.875	−11.458	5.943	1.00	16.55	C
ATOM	952	OD1	ASP	A	265	−2.920	−10.277	6.358	1.00	15.74	O
ATOM	953	OD2	ASP	A	265	−2.022	−11.858	5.106	1.00	16.21	O
ATOM	954	N	ASP	A	266	−3.449	−13.013	9.745	1.00	15.99	N
ATOM	955	CA	ASP	A	266	−2.527	−12.977	10.867	1.00	16.72	C
ATOM	956	C	ASP	A	266	−1.843	−14.321	11.085	1.00	19.73	C
ATOM	957	O	ASP	A	266	−2.100	−15.292	10.371	1.00	18.63	O
ATOM	958	CB	ASP	A	266	−3.244	−12.542	12.139	1.00	15.67	C
ATOM	959	CG	ASP	A	266	−2.356	−11.743	13.041	1.00	20.35	C
ATOM	960	OD2	ASP	A	266	−2.877	−10.827	13.717	1.00	20.40	O
ATOM	961	OD1	ASP	A	266	−1.130	−12.024	13.055	1.00	18.05	O
ATOM	962	N	VAL	A	267	−0.951	−14.365	12.069	1.00	21.31	N
ATOM	963	CA	VAL	A	267	−0.236	−15.588	12.357	1.00	20.03	C
ATOM	964	C	VAL	A	267	−1.206	−16.604	12.957	1.00	17.18	C
ATOM	965	O	VAL	A	267	−1.904	−16.301	13.923	1.00	19.78	O
ATOM	966	CB	VAL	A	267	0.935	−15.327	13.302	1.00	18.16	C
ATOM	967	CG1	VAL	A	267	1.670	−16.609	13.576	1.00	19.68	C
ATOM	968	CG2	VAL	A	267	1.862	−14.301	12.685	1.00	15.95	C
ATOM	969	N	CYS	A	268	−1.246	−17.803	12.383	1.00	12.37	N
ATOM	970	CA	CYS	A	268	−2.213	−18.818	12.785	1.00	14.68	C
ATOM	971	C	CYS	A	268	−2.031	−19.284	14.238	1.00	14.79	C
ATOM	972	O	CYS	A	268	−2.960	−19.800	14.855	1.00	17.64	O
ATOM	973	CB	CYS	A	268	−2.140	−20.010	11.832	1.00	15.66	C
ATOM	974	SG	CYS	A	268	−2.628	−19.567	10.101	1.00	27.47	S
ATOM	975	N	GLN	A	269	−0.851	−19.069	14.786	1.00	13.72	N
ATOM	976	CA	GLN	A	269	−0.559	−19.493	16.149	1.00	16.48	C
ATOM	977	C	GLN	A	269	−1.136	−18.565	17.190	1.00	15.79	C
ATOM	978	O	GLN	A	269	−1.204	−18.920	18.376	1.00	17.70	O
ATOM	979	CB	GLN	A	269	0.934	−19.562	16.397	1.00	17.79	C
ATOM	980	CG	GLN	A	269	1.752	−20.417	15.507	1.00	20.66	C
ATOM	981	CD	GLN	A	269	3.240	−20.205	15.825	1.00	31.48	C
ATOM	982	OE1	GLN	A	269	3.870	−19.269	15.315	1.00	28.23	O
ATOM	983	NE2	GLN	A	269	3.786	−21.039	16.708	1.00	24.46	N
ATOM	984	N	ARG	A	270	−1.501	−17.358	16.781	1.00	13.72	N
ATOM	985	CA	ARG	A	270	−2.043	−16.420	17.759	1.00	14.78	C
ATOM	986	C	ARG	A	270	−3.318	−16.974	18.307	1.00	13.79	C
ATOM	987	O	ARG	A	270	−4.116	−17.542	17.558	1.00	16.01	O
ATOM	988	CB	ARG	A	270	−2.301	−15.045	17.162	1.00	13.63	C
ATOM	989	CG	ARG	A	270	−1.059	−14.369	16.672	1.00	17.92	C
ATOM	990	CD	ARG	A	270	−1.316	−12.904	16.442	1.00	15.26	C
ATOM	991	NE	ARG	A	270	−0.240	−12.295	15.678	1.00	18.21	N
ATOM	992	CZ	ARG	A	270	0.907	−11.880	16.206	1.00	17.13	C
ATOM	993	NH1	ARG	A	270	1.137	−12.008	17.513	1.00	15.71	N
ATOM	994	NH2	ARG	A	270	1.814	−11.320	15.426	1.00	12.96	N
ATOM	995	N	PRO	A	271	−3.503	−16.833	19.623	1.00	14.36	N
ATOM	996	CA	PRO	A	271	−4.769	−17.166	20.253	1.00	12.34	C
ATOM	997	C	PRO	A	271	−5.760	−15.999	20.077	1.00	13.26	C
ATOM	998	O	PRO	A	271	−5.535	−14.874	20.507	1.00	14.69	O
ATOM	999	CB	PRO	A	271	−4.381	−17.391	21.727	1.00	15.38	C
ATOM	1000	CG	PRO	A	271	−3.151	−16.556	21.928	1.00	15.88	C
ATOM	1001	CD	PRO	A	271	−2.502	−16.336	20.593	1.00	15.31	C
ATOM	1002	N	TYR	A	272	−6.855	−16.285	19.400	1.00	13.29	N
ATOM	1003	CA	TYR	A	272	−7.918	−15.315	19.193	1.00	16.14	C
ATOM	1004	C	TYR	A	272	−9.201	−16.027	19.549	1.00	13.34	C
ATOM	1005	O	TYR	A	272	−9.224	−17.253	19.601	1.00	12.02	O
ATOM	1006	CB	TYR	A	272	−7.982	−14.830	17.736	1.00	11.47	C
ATOM	1007	CG	TYR	A	272	−6.967	−13.776	17.310	1.00	13.69	C
ATOM	1008	CD1	TYR	A	272	−6.439	−12.872	18.213	1.00	9.93	C
ATOM	1009	CD2	TYR	A	272	−6.574	−13.673	15.969	1.00	12.95	C
ATOM	1010	CE1	TYR	A	272	−5.538	−11.914	17.807	1.00	11.19	C
ATOM	1011	CE2	TYR	A	272	−5.684	−12.723	15.561	1.00	9.94	C
ATOM	1012	CZ	TYR	A	272	−5.164	−11.845	16.484	1.00	14.00	C
ATOM	1013	OH	TYR	A	272	−4.257	−10.893	16.080	1.00	17.41	O
ATOM	1014	N	ARG	A	273	−10.271	−15.272	19.765	1.00	12.95	N
ATOM	1015	CA	ARG	A	273	−11.572	−15.885	19.870	1.00	12.35	C
ATOM	1016	C	ARG	A	273	−11.927	−16.389	18.493	1.00	14.06	C
ATOM	1017	O	ARG	A	273	−11.229	−16.088	17.517	1.00	14.38	O
ATOM	1018	CB	ARG	A	273	−12.611	−14.905	20.397	1.00	14.33	C
ATOM	1019	CG	ARG	A	273	−12.364	−14.520	21.841	1.00	12.78	C
ATOM	1020	CD	ARG	A	273	−13.449	−13.645	22.401	1.00	17.64	C
ATOM	1021	NE	ARG	A	273	−13.276	−13.515	23.840	1.00	21.61	N
ATOM	1022	CZ	ARG	A	273	−14.015	−12.742	24.625	1.00	24.75	C
ATOM	1023	NH1	ARG	A	273	−14.997	−12.010	24.109	1.00	30.00	N
ATOM	1024	NH2	ARG	A	273	−13.763	−12.702	25.930	1.00	20.72	N
ATOM	1025	N	TRP	A	274	−12.986	−17.183	18.411	1.00	13.15	N
ATOM	1026	CA	TRP	A	274	−13.420	−17.706	17.130	1.00	13.83	C
ATOM	1027	C	TRP	A	274	−14.926	−17.845	17.166	1.00	15.15	C
ATOM	1028	O	TRP	A	274	−15.525	−17.760	18.227	1.00	14.10	O
ATOM	1029	CB	TRP	A	274	−12.758	−19.043	16.833	1.00	12.63	C
ATOM	1030	CG	TRP	A	274	−13.207	−20.135	17.726	1.00	16.63	C
ATOM	1031	CD1	TRP	A	274	−14.106	−21.107	17.428	1.00	18.08	C
ATOM	1032	CD2	TRP	A	274	−12.780	−20.377	19.080	1.00	14.16	C
ATOM	1033	NE1	TRP	A	274	−14.265	−21.951	18.507	1.00	15.30	N
ATOM	1034	CE2	TRP	A	274	−13.463	−21.521	19.533	1.00	15.80	C
ATOM	1035	CE3	TRP	A	274	−11.874	−19.744	19.944	1.00	16.39	C
ATOM	1036	CZ2	TRP	A	274	−13.282	−22.046	20.822	1.00	16.41	C
ATOM	1037	CZ3	TRP	A	274	−11.700	−20.261	21.226	1.00	17.93	C
ATOM	1038	CH2	TRP	A	274	−12.407	−21.401	21.651	1.00	14.81	C
ATOM	1039	N	VAL	A	275	−15.532	−18.025	16.003	1.00	13.91	N
ATOM	1040	CA	VAL	A	275	−16.954	−18.282	15.911	1.00	14.90	C
ATOM	1041	C	VAL	A	275	−17.157	−19.604	15.214	1.00	17.68	C
ATOM	1042	O	VAL	A	275	−16.570	−19.843	14.160	1.00	16.82	O
ATOM	1043	CB	VAL	A	275	−17.690	−17.199	15.126	1.00	15.04	C
ATOM	1044	CG1	VAL	A	275	−19.194	−17.473	15.122	1.00	14.67	C
ATOM	1045	CG2	VAL	A	275	−17.359	−15.825	15.676	1.00	12.68	C
ATOM	1046	N	CYS	A	276	−17.993	−20.463	15.791	1.00	18.92	N
ATOM	1047	CA	CYS	A	276	−18.396	−21.676	15.095	1.00	20.03	C
ATOM	1048	C	CYS	A	276	−19.725	−21.444	14.397	1.00	19.45	C
ATOM	1049	O	CYS	A	276	−20.581	−20.714	14.896	1.00	17.29	O
ATOM	1050	CB	CYS	A	276	−18.493	−22.859	16.055	1.00	22.59	C
ATOM	1051	SG	CYS	A	276	−16.895	−23.523	16.446	1.00	31.78	S
ATOM	1052	N	GLU	A	277	−19.865	−22.050	13.225	1.00	18.94	N
ATOM	1053	CA	GLU	A	277	−21.077	−21.941	12.437	1.00	21.40	C
ATOM	1054	C	GLU	A	277	−21.492	−23.299	11.919	1.00	19.98	C
ATOM	1055	O	GLU	A	277	−20.668	−24.086	11.467	1.00	20.59	O
ATOM	1056	CB	GLU	A	277	−20.887	−20.988	11.263	1.00	17.46	C
ATOM	1057	CG	GLU	A	277	−22.187	−20.673	10.536	1.00	21.39	C
ATOM	1058	CD	GLU	A	277	−21.972	−20.063	9.154	1.00	22.43	C
ATOM	1059	OE1	GLU	A	277	−20.817	−20.032	8.682	1.00	21.58	O
ATOM	1060	OE2	GLU	A	277	−22.962	−19.607	8.540	1.00	22.39	O
ATOM	1061	N	THR	A	278	−22.778	−23.572	11.998	1.00	19.21	N
ATOM	1062	CA	THR	A	278	−23.351	−24.710	11.309	1.00	24.97	C
ATOM	1063	C	THR	A	278	−24.612	−24.250	10.581	1.00	25.29	C
ATOM	1064	O	THR	A	278	−25.166	−23.196	10.887	1.00	24.46	O
ATOM	1065	CB	THR	A	278	−23.688	−25.846	12.267	1.00	25.96	C
ATOM	1066	OG1	THR	A	278	−23.799	−27.063	11.527	1.00	36.51	O
ATOM	1067	CG2	THR	A	278	−24.996	−25.566	12.973	1.00	23.69	C
ATOM	1068	N	GLU	A	279	−25.065	−25.033	9.613	1.00	29.02	N
ATOM	1069	CA	GLU	A	279	−26.228	−24.630	8.841	1.00	31.70	C
ATOM	1070	C	GLU	A	279	−27.438	−25.498	9.167	1.00	29.56	C
ATOM	1071	O	GLU	A	279	−27.299	−26.687	9.406	1.00	29.11	O
ATOM	1072	CB	GLU	A	279	−25.911	−24.678	7.347	1.00	28.64	C
ATOM	1073	CG	GLU	A	279	−24.969	−23.568	6.885	1.00	27.57	C
ATOM	1074	CD	GLU	A	279	−23.497	−23.939	7.011	1.00	31.65	C
ATOM	1075	OE1	GLU	A	279	−22.662	−23.026	7.182	1.00	30.86	O
ATOM	1076	OE2	GLU	A	279	−23.166	−25.139	6.923	1.00	32.59	O
ATOM	1077	N	LEU	A	280	−28.617	−24.885	9.219	1.00	34.32	N
ATOM	1078	CA	LEU	A	280	−29.855	−25.649	9.304	1.00	35.91	C
ATOM	1079	C	LEU	A	280	−30.265	−26.069	7.893	1.00	40.23	C
ATOM	1080	O	LEU	A	280	−30.735	−27.187	7.666	1.00	43.65	O
ATOM	1081	CB	LEU	A	280	−30.974	−24.837	9.959	1.00	37.40	C
ATOM	1082	CG	LEU	A	280	−30.811	−24.359	11.398	1.00	33.17	C
ATOM	1083	CD1	LEU	A	280	−32.064	−23.616	11.839	1.00	39.13	C
ATOM	1084	CD2	LEU	A	280	−30.516	−25.518	12.322	1.00	36.44	C
ATOM	1085	OXT	LEU	A	280	−30.126	−25.285	6.942	1.00	35.92	O
HETATM	1086	CA	CA	A	1001	−0.390	−15.928	3.667	1.00	18.60	Ca
HETATM	1087	CA	CA	A	1002	−1.936	−8.931	8.005	1.00	15.61	Ca
HETATM	1088	CA	CA	A	1003	−22.072	−18.548	6.675	1.00	20.87	Ca
HETATM	1089	CL	CL	A	1004	−0.586	−12.976	20.217	1.00	15.82	Cl
HETATM	1090	CL	CL	A	1005	−16.511	−11.093	27.288	1.00	51.09	Cl
TER
HETATM	1091	C1	NGA	D	1	−0.855	−5.202	11.893	1.00	29.65	C
HETATM	1092	C2	NGA	D	1	−1.637	−6.424	11.455	1.00	25.74	C
HETATM	1093	C3	NGA	D	1	−0.719	−7.433	10.877	1.00	19.12	C
HETATM	1094	C4	NGA	D	1	0.140	−6.858	9.782	1.00	26.89	C
HETATM	1095	C5	NGA	D	1	0.800	−5.564	10.227	1.00	27.00	C
HETATM	1096	C6	NGA	D	1	1.564	−4.950	9.107	1.00	23.07	C
HETATM	1097	C7	NGA	D	1	−3.674	−6.716	12.908	1.00	23.79	C
HETATM	1098	C8	NGA	D	1	−4.345	−7.353	14.124	1.00	17.91	C
HETATM	1099	N2	NGA	D	1	−2.306	−7.017	12.612	1.00	24.92	N
HETATM	1100	O1	NGA	D	1	−1.657	−4.257	12.478	1.00	40.15	O
HETATM	1101	O3	NGA	D	1	−1.485	−8.575	10.399	1.00	17.51	O
HETATM	1102	O4	NGA	D	1	−0.627	−6.578	8.599	1.00	18.77	O
HETATM	1103	O5	NGA	D	1	−0.199	−4.606	10.704	1.00	21.93	O
HETATM	1104	O6	NGA	D	1	2.201	−3.801	9.619	1.00	23.93	O
HETATM	1105	O7	NGA	D	1	−4.290	−5.954	12.181	1.00	26.58	O
TER
END

TABLE 10.2
ATOM	1	N	GLN	A	1	4.287	−11.302	31.298	1.00	52.13		N
ATOM	2	CA	GLN	A	1	2.840	−11.140	31.183	1.00	68.91		C
ATOM	3	C	GLN	A	1	2.320	−11.699	29.861	1.00	58.31		C
ATOM	4	O	GLN	A	1	3.071	−11.816	28.894	1.00	49.26		O
ATOM	5	CB	GLN	A	1	2.457	−9.664	31.320	1.00	75.74		C
ATOM	6	CG	GLN	A	1	2.710	−9.088	32.707	1.00	88.73		C
ATOM	7	CD	GLN	A	1	1.879	−9.771	33.783	1.00	100.20		C
ATOM	8	NE2	GLN	A	1	2.448	−9.903	34.978	1.00	94.67		N
ATOM	9	OE1	GLN	A	1	0.742	−10.179	33.539	1.00	98.51		O
ATOM	10	N	VAL	A	2	1.035	−12.043	29.824	1.00	56.43		N
ATOM	11	CA	VAL	A	2	0.425	−12.599	28.617	1.00	47.45		C
ATOM	12	C	VAL	A	2	0.210	−11.533	27.541	1.00	49.76		C
ATOM	13	O	VAL	A	2	−0.422	−10.506	27.790	1.00	52.22		O
ATOM	14	CB	VAL	A	2	−0.928	−13.275	28.926	1.00	51.59		C
ATOM	15	CG1	VAL	A	2	−1.627	−13.682	27.636	1.00	51.80		C
ATOM	16	CG2	VAL	A	2	−0.727	−14.481	29.825	1.00	44.15		C
ATOM	17	N	GLN	A	3	0.740	−11.785	26.348	1.00	39.57		N
ATOM	18	CA	GLN	A	3	0.582	−10.876	25.219	1.00	41.94		C
ATOM	19	C	GLN	A	3	0.085	−11.615	23.981	1.00	38.69		C
ATOM	20	O	GLN	A	3	0.586	−12.691	23.649	1.00	39.97		O
ATOM	21	CB	GLN	A	3	1.903	−10.176	24.891	1.00	40.78		C
ATOM	22	CG	GLN	A	3	2.450	−9.275	25.980	1.00	61.11		C
ATOM	23	CD	GLN	A	3	3.756	−8.612	25.570	1.00	71.25		C
ATOM	24	NE2	GLN	A	3	4.265	−7.724	26.417	1.00	63.18		N
ATOM	25	OE1	GLN	A	3	4.299	−8.899	24.502	1.00	74.87		O
ATOM	26	N	LEU	A	4	−0.896	−11.035	23.298	1.00	33.31		N
ATOM	27	CA	LEU	A	4	−1.361	−11.577	22.025	1.00	32.23		C
ATOM	28	C	LEU	A	4	−1.077	−10.581	20.903	1.00	34.08		C
ATOM	29	O	LEU	A	4	−1.523	−9.436	20.954	1.00	35.79		O
ATOM	30	CB	LEU	A	4	−2.854	−11.904	22.076	1.00	24.96		C
ATOM	31	CG	LEU	A	4	−3.339	−12.906	23.123	1.00	35.14		C
ATOM	32	CD1	LEU	A	4	−4.849	−13.045	23.036	1.00	33.63		C
ATOM	33	CD2	LEU	A	4	−2.665	−14.259	22.950	1.00	36.57		C
ATOM	34	N	VAL	A	5	−0.333	−11.023	19.894	1.00	34.68		N
ATOM	35	CA	VAL	A	5	0.072	−10.150	18.794	1.00	31.10		C
ATOM	36	C	VAL	A	5	−0.418	−10.708	17.466	1.00	27.37		C
ATOM	37	O	VAL	A	5	−0.029	−11.804	17.061	1.00	33.78		O
ATOM	38	CB	VAL	A	5	1.603	−9.971	18.747	1.00	33.23		C
ATOM	39	CG1	VAL	A	5	2.000	−9.098	17.564	1.00	39.33		C
ATOM	40	CG2	VAL	A	5	2.107	−9.365	20.052	1.00	30.20		C
ATOM	41	N	GLN	A	6	−1.280	−9.951	16.792	1.00	27.57		N
ATOM	42	CA	GLN	A	6	−1.882	−10.411	15.545	1.00	31.03		C
ATOM	43	C	GLN	A	6	−1.155	−9.849	14.333	1.00	32.02		C
ATOM	44	O	GLN	A	6	−0.447	−8.847	14.431	1.00	31.18		O
ATOM	45	CB	GLN	A	6	−3.362	−10.026	15.492	1.00	23.97		C
ATOM	46	CG	GLN	A	6	−4.154	−10.551	16.674	1.00	31.59		C
ATOM	47	CD	GLN	A	6	−5.613	−10.158	16.634	1.00	31.89		C
ATOM	48	NE2	GLN	A	6	−6.203	−10.163	15.438	1.00	30.10		N
ATOM	49	OE1	GLN	A	6	−6.210	−9.863	17.669	1.00	28.34		O
ATOM	50	N	SER	A	7	−1.343	−10.498	13.190	1.00	28.18		N
ATOM	51	CA	SER	A	7	−0.769	−10.018	11.941	1.00	37.96		C
ATOM	52	C	SER	A	7	−1.529	−8.784	11.456	1.00	36.31		C
ATOM	53	O	SER	A	7	−2.504	−8.356	12.088	1.00	29.94		O
ATOM	54	CB	SER	A	7	−0.782	−11.125	10.884	1.00	31.07		C
ATOM	55	OG	SER	A	7	−2.003	−11.840	10.917	1.00	34.72		O
ATOM	56	N	GLY	A	8	−1.084	−8.220	10.336	1.00	37.68		N
ATOM	57	CA	GLY	A	8	−1.579	−6.932	9.880	1.00	34.93		C
ATOM	58	C	GLY	A	8	−2.778	−6.994	8.957	1.00	39.24		C
ATOM	59	O	GLY	A	8	−3.278	−8.071	8.641	1.00	43.54		O
ATOM	60	N	THR	A	9	−3.221	−5.818	8.519	1.00	33.12		N
ATOM	61	CA	THR	A	9	−4.417	−5.660	7.698	1.00	34.90		C
ATOM	62	C	THR	A	9	−4.411	−6.499	6.424	1.00	34.53		C
ATOM	63	O	THR	A	9	−3.369	−6.699	5.809	1.00	36.17		O
ATOM	64	CB	THR	A	9	−4.612	−4.186	7.290	1.00	34.99		C
ATOM	65	OG1	THR	A	9	−4.305	−3.333	8.400	1.00	54.03		O
ATOM	66	CG2	THR	A	9	−6.032	−3.948	6.877	1.00	25.09		C
ATOM	67	N	GLU	A	10	−5.591	−6.977	6.042	1.00	38.28		N
ATOM	68	CA	GLU	A	10	−5.770	−7.781	4.840	1.00	36.11		C
ATOM	69	C	GLU	A	10	−6.846	−7.183	3.942	1.00	42.38		C
ATOM	70	O	GLU	A	10	−7.825	−6.614	4.433	1.00	36.65		O
ATOM	71	CB	GLU	A	10	−6.156	−9.217	5.204	1.00	41.15		C
ATOM	72	CG	GLU	A	10	−5.177	−9.938	6.112	1.00	45.12		C
ATOM	73	CD	GLU	A	10	−4.128	−10.719	5.342	1.00	54.57		C
ATOM	74	OE1	GLU	A	10	−3.998	−10.501	4.118	1.00	60.79		O
ATOM	75	OE2	GLU	A	10	−3.438	−11.556	5.963	1.00	51.03		O
ATOM	76	N	VAL	A	11	−6.659	−7.314	2.630	1.00	33.01		N
ATOM	77	CA	VAL	A	11	−7.690	−6.970	1.654	1.00	35.41		C
ATOM	78	C	VAL	A	11	−7.886	−8.152	0.709	1.00	37.75		C
ATOM	79	O	VAL	A	11	−6.920	−8.678	0.153	1.00	40.66		O
ATOM	80	CB	VAL	A	11	−7.331	−5.718	0.826	1.00	41.44		C
ATOM	81	CG1	VAL	A	11	−8.587	−5.137	0.181	1.00	34.49		C
ATOM	82	CG2	VAL	A	11	−6.642	−4.681	1.692	1.00	43.75		C
ATOM	83	N	LYS	A	12	−9.133	−8.572	0.535	1.00	35.34		N
ATOM	84	CA	LYS	A	12	−9.430	−9.745	−0.276	1.00	34.88		C
ATOM	85	C	LYS	A	12	−10.619	−9.497	−1.196	1.00	41.54		C
ATOM	86	O	LYS	A	12	−11.503	−8.701	−0.881	1.00	37.51		O
ATOM	87	CB	LYS	A	12	−9.716	−10.958	0.618	1.00	37.30		C
ATOM	88	CG	LYS	A	12	−8.570	−11.375	1.529	1.00	31.97		C
ATOM	89	CD	LYS	A	12	−7.396	−11.926	0.737	1.00	39.11		C
ATOM	90	CE	LYS	A	12	−6.276	−12.372	1.664	1.00	40.25		C
ATOM	91	NZ	LYS	A	12	−5.084	−12.848	0.910	1.00	43.21		N
ATOM	92	N	LYS	A	13	−10.641	−10.186	−2.332	1.00	40.85		N
ATOM	93	CA	LYS	A	13	−11.800	−10.147	−3.217	1.00	46.07		C
ATOM	94	C	LYS	A	13	−12.873	−11.095	−2.687	1.00	41.63		C
ATOM	95	O	LYS	A	13	−12.557	−12.058	−1.991	1.00	42.80		O
ATOM	96	CB	LYS	A	13	−11.401	−10.525	−4.646	1.00	44.49		C
ATOM	97	CG	LYS	A	13	−10.368	−9.597	−5.262	1.00	51.17		C
ATOM	98	CD	LYS	A	13	−10.037	−10.015	−6.686	1.00	69.57		C
ATOM	99	CE	LYS	A	13	−9.093	−9.026	−7.351	1.00	76.15		C
ATOM	100	NZ	LYS	A	13	−8.805	−9.405	−8.763	1.00	81.80		N
ATOM	101	N	PRO	A	14	−14.149	−10.815	−2.992	1.00	40.61		N
ATOM	102	CA	PRO	A	14	−15.210	−11.741	−2.581	1.00	42.09		C
ATOM	103	C	PRO	A	14	−14.959	−13.147	−3.124	1.00	43.49		C
ATOM	104	O	PRO	A	14	−14.532	−13.286	−4.268	1.00	43.97		O
ATOM	105	CB	PRO	A	14	−16.474	−11.125	−3.191	1.00	41.78		C
ATOM	106	CG	PRO	A	14	−16.153	−9.669	−3.327	1.00	42.84		C
ATOM	107	CD	PRO	A	14	−14.683	−9.605	−3.641	1.00	40.32		C
ATOM	108	N	GLY	A	15	−15.191	−14.166	−2.302	1.00	44.15		N
ATOM	109	CA	GLY	A	15	−14.989	−15.542	−2.716	1.00	39.13		C
ATOM	110	C	GLY	A	15	−13.611	−16.090	−2.391	1.00	48.08		C
ATOM	111	O	GLY	A	15	−13.385	−17.297	−2.469	1.00	45.50		O
ATOM	112	N	ALA	A	16	−12.683	−15.208	−2.028	1.00	41.49		N
ATOM	113	CA	ALA	A	16	−11.334	−15.636	−1.665	1.00	40.38		C
ATOM	114	C	ALA	A	16	−11.263	−16.095	−0.209	1.00	44.65		C
ATOM	115	O	ALA	A	16	−12.281	−16.184	0.478	1.00	39.46		O
ATOM	116	CB	ALA	A	16	−10.340	−14.512	−1.908	1.00	42.69		C
ATOM	117	N	SER	A	17	−10.052	−16.383	0.257	1.00	41.27		N
ATOM	118	C	SER	A	17	−8.822	−15.906	2.328	1.00	41.94		C
ATOM	119	O	SER	A	17	−7.925	−15.363	1.688	1.00	46.41		O
ATOM	120	CA	ASER	A	17	−9.841	−16.800	1.638	0.70	41.50		C
ATOM	121	CB	ASER	A	17	−9.382	−18.258	1.699	0.70	42.17		C
ATOM	122	OG	ASER	A	17	−10.402	−19.130	1.247	0.70	48.56		O
ATOM	123	CA	BSER	A	17	−9.844	−16.800	1.638	0.30	41.51		C
ATOM	124	CB	BSER	A	17	−9.387	−18.259	1.703	0.30	42.20		C
ATOM	125	OG	BSER	A	17	−8.050	−18.394	1.253	0.30	38.89		O
ATOM	126	N	VAL	A	18	−8.963	−15.760	3.639	1.00	40.15		N
ATOM	127	CA	VAL	A	18	−8.023	−14.966	4.414	1.00	37.97		C
ATOM	128	C	VAL	A	18	−7.539	−15.771	5.615	1.00	36.78		C
ATOM	129	O	VAL	A	18	−8.313	−16.499	6.237	1.00	43.11		O
ATOM	130	CB	VAL	A	18	−8.657	−13.636	4.879	1.00	39.97		C
ATOM	131	CG1	VAL	A	18	−9.911	−13.893	5.706	1.00	34.36		C
ATOM	132	CG2	VAL	A	18	−7.651	−12.802	5.661	1.00	41.62		C
ATOM	133	N	LYS	A	19	−6.251	−15.664	5.921	1.00	39.92		N
ATOM	134	CA	LYS	A	19	−5.706	−16.304	7.110	1.00	40.61		C
ATOM	135	C	LYS	A	19	−5.015	−15.279	8.012	1.00	41.01		C
ATOM	136	O	LYS	A	19	−4.067	−14.610	7.599	1.00	42.89		O
ATOM	137	CB	LYS	A	19	−4.737	−17.424	6.731	1.00	38.22		C
ATOM	138	CG	LYS	A	19	−4.105	−18.105	7.932	1.00	35.23		C
ATOM	139	CD	LYS	A	19	−3.153	−19.219	7.527	1.00	37.78		C
ATOM	140	CE	LYS	A	19	−3.892	−20.532	7.324	1.00	52.29		C
ATOM	141	NZ	LYS	A	19	−2.953	−21.693	7.310	1.00	57.68		N
ATOM	142	N	VAL	A	20	−5.511	−15.165	9.241	1.00	38.03		N
ATOM	143	CA	VAL	A	20	−4.982	−14.234	10.235	1.00	34.63		C
ATOM	144	C	VAL	A	20	−4.240	−15.005	11.332	1.00	39.64		C
ATOM	145	O	VAL	A	20	−4.658	−16.099	11.720	1.00	36.81		O
ATOM	146	CB	VAL	A	20	−6.115	−13.388	10.867	1.00	33.08		C
ATOM	147	CG1	VAL	A	20	−5.553	−12.359	11.839	1.00	39.43		C
ATOM	148	CG2	VAL	A	20	−6.941	−12.707	9.784	1.00	38.82		C
ATOM	149	N	SER	A	21	−3.144	−14.439	11.832	1.00	30.21		N
ATOM	150	CA	SER	A	21	−2.338	−15.124	12.838	1.00	32.22		C
ATOM	151	C	SER	A	21	−2.354	−14.384	14.168	1.00	34.12		C
ATOM	152	O	SER	A	21	−2.566	−13.176	14.218	1.00	32.94		O
ATOM	153	CB	SER	A	21	−0.892	−15.289	12.354	1.00	32.38		C
ATOM	154	OG	SER	A	21	−0.205	−14.046	12.353	1.00	35.31		O
ATOM	155	N	CYS	A	22	−2.116	−15.123	15.244	1.00	36.35		N
ATOM	156	CA	CYS	A	22	−2.109	−14.565	16.587	1.00	33.43		C
ATOM	157	C	CYS	A	22	−0.985	−15.204	17.401	1.00	38.78		C
ATOM	158	O	CYS	A	22	−1.059	−16.380	17.757	1.00	39.38		O
ATOM	159	CB	CYS	A	22	−3.468	−14.791	17.260	1.00	38.36		C
ATOM	160	SG	CYS	A	22	−3.592	−14.210	18.969	1.00	47.87		S
ATOM	161	N	LYS	A	23	0.064	−14.440	17.681	1.00	37.86		N
ATOM	162	CA	LYS	A	23	1.207	−14.980	18.410	1.00	40.02		C
ATOM	163	C	LYS	A	23	1.019	−14.817	19.912	1.00	36.84		C
ATOM	164	O	LYS	A	23	0.925	−13.697	20.415	1.00	38.22		O
ATOM	165	CB	LYS	A	23	2.506	−14.303	17.966	1.00	40.53		C
ATOM	166	CG	LYS	A	23	3.763	−15.022	18.446	1.00	49.89		C
ATOM	167	CD	LYS	A	23	5.015	−14.206	18.167	1.00	49.82		C
ATOM	168	CE	LYS	A	23	6.195	−15.104	17.823	1.00	63.34		C
ATOM	169	NZ	LYS	A	23	6.392	−16.183	18.827	1.00	59.88		N
ATOM	170	N	ALA	A	24	0.960	−15.940	20.621	1.00	39.67		N
ATOM	171	CA	ALA	A	24	0.756	−15.929	22.066	1.00	44.74		C
ATOM	172	C	ALA	A	24	2.070	−16.103	22.819	1.00	52.29		C
ATOM	173	O	ALA	A	24	2.952	−16.844	22.390	1.00	57.40		O
ATOM	174	CB	ALA	A	24	−0.227	−17.014	22.468	1.00	43.19		C
ATOM	175	N	SER	A	25	2.193	−15.416	23.949	1.00	49.70		N
ATOM	176	CA	SER	A	25	3.390	−15.511	24.771	1.00	51.40		C
ATOM	177	C	SER	A	25	3.108	−15.073	26.206	1.00	52.18		C
ATOM	178	O	SER	A	25	2.195	−14.282	26.449	1.00	44.33		O
ATOM	179	CB	SER	A	25	4.513	−14.665	24.171	1.00	54.47		C
ATOM	180	OG	SER	A	25	4.108	−13.314	24.022	1.00	61.15		O
ATOM	181	N	GLY	A	26	3.887	−15.597	27.149	1.00	43.62		N
ATOM	182	CA	GLY	A	26	3.797	−15.182	28.539	1.00	42.96		C
ATOM	183	C	GLY	A	26	2.914	−16.042	29.429	1.00	47.24		C
ATOM	184	O	GLY	A	26	2.711	−15.718	30.599	1.00	47.28		O
ATOM	185	N	TYR	A	27	2.388	−17.136	28.889	1.00	41.19		N
ATOM	186	CA	TYR	A	27	1.504	−18.006	29.657	1.00	39.91		C
ATOM	187	C	TYR	A	27	2.259	−18.809	30.704	1.00	53.27		C
ATOM	188	O	TYR	A	27	3.307	−19.393	30.423	1.00	48.93		O
ATOM	189	CB	TYR	A	27	0.740	−18.956	28.733	1.00	48.01		C
ATOM	190	CG	TYR	A	27	−0.376	−18.280	27.978	1.00	52.64		C
ATOM	191	CD2	TYR	A	27	−0.151	−17.727	26.726	1.00	45.16		C
ATOM	192	CD1	TYR	A	27	−1.655	−18.180	28.526	1.00	47.65		C
ATOM	193	CE2	TYR	A	27	−1.163	−17.099	26.032	1.00	50.12		C
ATOM	194	CE1	TYR	A	27	−2.678	−17.555	27.837	1.00	41.89		C
ATOM	195	CZ	TYR	A	27	−2.422	−17.015	26.590	1.00	49.26		C
ATOM	196	OH	TYR	A	27	−3.417	−16.385	25.887	1.00	50.17		O
ATOM	197	N	THR	A	28	1.705	−18.844	31.910	1.00	55.54		N
ATOM	198	CA	THR	A	28	2.345	−19.511	33.035	1.00	52.97		C
ATOM	199	C	THR	A	28	1.695	−20.867	33.330	1.00	58.74		C
ATOM	200	O	THR	A	28	2.080	−21.560	34.275	1.00	53.17		O
ATOM	201	CB	THR	A	28	2.301	−18.622	34.297	1.00	45.57		C
ATOM	202	CG2	THR	A	28	0.870	−18.237	34.629	1.00	50.36		C
ATOM	203	OG1	THR	A	28	2.873	−19.326	35.405	1.00	80.42		O
ATOM	204	O	PHE	A	29	−0.347	−22.422	30.294	1.00	42.50		O
ATOM	205	N	PHE	A	29	0.711	−21.242	32.516	1.00	52.37		N
ATOM	206	CA	PHE	A	29	0.048	−22.536	32.661	1.00	40.27		C
ATOM	207	C	PHE	A	29	−0.288	−23.133	31.297	1.00	41.00		C
ATOM	208	CB	PHE	A	29	−1.216	−22.409	33.519	1.00	44.95		C
ATOM	209	CG	PHE	A	29	−2.147	−21.312	33.081	1.00	42.97		C
ATOM	210	CD2	PHE	A	29	−2.146	−20.087	33.728	1.00	44.83		C
ATOM	211	CD1	PHE	A	29	−3.034	−21.512	32.034	1.00	41.74		C
ATOM	212	CE2	PHE	A	29	−3.005	−19.077	33.334	1.00	49.55		C
ATOM	213	CE1	PHE	A	29	−3.893	−20.508	31.635	1.00	43.96		C
ATOM	214	CZ	PHE	A	29	−3.879	−19.287	32.286	1.00	50.75		C
ATOM	215	O	THR	A	30	−1.919	−25.101	28.021	1.00	42.53		O
ATOM	216	N	THR	A	30	−0.530	−24.439	31.272	1.00	40.36		N
ATOM	217	CA	THR	A	30	−0.586	−25.179	30.016	1.00	42.39		C
ATOM	218	C	THR	A	30	−1.914	−25.074	29.255	1.00	42.49		C
ATOM	219	CB	THR	A	30	−0.281	−26.682	30.251	1.00	43.93		C
ATOM	220	OG1	THR	A	30	−1.295	−27.254	31.083	1.00	62.78		O
ATOM	221	CG2	THR	A	30	1.071	−26.857	30.923	1.00	45.80		C
ATOM	222	O	ASN	A	31	−5.415	−23.080	30.210	1.00	32.62		O
ATOM	223	N	ASN	A	31	−3.035	−24.959	29.965	1.00	33.58		N
ATOM	224	CA	ASN	A	31	−4.334	−25.021	29.288	1.00	29.92		C
ATOM	225	C	ASN	A	31	−5.085	−23.699	29.201	1.00	35.69		C
ATOM	226	CB	ASN	A	31	−5.230	−26.055	29.963	1.00	36.07		C
ATOM	227	CG	ASN	A	31	−4.646	−27.449	29.903	1.00	37.13		C
ATOM	228	OD1	ASN	A	31	−4.449	−28.006	28.821	1.00	32.81		O
ATOM	229	ND2	ASN	A	31	−4.361	−28.018	31.066	1.00	28.91		N
ATOM	230	N	TYR	A	32	−5.354	−23.289	27.968	1.00	31.28		N
ATOM	231	CA	TYR	A	32	−6.159	−22.112	27.677	1.00	34.89		C
ATOM	232	C	TYR	A	32	−6.695	−22.261	26.258	1.00	37.67		C
ATOM	233	O	TYR	A	32	−6.197	−23.085	25.491	1.00	29.11		O
ATOM	234	CB	TYR	A	32	−5.339	−20.825	27.826	1.00	30.61		C
ATOM	235	CG	TYR	A	32	−4.090	−20.799	26.970	1.00	42.67		C
ATOM	236	CD1	TYR	A	32	−2.900	−21.355	27.425	1.00	39.54		C
ATOM	237	CD2	TYR	A	32	−4.101	−20.225	25.704	1.00	38.42		C
ATOM	238	CE1	TYR	A	32	−1.758	−21.341	26.643	1.00	41.78		C
ATOM	239	CE2	TYR	A	32	−2.962	−20.206	24.921	1.00	42.06		C
ATOM	240	CZ	TYR	A	32	−1.797	−20.765	25.393	1.00	47.23		C
ATOM	241	OH	TYR	A	32	−0.666	−20.741	24.609	1.00	56.16		O
ATOM	242	N	ASP	A	33	−7.716	−21.482	25.919	1.00	30.49		N
ATOM	243	CA	ASP	A	33	−8.271	−21.484	24.570	1.00	29.65		C
ATOM	244	C	ASP	A	33	−7.998	−20.161	23.883	1.00	31.10		C
ATOM	245	O	ASP	A	33	−8.062	−19.113	24.513	1.00	28.34		O
ATOM	246	CB	ASP	A	33	−9.779	−21.734	24.591	1.00	29.08		C
ATOM	247	CG	ASP	A	33	−10.139	−23.124	25.082	1.00	34.81		C
ATOM	248	OD1	ASP	A	33	−9.427	−24.090	24.729	1.00	31.12		O
ATOM	249	OD2	ASP	A	33	−11.145	−23.247	25.814	1.00	30.55		O
ATOM	250	N	ILE	A	34	−7.685	−20.204	22.593	1.00	28.80		N
ATOM	251	CA	ILE	A	34	−7.698	−18.989	21.801	1.00	29.45		C
ATOM	252	C	ILE	A	34	−9.070	−18.897	21.155	1.00	28.08		C
ATOM	253	O	ILE	A	34	−9.518	−19.838	20.500	1.00	32.08		O
ATOM	254	CB	ILE	A	34	−6.587	−18.954	20.729	1.00	34.02		C
ATOM	255	CG1	ILE	A	34	−5.301	−18.380	21.315	1.00	40.10		C
ATOM	256	CG2	ILE	A	34	−6.981	−18.048	19.581	1.00	33.89		C
ATOM	257	CD1	ILE	A	34	−4.555	−19.327	22.160	1.00	37.52		C
ATOM	258	N	ASN	A	35	−9.743	−17.774	21.381	1.00	23.45		N
ATOM	259	CA	ASN	A	35	−11.044	−17.502	20.786	1.00	28.14		C
ATOM	260	C	ASN	A	35	−10.911	−16.447	19.693	1.00	30.81		C
ATOM	261	O	ASN	A	35	−10.013	−15.607	19.733	1.00	33.76		O
ATOM	262	CB	ASN	A	35	−12.045	−17.023	21.849	1.00	30.44		C
ATOM	263	CG	ASN	A	35	−12.218	−18.015	22.989	1.00	30.22		C
ATOM	264	OD1	ASN	A	35	−13.183	−18.779	23.018	1.00	29.29		O
ATOM	265	ND2	ASN	A	35	−11.293	−17.995	23.943	1.00	26.20		N
ATOM	266	N	TRP	A	36	−11.802	−16.482	18.715	1.00	28.47		N
ATOM	267	CA	TRP	A	36	−11.807	−15.447	17.697	1.00	32.59		C
ATOM	268	C	TRP	A	36	−13.139	−14.720	17.718	1.00	32.65		C
ATOM	269	O	TRP	A	36	−14.202	−15.337	17.703	1.00	30.35		O
ATOM	270	CB	TRP	A	36	−11.509	−16.038	16.318	1.00	30.51		C
ATOM	271	CG	TRP	A	36	−10.106	−16.553	16.242	1.00	27.75		C
ATOM	272	CD1	TRP	A	36	−9.665	−17.781	16.637	1.00	28.80		C
ATOM	273	CD2	TRP	A	36	−8.951	−15.840	15.779	1.00	33.27		C
ATOM	274	CE2	TRP	A	36	−7.847	−16.707	15.906	1.00	31.39		C
ATOM	275	CE3	TRP	A	36	−8.745	−14.557	15.260	1.00	31.98		C
ATOM	276	NE1	TRP	A	36	−8.309	−17.884	16.434	1.00	36.72		N
ATOM	277	CZ2	TRP	A	36	−6.554	−16.334	15.535	1.00	38.10		C
ATOM	278	CZ3	TRP	A	36	−7.457	−14.186	14.890	1.00	30.43		C
ATOM	279	CH2	TRP	A	36	−6.380	−15.071	15.030	1.00	33.42		C
ATOM	280	N	VAL	A	37	−13.053	−13.397	17.790	1.00	27.11		N
ATOM	281	CA	VAL	A	37	−14.207	−12.528	17.936	1.00	30.57		C
ATOM	282	C	VAL	A	37	−14.076	−11.410	16.914	1.00	33.89		C
ATOM	283	O	VAL	A	37	−13.032	−10.759	16.846	1.00	33.58		O
ATOM	284	CB	VAL	A	37	−14.301	−11.929	19.370	1.00	25.89		C
ATOM	285	CG1	VAL	A	37	−15.467	−10.957	19.478	1.00	27.13		C
ATOM	286	CG2	VAL	A	37	−14.423	−13.031	20.417	1.00	26.86		C
ATOM	287	N	ARG	A	38	−15.116	−11.188	16.115	1.00	29.31		N
ATOM	288	CA	ARG	A	38	−15.054	−10.150	15.088	1.00	28.87		C
ATOM	289	C	ARG	A	38	−16.002	−8.995	15.395	1.00	32.02		C
ATOM	290	O	ARG	A	38	−17.005	−9.163	16.089	1.00	30.64		O
ATOM	291	CB	ARG	A	38	−15.367	−10.732	13.708	1.00	35.52		C
ATOM	292	CG	ARG	A	38	−16.652	−11.529	13.656	1.00	39.93		C
ATOM	293	CD	ARG	A	38	−17.550	−11.096	12.506	1.00	43.60		C
ATOM	294	NE	ARG	A	38	−17.164	−11.681	11.229	1.00	44.71		N
ATOM	295	CZ	ARG	A	38	−18.023	−12.119	10.311	1.00	45.96		C
ATOM	296	NH1	ARG	A	38	−19.329	−12.055	10.529	1.00	39.60		N
ATOM	297	NH2	ARG	A	38	−17.572	−12.626	9.170	1.00	33.94		N
ATOM	298	N	GLN	A	39	−15.669	−7.821	14.871	1.00	30.63		N
ATOM	299	CA	GLN	A	39	−16.452	−6.618	15.103	1.00	28.53		C
ATOM	300	C	GLN	A	39	−16.568	−5.795	13.825	1.00	31.84		C
ATOM	301	O	GLN	A	39	−15.569	−5.314	13.294	1.00	29.51		O
ATOM	302	CB	GLN	A	39	−15.819	−5.775	16.219	1.00	30.14		C
ATOM	303	CG	GLN	A	39	−16.516	−4.444	16.478	1.00	28.25		C
ATOM	304	CD	GLN	A	39	−16.024	−3.781	17.751	1.00	39.30		C
ATOM	305	NE2	GLN	A	39	−16.896	−3.689	18.751	1.00	30.37		N
ATOM	306	OE1	GLN	A	39	−14.870	−3.368	17.839	1.00	39.08		O
ATOM	307	N	ALA	A	40	−17.788	−5.637	13.330	1.00	37.04		N
ATOM	308	CA	ALA	A	40	−18.016	−4.815	12.149	1.00	44.35		C
ATOM	309	C	ALA	A	40	−18.259	−3.363	12.548	1.00	49.15		C
ATOM	310	O	ALA	A	40	−18.880	−3.094	13.579	1.00	49.51		O
ATOM	311	CB	ALA	A	40	−19.190	−5.352	11.341	1.00	36.53		C
ATOM	312	N	THR	A	41	−17.768	−2.444	11.715	1.00	55.43		N
ATOM	313	CA	THR	A	41	−17.923	−0.987	11.865	1.00	45.13		C
ATOM	314	C	THR	A	41	−17.917	−0.449	13.304	1.00	61.05		C
ATOM	315	O	THR	A	41	−18.779	0.345	13.688	1.00	60.70		O
ATOM	316	CB	THR	A	41	−19.224	−0.480	11.157	1.00	56.54		C
ATOM	317	OG1	THR	A	41	−19.398	0.918	11.416	1.00	74.65		O
ATOM	318	CG2	THR	A	41	−20.475	−1.233	11.611	1.00	50.35		C
ATOM	319	N	GLY	A	42	−16.931	−0.880	14.088	1.00	60.31		N
ATOM	320	CA	GLY	A	42	−16.677	−0.311	15.402	1.00	50.20		C
ATOM	321	C	GLY	A	42	−17.674	−0.603	16.515	1.00	58.90		C
ATOM	322	O	GLY	A	42	−17.496	−0.125	17.638	1.00	64.22		O
ATOM	323	N	GLN	A	43	−18.718	−1.377	16.225	1.00	61.17		N
ATOM	324	CA	GLN	A	43	−19.700	−1.716	17.255	1.00	58.73		C
ATOM	325	C	GLN	A	43	−20.368	−3.072	17.007	1.00	47.27		C
ATOM	326	O	GLN	A	43	−20.811	−3.369	15.897	1.00	54.96		O
ATOM	327	CB	GLN	A	43	−20.761	−0.613	17.362	1.00	57.68		C
ATOM	328	CG	GLN	A	43	−21.613	−0.690	18.627	1.00	55.99		C
ATOM	329	CD	GLN	A	43	−22.130	0.669	19.075	1.00	60.55		C
ATOM	330	NE2	GLN	A	43	−21.668	1.727	18.416	1.00	61.26		N
ATOM	331	OE1	GLN	A	43	−22.929	0.765	20.007	1.00	62.03		O
ATOM	332	N	GLY	A	44	−20.438	−3.885	18.059	1.00	52.11		N
ATOM	333	CA	GLY	A	44	−21.017	−5.215	17.978	1.00	38.87		C
ATOM	334	C	GLY	A	44	−19.946	−6.290	17.933	1.00	40.89		C
ATOM	335	O	GLY	A	44	−19.033	−6.225	17.115	1.00	48.89		O
ATOM	336	N	LEU	A	45	−20.051	−7.281	18.811	1.00	28.02		N
ATOM	337	CA	LEU	A	45	−19.065	−8.355	18.862	1.00	32.48		C
ATOM	338	C	LEU	A	45	−19.726	−9.703	18.639	1.00	29.29		C
ATOM	339	O	LEU	A	45	−20.768	−9.993	19.226	1.00	35.37		O
ATOM	340	CB	LEU	A	45	−18.331	−8.345	20.209	1.00	30.66		C
ATOM	341	CG	LEU	A	45	−17.553	−7.072	20.561	1.00	31.07		C
ATOM	342	CD1	LEU	A	45	−17.379	−6.937	22.068	1.00	32.58		C
ATOM	343	CD2	LEU	A	45	−16.198	−7.075	19.873	1.00	29.40		C
ATOM	344	N	GLU	A	46	−19.140	−10.533	17.785	1.00	29.17		N
ATOM	345	CA	GLU	A	46	−19.639	−11.895	17.673	1.00	35.62		C
ATOM	346	C	GLU	A	46	−18.513	−12.920	17.699	1.00	35.22		C
ATOM	347	O	GLU	A	46	−17.496	−12.798	17.009	1.00	32.17		O
ATOM	348	CB	GLU	A	46	−20.511	−12.072	16.421	1.00	37.90		C
ATOM	349	CG	GLU	A	46	−19.828	−11.914	15.092	1.00	47.11		C
ATOM	350	CD	GLU	A	46	−20.765	−12.211	13.925	1.00	55.52		C
ATOM	351	OE1	GLU	A	46	−21.675	−13.052	14.087	1.00	54.51		O
ATOM	352	OE2	GLU	A	46	−20.601	−11.595	12.850	1.00	58.10		O
ATOM	353	N	TRP	A	47	−18.732	−13.926	18.536	1.00	32.28		N
ATOM	354	CA	TRP	A	47	−17.800	−15.012	18.788	1.00	36.07		C
ATOM	355	C	TRP	A	47	−17.838	−16.016	17.641	1.00	34.08		C
ATOM	356	O	TRP	A	47	−18.910	−16.392	17.169	1.00	29.79		O
ATOM	357	CB	TRP	A	47	−18.166	−15.664	20.121	1.00	25.80		C
ATOM	358	CG	TRP	A	47	−17.311	−16.791	20.594	1.00	33.81		C
ATOM	359	CD1	TRP	A	47	−16.096	−16.703	21.210	1.00	32.06		C
ATOM	360	CD2	TRP	A	47	−17.644	−18.182	20.562	1.00	33.38		C
ATOM	361	CE2	TRP	A	47	−16.572	−18.882	21.149	1.00	34.18		C
ATOM	362	CE3	TRP	A	47	−18.740	−18.904	20.079	1.00	35.50		C
ATOM	363	NE1	TRP	A	47	−15.638	−17.957	21.536	1.00	29.56		N
ATOM	364	CZ2	TRP	A	47	−16.565	−20.271	21.268	1.00	31.56		C
ATOM	365	CZ3	TRP	A	47	−18.729	−20.282	20.196	1.00	42.35		C
ATOM	366	CH2	TRP	A	47	−17.647	−20.950	20.787	1.00	34.97		C
ATOM	367	N	MET	A	48	−16.668	−16.437	17.179	1.00	32.09		N
ATOM	368	CA	MET	A	48	−16.596	−17.326	16.028	1.00	30.89		C
ATOM	369	C	MET	A	48	−16.261	−18.755	16.429	1.00	29.94		C
ATOM	370	O	MET	A	48	−16.653	−19.705	15.757	1.00	33.43		O
ATOM	371	CB	MET	A	48	−15.558	−16.823	15.028	1.00	28.48		C
ATOM	372	CG	MET	A	48	−15.790	−15.409	14.538	1.00	33.13		C
ATOM	373	SD	MET	A	48	−14.488	−14.924	13.396	1.00	37.93		S
ATOM	374	CE	MET	A	48	−14.665	−16.165	12.119	1.00	39.94		C
ATOM	375	N	GLY	A	49	−15.511	−18.908	17.511	1.00	33.42		N
ATOM	376	CA	GLY	A	49	−15.128	−20.234	17.955	1.00	33.05		C
ATOM	377	C	GLY	A	49	−13.878	−20.244	18.806	1.00	34.29		C
ATOM	378	O	GLY	A	49	−13.256	−19.202	19.031	1.00	34.24		O
ATOM	379	N	TRP	A	50	−13.509	−21.429	19.279	1.00	30.14		N
ATOM	380	CA	TRP	A	50	−12.368	−21.562	20.176	1.00	27.60		C
ATOM	381	C	TRP	A	50	−11.393	−22.619	19.679	1.00	36.00		C
ATOM	382	O	TRP	A	50	−11.758	−23.513	18.915	1.00	26.22		O
ATOM	383	CB	TRP	A	50	−12.833	−21.906	21.595	1.00	27.32		C
ATOM	384	CG	TRP	A	50	−13.525	−23.240	21.714	1.00	31.33		C
ATOM	385	CD1	TRP	A	50	−14.867	−23.479	21.627	1.00	31.09		C
ATOM	386	CD2	TRP	A	50	−12.907	−24.513	21.952	1.00	32.23		C
ATOM	387	CE2	TRP	A	50	−13.936	−25.476	21.994	1.00	36.04		C
ATOM	388	CE3	TRP	A	50	−11.583	−24.932	22.133	1.00	35.42		C
ATOM	389	NE1	TRP	A	50	−15.122	−24.819	21.791	1.00	30.64		N
ATOM	390	CZ2	TRP	A	50	−13.684	−26.834	22.208	1.00	34.17		C
ATOM	391	CZ3	TRP	A	50	−11.334	−26.282	22.347	1.00	33.78		C
ATOM	392	CH2	TRP	A	50	−12.379	−27.215	22.381	1.00	34.68		C
ATOM	393	N	MET	A	51	−10.147	−22.507	20.120	1.00	29.16		N
ATOM	394	CA	MET	A	51	−9.148	−23.507	19.807	1.00	28.07		C
ATOM	395	C	MET	A	51	−8.191	−23.679	20.975	1.00	31.55		C
ATOM	396	O	MET	A	51	−7.728	−22.696	21.553	1.00	33.21		O
ATOM	397	CB	MET	A	51	−8.374	−23.130	18.549	1.00	31.45		C
ATOM	398	CG	MET	A	51	−7.420	−24.221	18.093	1.00	37.56		C
ATOM	399	SD	MET	A	51	−5.818	−23.586	17.594	1.00	57.24		S
ATOM	400	CE	MET	A	51	−5.222	−22.920	19.142	1.00	46.36		C
ATOM	401	N	HIS	A	52	−7.902	−24.935	21.305	1.00	27.88		N
ATOM	402	CA	HIS	A	52	−6.991	−25.294	22.391	1.00	35.15		C
ATOM	403	C	HIS	A	52	−5.615	−25.621	21.816	1.00	35.88		C
ATOM	404	O	HIS	A	52	−5.449	−26.650	21.169	1.00	39.53		O
ATOM	405	CB	HIS	A	52	−7.557	−26.491	23.173	1.00	31.19		C
ATOM	406	CG	HIS	A	52	−6.737	−26.899	24.362	1.00	32.88		C
ATOM	407	CD2	HIS	A	52	−6.353	−26.213	25.462	1.00	35.83		C
ATOM	408	ND1	HIS	A	52	−6.248	−28.180	24.520	1.00	33.47		N
ATOM	409	CE1	HIS	A	52	−5.585	−28.258	25.660	1.00	32.93		C
ATOM	410	NE2	HIS	A	52	−5.631	−27.080	26.252	1.00	33.96		N
ATOM	411	N	PRO	A	53	−4.629	−24.737	22.035	1.00	36.74		N
ATOM	412	CA	PRO	A	53	−3.284	−24.901	21.465	1.00	41.48		C
ATOM	413	C	PRO	A	53	−2.619	−26.232	21.802	1.00	43.82		C
ATOM	414	O	PRO	A	53	−1.959	−26.811	20.941	1.00	42.27		O
ATOM	415	CB	PRO	A	53	−2.497	−23.744	22.088	1.00	37.52		C
ATOM	416	CG	PRO	A	53	−3.521	−22.710	22.372	1.00	42.21		C
ATOM	417	CD	PRO	A	53	−4.768	−23.456	22.751	1.00	37.85		C
ATOM	418	N	ASN	A	54	−2.795	−26.709	23.029	1.00	40.74		N
ATOM	419	CA	ASN	A	54	−2.088	−27.903	23.482	1.00	40.42		C
ATOM	420	C	ASN	A	54	−2.575	−29.192	22.814	1.00	44.96		C
ATOM	421	O	ASN	A	54	−1.848	−30.184	22.781	1.00	53.00		O
ATOM	422	CB	ASN	A	54	−2.201	−28.035	25.003	1.00	41.59		C
ATOM	423	CG	ASN	A	54	−0.988	−28.704	25.620	1.00	48.60		C
ATOM	424	ND2	ASN	A	54	−1.220	−29.565	26.607	1.00	49.53		N
ATOM	425	OD1	ASN	A	54	0.146	−28.456	25.208	1.00	54.90		O
ATOM	426	N	SER	A	55	−3.792	−29.179	22.276	1.00	41.51		N
ATOM	427	CA	SER	A	55	−4.354	−30.372	21.641	1.00	39.42		C
ATOM	428	C	SER	A	55	−4.800	−30.137	20.196	1.00	45.89		C
ATOM	429	O	SER	A	55	−4.958	−31.083	19.428	1.00	45.29		O
ATOM	430	CB	SER	A	55	−5.544	−30.886	22.444	1.00	40.90		C
ATOM	431	OG	SER	A	55	−6.661	−30.030	22.269	1.00	41.20		O
ATOM	432	N	GLY	A	56	−5.020	−28.878	19.831	1.00	39.03		N
ATOM	433	CA	GLY	A	56	−5.491	−28.550	18.497	1.00	34.31		C
ATOM	434	C	GLY	A	56	−6.992	−28.707	18.348	1.00	33.47		C
ATOM	435	O	GLY	A	56	−7.551	−28.402	17.298	1.00	35.63		O
ATOM	436	N	ASN	A	57	−7.649	−29.185	19.401	1.00	32.07		N
ATOM	437	CA	ASN	A	57	−9.099	−29.323	19.384	1.00	35.35		C
ATOM	438	C	ASN	A	57	−9.792	−27.972	19.257	1.00	35.99		C
ATOM	439	O	ASN	A	57	−9.298	−26.956	19.753	1.00	31.96		O
ATOM	440	CB	ASN	A	57	−9.585	−30.042	20.638	1.00	36.70		C
ATOM	441	CG	ASN	A	57	−9.149	−31.490	20.679	1.00	51.73		C
ATOM	442	OD1	ASN	A	57	−8.193	−31.882	20.005	1.00	51.72		O
ATOM	443	ND2	ASN	A	57	−9.851	−32.297	21.467	1.00	40.02		N
ATOM	444	N	THR	A	58	−10.938	−27.966	18.585	1.00	32.70		N
ATOM	445	CA	THR	A	58	−11.657	−26.728	18.315	1.00	34.35		C
ATOM	446	C	THR	A	58	−13.149	−26.874	18.543	1.00	36.07		C
ATOM	447	O	THR	A	58	−13.664	−27.985	18.682	1.00	35.59		O
ATOM	448	CB	THR	A	58	−11.463	−26.251	16.859	1.00	35.50		C
ATOM	449	CG2	THR	A	58	−9.986	−26.209	16.474	1.00	29.82		C
ATOM	450	OG1	THR	A	58	−12.167	−27.132	15.976	1.00	34.89		O
ATOM	451	N	GLY	A	59	−13.833	−25.735	18.563	1.00	34.36		N
ATOM	452	CA	GLY	A	59	−15.283	−25.682	18.542	1.00	31.26		C
ATOM	453	C	GLY	A	59	−15.712	−24.404	17.843	1.00	36.02		C
ATOM	454	O	GLY	A	59	−15.268	−23.319	18.214	1.00	34.77		O
ATOM	455	N	TYR	A	60	−16.561	−24.528	16.826	1.00	38.85		N
ATOM	456	CA	TYR	A	60	−17.004	−23.374	16.045	1.00	36.79		C
ATOM	457	C	TYR	A	60	−18.467	−23.041	16.310	1.00	43.76		C
ATOM	458	O	TYR	A	60	−19.269	−23.933	16.581	1.00	40.31		O
ATOM	459	CB	TYR	A	60	−16.818	−23.630	14.546	1.00	40.99		C
ATOM	460	CG	TYR	A	60	−15.446	−24.123	14.157	1.00	40.11		C
ATOM	461	CD1	TYR	A	60	−14.305	−23.583	14.729	1.00	37.87		C
ATOM	462	CD2	TYR	A	60	−15.292	−25.132	13.213	1.00	40.09		C
ATOM	463	CE1	TYR	A	60	−13.050	−24.031	14.374	1.00	39.91		C
ATOM	464	CE2	TYR	A	60	−14.037	−25.587	12.851	1.00	40.87		C
ATOM	465	CZ	TYR	A	60	−12.920	−25.030	13.436	1.00	42.40		C
ATOM	466	OH	TYR	A	60	−11.666	−25.467	13.091	1.00	41.60		O
ATOM	467	N	ALA	A	61	−18.816	−21.760	16.223	1.00	32.46		N
ATOM	468	CA	ALA	A	61	−20.219	−21.370	16.223	1.00	39.25		C
ATOM	469	C	ALA	A	61	−20.873	−21.880	14.940	1.00	40.91		C
ATOM	470	O	ALA	A	61	−20.228	−21.916	13.891	1.00	43.24		O
ATOM	471	CB	ALA	A	61	−20.363	−19.856	16.343	1.00	34.62		C
ATOM	472	N	GLN	A	62	−22.140	−22.280	15.030	1.00	45.76		N
ATOM	473	CA	GLN	A	62	−22.878	−22.825	13.887	1.00	53.88		C
ATOM	474	C	GLN	A	62	−22.795	−21.937	12.646	1.00	47.20		C
ATOM	475	O	GLN	A	62	−22.716	−22.431	11.522	1.00	48.71		O
ATOM	476	CB	GLN	A	62	−24.349	−23.042	14.258	1.00	52.36		C
ATOM	477	CG	GLN	A	62	−24.596	−24.209	15.206	1.00	79.57		C
ATOM	478	CD	GLN	A	62	−24.422	−25.562	14.534	1.00	86.89		C
ATOM	479	NE2	GLN	A	62	−24.222	−26.603	15.339	1.00	75.39		N
ATOM	480	OE1	GLN	A	62	−24.468	−25.670	13.306	1.00	81.01		O
ATOM	481	N	LYS	A	63	−22.804	−20.626	12.865	1.00	48.15		N
ATOM	482	CA	LYS	A	63	−22.788	−19.644	11.787	1.00	42.61		C
ATOM	483	C	LYS	A	63	−21.524	−19.723	10.919	1.00	43.90		C
ATOM	484	O	LYS	A	63	−21.540	−19.325	9.756	1.00	41.77		O
ATOM	485	CB	LYS	A	63	−22.936	−18.235	12.377	1.00	45.82		C
ATOM	486	CG	LYS	A	63	−23.079	−17.120	11.353	1.00	50.01		C
ATOM	487	CD	LYS	A	63	−23.154	−15.753	12.024	1.00	52.82		C
ATOM	488	CE	LYS	A	63	−23.046	−14.631	10.996	1.00	50.15		C
ATOM	489	NZ	LYS	A	63	−23.127	−13.283	11.624	1.00	61.30		N
ATOM	490	N	PHE	A	64	−20.435	−20.246	11.478	1.00	41.78		N
ATOM	491	CA	PHE	A	64	−19.156	−20.267	10.768	1.00	39.68		C
ATOM	492	C	PHE	A	64	−18.656	−21.675	10.456	1.00	44.13		C
ATOM	493	O	PHE	A	64	−17.611	−21.836	9.821	1.00	46.68		O
ATOM	494	CB	PHE	A	64	−18.094	−19.513	11.574	1.00	35.08		C
ATOM	495	CG	PHE	A	64	−18.454	−18.086	11.848	1.00	41.60		C
ATOM	496	CD1	PHE	A	64	−18.254	−17.109	10.885	1.00	42.81		C
ATOM	497	CD2	PHE	A	64	−19.008	−17.720	13.062	1.00	34.34		C
ATOM	498	CE1	PHE	A	64	−18.593	−15.790	11.135	1.00	34.56		C
ATOM	499	CE2	PHE	A	64	−19.350	−16.405	13.313	1.00	40.22		C
ATOM	500	CZ	PHE	A	64	−19.142	−15.441	12.348	1.00	32.48		C
ATOM	501	N	GLN	A	65	−19.389	−22.689	10.907	1.00	49.73		N
ATOM	502	CA	GLN	A	65	−19.066	−24.069	10.552	1.00	46.28		C
ATOM	503	C	GLN	A	65	−19.116	−24.231	9.040	1.00	44.61		C
ATOM	504	O	GLN	A	65	−20.120	−23.905	8.408	1.00	45.36		O
ATOM	505	CB	GLN	A	65	−20.024	−25.051	11.229	1.00	47.60		C
ATOM	506	CG	GLN	A	65	−19.573	−25.483	12.619	1.00	59.40		C
ATOM	507	CD	GLN	A	65	−20.692	−26.096	13.442	1.00	69.19		C
ATOM	508	NE2	GLN	A	65	−20.460	−26.234	14.745	1.00	55.87		N
ATOM	509	OE1	GLN	A	65	−21.754	−26.434	12.916	1.00	71.81		O
ATOM	510	N	GLY	A	66	−18.019	−24.711	8.464	1.00	39.34		N
ATOM	511	CA	GLY	A	66	−17.919	−24.856	7.026	1.00	46.10		C
ATOM	512	C	GLY	A	66	−17.130	−23.748	6.349	1.00	56.88		C
ATOM	513	O	GLY	A	66	−16.677	−23.912	5.214	1.00	58.19		O
ATOM	514	N	ARG	A	67	−16.966	−22.617	7.031	1.00	44.44		N
ATOM	515	CA	ARG	A	67	−16.192	−21.511	6.470	1.00	43.73		C
ATOM	516	C	ARG	A	67	−14.935	−21.213	7.280	1.00	45.38		C
ATOM	517	O	ARG	A	67	−13.937	−20.745	6.732	1.00	45.99		O
ATOM	518	CB	ARG	A	67	−17.045	−20.244	6.368	1.00	47.99		C
ATOM	519	CG	ARG	A	67	−18.207	−20.359	5.406	1.00	47.03		C
ATOM	520	CD	ARG	A	67	−18.570	−19.011	4.793	1.00	47.09		C
ATOM	521	NE	ARG	A	67	−19.006	−18.032	5.783	1.00	50.09		N
ATOM	522	CZ	ARG	A	67	−18.526	−16.794	5.866	1.00	49.71		C
ATOM	523	NH1	ARG	A	67	−17.590	−16.383	5.020	1.00	46.73		N
ATOM	524	NH2	ARG	A	67	−18.983	−15.964	6.794	1.00	47.52		N
ATOM	525	N	VAL	A	68	−14.979	−21.480	8.582	1.00	39.50		N
ATOM	526	CA	VAL	A	68	−13.848	−21.157	9.443	1.00	35.99		C
ATOM	527	C	VAL	A	68	−12.994	−22.390	9.737	1.00	39.26		C
ATOM	528	O	VAL	A	68	−13.491	−23.514	9.795	1.00	40.40		O
ATOM	529	CB	VAL	A	68	−14.314	−20.511	10.777	1.00	43.31		C
ATOM	530	CG1	VAL	A	68	−14.925	−21.554	11.709	1.00	44.00		C
ATOM	531	CG2	VAL	A	68	−13.155	−19.793	11.461	1.00	36.66		C
ATOM	532	N	THR	A	69	−11.694	−22.167	9.893	1.00	34.83		N
ATOM	533	CA	THR	A	69	−10.772	−23.220	10.282	1.00	37.94		C
ATOM	534	C	THR	A	69	−9.749	−22.651	11.247	1.00	36.48		C
ATOM	535	O	THR	A	69	−9.020	−21.722	10.905	1.00	39.14		O
ATOM	536	CB	THR	A	69	−10.049	−23.833	9.069	1.00	38.15		C
ATOM	537	CG2	THR	A	69	−9.167	−24.998	9.508	1.00	36.65		C
ATOM	538	OG1	THR	A	69	−11.015	−24.297	8.120	1.00	40.71		O
ATOM	539	N	LEU	A	70	−9.705	−23.202	12.454	1.00	32.50		N
ATOM	540	CA	LEU	A	70	−8.759	−22.746	13.463	1.00	32.88		C
ATOM	541	C	LEU	A	70	−7.647	−23.769	13.633	1.00	41.47		C
ATOM	542	O	LEU	A	70	−7.911	−24.942	13.900	1.00	41.36		O
ATOM	543	CB	LEU	A	70	−9.465	−22.501	14.797	1.00	32.92		C
ATOM	544	CG	LEU	A	70	−10.682	−21.573	14.763	1.00	41.37		C
ATOM	545	CD1	LEU	A	70	−11.203	−21.301	16.178	1.00	36.02		C
ATOM	546	CD2	LEU	A	70	−10.360	−20.271	14.047	1.00	32.82		C
ATOM	547	N	THR	A	71	−6.405	−23.324	13.465	1.00	33.46		N
ATOM	548	CA	THR	A	71	−5.250	−24.204	13.587	1.00	35.36		C
ATOM	549	C	THR	A	71	−4.166	−23.523	14.409	1.00	39.68		C
ATOM	550	O	THR	A	71	−4.299	−22.357	14.775	1.00	38.29		O
ATOM	551	CB	THR	A	71	−4.684	−24.607	12.203	1.00	40.98		C
ATOM	552	CG2	THR	A	71	−5.679	−25.475	11.451	1.00	37.98		C
ATOM	553	OG1	THR	A	71	−4.413	−23.432	11.427	1.00	44.28		O
ATOM	554	N	ARG	A	72	−3.097	−24.250	14.713	1.00	41.13		N
ATOM	555	CA	ARG	A	72	−1.996	−23.659	15.460	1.00	41.98		C
ATOM	556	C	ARG	A	72	−0.644	−24.252	15.077	1.00	44.70		C
ATOM	557	O	ARG	A	72	−0.566	−25.292	14.429	1.00	41.56		O
ATOM	558	CB	ARG	A	72	−2.231	−23.811	16.970	1.00	44.74		C
ATOM	559	CG	ARG	A	72	−2.599	−25.216	17.439	1.00	46.36		C
ATOM	560	CD	ARG	A	72	−1.366	−26.056	17.691	1.00	52.55		C
ATOM	561	NE	ARG	A	72	−1.653	−27.299	18.401	1.00	45.44		N
ATOM	562	CZ	ARG	A	72	−2.105	−28.406	17.824	1.00	51.24		C
ATOM	563	NH1	ARG	A	72	−2.353	−28.429	16.522	1.00	53.24		N
ATOM	564	NH2	ARG	A	72	−2.319	−29.492	18.553	1.00	55.87		N
ATOM	565	N	ASP	A	73	0.413	−23.563	15.488	1.00	44.00		N
ATOM	566	CA	ASP	A	73	1.779	−24.033	15.331	1.00	45.95		C
ATOM	567	C	ASP	A	73	2.510	−23.807	16.652	1.00	45.15		C
ATOM	568	O	ASP	A	73	3.010	−22.710	16.916	1.00	46.41		O
ATOM	569	CB	ASP	A	73	2.473	−23.305	14.175	1.00	52.61		C
ATOM	570	CG	ASP	A	73	3.922	−23.728	13.995	1.00	58.41		C
ATOM	571	OD1	ASP	A	73	4.345	−24.730	14.609	1.00	57.08		O
ATOM	572	OD2	ASP	A	73	4.639	−23.059	13.220	1.00	60.43		O
ATOM	573	N	THR	A	74	2.560	−24.847	17.480	1.00	46.17		N
ATOM	574	CA	THR	A	74	3.082	−24.726	18.841	1.00	48.47		C
ATOM	575	C	THR	A	74	4.559	−24.346	18.884	1.00	46.89		C
ATOM	576	O	THR	A	74	5.012	−23.723	19.842	1.00	53.90		O
ATOM	577	CB	THR	A	74	2.888	−26.035	19.636	1.00	54.20		C
ATOM	578	CG2	THR	A	74	1.439	−26.185	20.072	1.00	48.42		C
ATOM	579	OG1	THR	A	74	3.250	−27.155	18.817	1.00	60.06		O
ATOM	580	N	SER	A	75	5.303	−24.710	17.845	1.00	51.70		N
ATOM	581	CA	SER	A	75	6.737	−24.436	17.801	1.00	54.91		C
ATOM	582	C	SER	A	75	7.036	−22.937	17.815	1.00	55.26		C
ATOM	583	O	SER	A	75	8.114	−22.515	18.237	1.00	49.86		O
ATOM	584	CB	SER	A	75	7.365	−25.088	16.568	1.00	55.81		C
ATOM	585	OG	SER	A	75	6.713	−24.668	15.382	1.00	60.43		O
ATOM	586	N	ILE	A	76	6.077	−22.136	17.359	1.00	52.63		N
ATOM	587	CA	ILE	A	76	6.224	−20.684	17.386	1.00	47.56		C
ATOM	588	C	ILE	A	76	5.090	−20.021	18.170	1.00	50.56		C
ATOM	589	O	ILE	A	76	4.920	−18.802	18.109	1.00	52.59		O
ATOM	590	CB	ILE	A	76	6.271	−20.093	15.962	1.00	50.46		C
ATOM	591	CG1	ILE	A	76	5.040	−20.521	15.163	1.00	47.49		C
ATOM	592	CG2	ILE	A	76	7.536	−20.531	15.248	1.00	46.69		C
ATOM	593	CD1	ILE	A	76	4.922	−19.840	13.817	1.00	48.75		C
ATOM	594	N	SER	A	77	4.324	−20.834	18.896	1.00	49.81		N
ATOM	595	CA	SER	A	77	3.229	−20.357	19.744	1.00	45.00		C
ATOM	596	C	SER	A	77	2.246	−19.470	18.988	1.00	46.19		C
ATOM	597	O	SER	A	77	1.894	−18.387	19.456	1.00	40.30		O
ATOM	598	CB	SER	A	77	3.781	−19.591	20.951	1.00	43.85		C
ATOM	599	OG	SER	A	77	4.716	−20.370	21.673	1.00	63.87		O
ATOM	600	N	THR	A	78	1.800	−19.925	17.822	1.00	39.04		N
ATOM	601	CA	THR	A	78	0.956	−19.090	16.979	1.00	37.69		C
ATOM	602	C	THR	A	78	−0.337	−19.788	16.575	1.00	37.97		C
ATOM	603	O	THR	A	78	−0.325	−20.930	16.115	1.00	39.48		O
ATOM	604	CB	THR	A	78	1.718	−18.641	15.712	1.00	38.64		C
ATOM	605	CG2	THR	A	78	0.810	−17.840	14.787	1.00	38.64		C
ATOM	606	OG1	THR	A	78	2.828	−17.822	16.094	1.00	35.01		O
ATOM	607	N	ALA	A	79	−1.454	−19.093	16.765	1.00	33.81		N
ATOM	608	CA	ALA	A	79	−2.756	−19.592	16.336	1.00	34.16		C
ATOM	609	C	ALA	A	79	−3.165	−18.934	15.023	1.00	34.47		C
ATOM	610	O	ALA	A	79	−2.748	−17.815	14.720	1.00	33.95		O
ATOM	611	CB	ALA	A	79	−3.805	−19.340	17.403	1.00	24.34		C
ATOM	612	N	TYR	A	80	−3.990	−19.631	14.252	1.00	31.73		N
ATOM	613	CA	TYR	A	80	−4.432	−19.135	12.958	1.00	37.57		C
ATOM	614	C	TYR	A	80	−5.942	−19.198	12.810	1.00	39.18		C
ATOM	615	O	TYR	A	80	−6.598	−20.132	13.278	1.00	37.02		O
ATOM	616	CB	TYR	A	80	−3.786	−19.929	11.819	1.00	36.79		C
ATOM	617	CG	TYR	A	80	−2.281	−19.862	11.797	1.00	40.36		C
ATOM	618	CD1	TYR	A	80	−1.621	−18.821	11.158	1.00	37.20		C
ATOM	619	CD2	TYR	A	80	−1.517	−20.847	12.413	1.00	38.74		C
ATOM	620	CE1	TYR	A	80	−0.238	−18.761	11.135	1.00	37.53		C
ATOM	621	CE2	TYR	A	80	−0.140	−20.797	12.395	1.00	37.97		C
ATOM	622	CZ	TYR	A	80	0.497	−19.755	11.756	1.00	43.48		C
ATOM	623	OH	TYR	A	80	1.872	−19.708	11.742	1.00	41.36		O
ATOM	624	N	MET	A	81	−6.486	−18.195	12.141	1.00	31.97		N
ATOM	625	CA	MET	A	81	−7.895	−18.185	11.803	1.00	37.08		C
ATOM	626	C	MET	A	81	−7.999	−18.062	10.297	1.00	34.14		C
ATOM	627	O	MET	A	81	−7.505	−17.096	9.717	1.00	38.01		O
ATOM	628	CB	MET	A	81	−8.619	−17.036	12.509	1.00	39.39		C
ATOM	629	CG	MET	A	81	−10.137	−17.099	12.445	1.00	43.17		C
ATOM	630	SD	MET	A	81	−10.835	−16.468	10.907	1.00	56.54		S
ATOM	631	CE	MET	A	81	−10.224	−14.782	10.930	1.00	40.20		C
ATOM	632	N	GLU	A	82	−8.606	−19.054	9.659	1.00	36.27		N
ATOM	633	CA	GLU	A	82	−8.825	−18.989	8.222	1.00	37.25		C
ATOM	634	C	GLU	A	82	−10.310	−18.963	7.908	1.00	38.89		C
ATOM	635	O	GLU	A	82	−11.064	−19.831	8.343	1.00	42.10		O
ATOM	636	CB	GLU	A	82	−8.159	−20.161	7.504	1.00	34.97		C
ATOM	637	CG	GLU	A	82	−8.406	−20.149	6.003	1.00	48.29		C
ATOM	638	CD	GLU	A	82	−7.374	−20.946	5.228	1.00	61.14		C
ATOM	639	OE1	GLU	A	82	−6.617	−21.717	5.858	1.00	70.53		O
ATOM	640	OE2	GLU	A	82	−7.313	−20.793	3.989	1.00	62.98		O
ATOM	641	N	LEU	A	83	−10.726	−17.946	7.161	1.00	41.14		N
ATOM	642	CA	LEU	A	83	−12.118	−17.807	6.766	1.00	40.75		C
ATOM	643	C	LEU	A	83	−12.204	−17.828	5.246	1.00	42.77		C
ATOM	644	O	LEU	A	83	−11.572	−17.017	4.569	1.00	46.85		O
ATOM	645	CB	LEU	A	83	−12.716	−16.519	7.336	1.00	38.47		C
ATOM	646	CG	LEU	A	83	−14.233	−16.359	7.216	1.00	41.96		C
ATOM	647	CD1	LEU	A	83	−14.956	−17.499	7.919	1.00	40.57		C
ATOM	648	CD2	LEU	A	83	−14.677	−15.015	7.776	1.00	38.68		C
ATOM	649	N	SER	A	84	−12.974	−18.769	4.711	1.00	41.64		N
ATOM	650	CA	SER	A	84	−13.079	−18.936	3.267	1.00	42.87		C
ATOM	651	C	SER	A	84	−14.426	−18.442	2.740	1.00	44.92		C
ATOM	652	O	SER	A	84	−15.304	−18.067	3.522	1.00	44.37		O
ATOM	653	CB	SER	A	84	−12.868	−20.402	2.888	1.00	39.46		C
ATOM	654	OG	SER	A	84	−13.903	−21.211	3.416	1.00	44.27		O
ATOM	655	N	SER	A	85	−14.572	−18.454	1.414	1.00	47.43		N
ATOM	656	CA	SER	A	85	−15.769	−17.960	0.732	1.00	41.86		C
ATOM	657	C	SER	A	85	−16.189	−16.591	1.245	1.00	43.45		C
ATOM	658	O	SER	A	85	−17.337	−16.392	1.652	1.00	44.70		O
ATOM	659	CB	SER	A	85	−16.922	−18.952	0.882	1.00	45.07		C
ATOM	660	OG	SER	A	85	−16.674	−20.125	0.128	1.00	51.48		O
ATOM	661	N	LEU	A	86	−15.249	−15.650	1.223	1.00	43.44		N
ATOM	662	CA	LEU	A	86	−15.457	−14.338	1.826	1.00	41.57		C
ATOM	663	C	LEU	A	86	−16.526	−13.526	1.104	1.00	46.59		C
ATOM	664	O	LEU	A	86	−16.551	−13.456	−0.128	1.00	40.39		O
ATOM	665	CB	LEU	A	86	−14.142	−13.557	1.858	1.00	40.33		C
ATOM	666	CG	LEU	A	86	−13.076	−14.119	2.800	1.00	41.08		C
ATOM	667	CD1	LEU	A	86	−11.732	−13.444	2.573	1.00	39.92		C
ATOM	668	CD2	LEU	A	86	−13.527	−13.966	4.241	1.00	33.71		C
ATOM	669	N	ARG	A	87	−17.420	−12.933	1.888	1.00	37.30		N
ATOM	670	CA	ARG	A	87	−18.411	−12.002	1.371	1.00	42.71		C
ATOM	671	C	ARG	A	87	−18.086	−10.616	1.905	1.00	44.74		C
ATOM	672	O	ARG	A	87	−17.304	−10.483	2.846	1.00	42.11		O
ATOM	673	CB	ARG	A	87	−19.828	−12.418	1.774	1.00	47.73		C
ATOM	674	CG	ARG	A	87	−20.231	−13.806	1.298	1.00	57.87		C
ATOM	675	CD	ARG	A	87	−21.702	−14.088	1.577	1.00	78.50		C
ATOM	676	NE	ARG	A	87	−22.154	−15.318	0.928	1.00	98.72		N
ATOM	677	CZ	ARG	A	87	−23.391	−15.800	1.009	1.00	102.44		C
ATOM	678	NH1	ARG	A	87	−24.311	−15.158	1.716	1.00	100.96		N
ATOM	679	NH2	ARG	A	87	−23.708	−16.927	0.384	1.00	94.73		N
ATOM	680	N	SER	A	88	−18.682	−9.586	1.315	1.00	48.46		N
ATOM	681	CA	SER	A	88	−18.426	−8.221	1.759	1.00	47.83		C
ATOM	682	C	SER	A	88	−18.871	−8.035	3.212	1.00	43.27		C
ATOM	683	O	SER	A	88	−18.315	−7.210	3.935	1.00	45.67		O
ATOM	684	CB	SER	A	88	−19.126	−7.209	0.843	1.00	46.62		C
ATOM	685	OG	SER	A	88	−20.530	−7.399	0.826	1.00	56.66		O
ATOM	686	N	GLU	A	89	−19.857	−8.823	3.638	1.00	43.65		N
ATOM	687	CA	GLU	A	89	−20.347	−8.780	5.012	1.00	42.47		C
ATOM	688	C	GLU	A	89	−19.332	−9.323	6.015	1.00	42.20		C
ATOM	689	O	GLU	A	89	−19.508	−9.163	7.224	1.00	44.31		O
ATOM	690	CB	GLU	A	89	−21.658	−9.562	5.146	1.00	48.07		C
ATOM	691	CG	GLU	A	89	−22.881	−8.844	4.594	1.00	69.24		C
ATOM	692	CD	GLU	A	89	−22.970	−8.904	3.079	1.00	77.53		C
ATOM	693	OE1	GLU	A	89	−22.301	−9.773	2.476	1.00	65.90		O
ATOM	694	OE2	GLU	A	89	−23.710	−8.081	2.493	1.00	76.65		O
ATOM	695	N	ASP	A	90	−18.279	−9.969	5.519	1.00	36.36		N
ATOM	696	CA	ASP	A	90	−17.213	−10.463	6.388	1.00	34.38		C
ATOM	697	C	ASP	A	90	−16.197	−9.364	6.709	1.00	39.43		C
ATOM	698	O	ASP	A	90	−15.250	−9.589	7.463	1.00	38.18		O
ATOM	699	CB	ASP	A	90	−16.494	−11.658	5.751	1.00	38.88		C
ATOM	700	CG	ASP	A	90	−17.361	−12.903	5.681	1.00	42.31		C
ATOM	701	OD1	ASP	A	90	−18.157	−13.146	6.616	1.00	37.56		O
ATOM	702	OD2	ASP	A	90	−17.237	−13.646	4.683	1.00	47.30		O
ATOM	703	N	THR	A	91	−16.389	−8.183	6.127	1.00	34.63		N
ATOM	704	CA	THR	A	91	−15.525	−7.042	6.418	1.00	35.67		C
ATOM	705	C	THR	A	91	−15.661	−6.663	7.887	1.00	34.77		C
ATOM	706	O	THR	A	91	−16.743	−6.285	8.340	1.00	34.99		O
ATOM	707	CB	THR	A	91	−15.858	−5.818	5.532	1.00	37.50		C
ATOM	708	CG2	THR	A	91	−15.075	−4.591	5.994	1.00	34.40		C
ATOM	709	OG1	THR	A	91	−15.529	−6.104	4.164	1.00	40.03		O
ATOM	710	N	ALA	A	92	−14.562	−6.772	8.626	1.00	29.62		N
ATOM	711	CA	ALA	A	92	−14.588	−6.570	10.070	1.00	32.67		C
ATOM	712	C	ALA	A	92	−13.190	−6.544	10.665	1.00	27.73		C
ATOM	713	O	ALA	A	92	−12.209	−6.882	10.001	1.00	29.29		O
ATOM	714	CB	ALA	A	92	−15.416	−7.671	10.746	1.00	33.43		C
ATOM	715	N	VAL	A	93	−13.112	−6.143	11.929	1.00	30.17		N
ATOM	716	CA	VAL	A	93	−11.897	−6.308	12.704	1.00	26.67		C
ATOM	717	C	VAL	A	93	−11.959	−7.652	13.424	1.00	29.85		C
ATOM	718	O	VAL	A	93	−12.911	−7.934	14.154	1.00	32.54		O
ATOM	719	CB	VAL	A	93	−11.705	−5.169	13.726	1.00	31.84		C
ATOM	720	CG1	VAL	A	93	−10.539	−5.475	14.653	1.00	24.37		C
ATOM	721	CG2	VAL	A	93	−11.487	−3.842	13.009	1.00	25.26		C
ATOM	722	N	TYR	A	94	−10.948	−8.484	13.207	1.00	26.52		N
ATOM	723	CA	TYR	A	94	−10.911	−9.806	13.816	1.00	31.35		C
ATOM	724	C	TYR	A	94	−9.961	−9.826	15.005	1.00	33.59		C
ATOM	725	O	TYR	A	94	−8.769	−9.546	14.867	1.00	31.79		O
ATOM	726	CB	TYR	A	94	−10.518	−10.861	12.774	1.00	25.00		C
ATOM	727	CG	TYR	A	94	−11.629	−11.105	11.781	1.00	27.22		C
ATOM	728	CD1	TYR	A	94	−11.863	−10.216	10.739	1.00	30.50		C
ATOM	729	CD2	TYR	A	94	−12.469	−12.207	11.906	1.00	23.97		C
ATOM	730	CE1	TYR	A	94	−12.893	−10.423	9.842	1.00	27.95		C
ATOM	731	CE2	TYR	A	94	−13.492	−12.423	11.022	1.00	26.58		C
ATOM	732	CZ	TYR	A	94	−13.703	−11.527	9.989	1.00	32.87		C
ATOM	733	OH	TYR	A	94	−14.730	−11.739	9.104	1.00	30.47		O
ATOM	734	N	TYR	A	95	−10.511	−10.135	16.177	1.00	24.85		N
ATOM	735	CA	TYR	A	95	−9.731	−10.215	17.406	1.00	28.45		C
ATOM	736	C	TYR	A	95	−9.474	−11.661	17.805	1.00	27.62		C
ATOM	737	O	TYR	A	95	−10.356	−12.508	17.688	1.00	28.27		O
ATOM	738	CB	TYR	A	95	−10.450	−9.512	18.564	1.00	24.54		C
ATOM	739	CG	TYR	A	95	−10.626	−8.019	18.419	1.00	26.81		C
ATOM	740	CD1	TYR	A	95	−9.580	−7.148	18.692	1.00	27.26		C
ATOM	741	CD2	TYR	A	95	−11.847	−7.481	18.036	1.00	28.58		C
ATOM	742	CE1	TYR	A	95	−9.737	−5.778	18.571	1.00	27.06		C
ATOM	743	CE2	TYR	A	95	−12.017	−6.113	17.913	1.00	27.13		C
ATOM	744	CZ	TYR	A	95	−10.960	−5.269	18.184	1.00	27.27		C
ATOM	745	OH	TYR	A	95	−11.125	−3.911	18.060	1.00	31.79		O
ATOM	746	N	CYS	A	96	−8.274	−11.945	18.289	1.00	23.92		N
ATOM	747	CA	CYS	A	96	−8.073	−13.182	19.025	1.00	30.30		C
ATOM	748	C	CYS	A	96	−8.115	−12.829	20.505	1.00	27.04		C
ATOM	749	O	CYS	A	96	−7.708	−11.736	20.899	1.00	28.05		O
ATOM	750	CB	CYS	A	96	−6.758	−13.877	18.645	1.00	33.84		C
ATOM	751	SG	CYS	A	96	−5.246	−13.010	19.099	1.00	48.82		S
ATOM	752	N	ALA	A	97	−8.634	−13.742	21.316	1.00	28.58		N
ATOM	753	CA	ALA	A	97	−8.783	−13.497	22.743	1.00	26.57		C
ATOM	754	C	ALA	A	97	−8.768	−14.816	23.507	1.00	32.11		C
ATOM	755	O	ALA	A	97	−9.409	−15.780	23.091	1.00	30.87		O
ATOM	756	CB	ALA	A	97	−10.065	−12.736	23.016	1.00	26.61		C
ATOM	757	N	SER	A	98	−8.042	−14.864	24.621	1.00	27.25		N
ATOM	758	CA	SER	A	98	−7.888	−16.121	25.348	1.00	32.20		C
ATOM	759	C	SER	A	98	−8.839	−16.275	26.532	1.00	29.23		C
ATOM	760	O	SER	A	98	−9.249	−15.294	27.153	1.00	25.23		O
ATOM	761	CB	SER	A	98	−6.453	−16.280	25.845	1.00	33.45		C
ATOM	762	OG	SER	A	98	−6.155	−15.337	26.856	1.00	45.41		O
ATOM	763	N	SER	A	99	−9.169	−17.528	26.833	1.00	29.87		N
ATOM	764	CA	SER	A	99	−9.971	−17.885	28.001	1.00	30.05		C
ATOM	765	C	SER	A	99	−9.348	−19.099	28.689	1.00	35.19		C
ATOM	766	O	SER	A	99	−8.528	−19.794	28.086	1.00	30.60		O
ATOM	767	CB	SER	A	99	−11.417	−18.171	27.596	1.00	26.53		C
ATOM	768	OG	SER	A	99	−11.485	−19.129	26.552	1.00	29.62		O
ATOM	769	N	SER	A	100	−9.738	−19.355	29.938	1.00	33.90		N
ATOM	770	CA	SER	A	100	−9.099	−20.396	30.749	1.00	39.84		C
ATOM	771	C	SER	A	100	−10.060	−21.427	31.338	1.00	33.23		C
ATOM	772	O	SER	A	100	−9.932	−21.793	32.506	1.00	40.18		O
ATOM	773	CB	SER	A	100	−8.319	−19.758	31.900	1.00	32.53		C
ATOM	774	OG	SER	A	100	−7.194	−19.048	31.424	1.00	49.78		O
ATOM	775	O	GLY	A	101	−14.315	−23.137	30.676	1.00	40.43		O
ATOM	776	N	GLY	A	101	−11.017	−21.899	30.547	1.00	31.28		N
ATOM	777	CA	GLY	A	101	−11.974	−22.868	31.048	1.00	28.36		C
ATOM	778	C	GLY	A	101	−13.406	−22.374	30.999	1.00	32.57		C
ATOM	779	O	TRP	A	102	−13.530	−18.918	29.800	1.00	32.97		O
ATOM	780	N	TRP	A	102	−13.617	−21.110	31.357	1.00	23.41		N
ATOM	781	CA	TRP	A	102	−14.879	−20.435	31.059	1.00	26.91		C
ATOM	782	C	TRP	A	102	−14.626	−19.471	29.916	1.00	30.14		C
ATOM	783	CB	TRP	A	102	−15.432	−19.683	32.271	1.00	27.64		C
ATOM	784	CG	TRP	A	102	−15.721	−20.553	33.447	1.00	28.49		C
ATOM	785	CD1	TRP	A	102	−16.761	−21.428	33.587	1.00	25.22		C
ATOM	786	CD2	TRP	A	102	−14.972	−20.618	34.664	1.00	25.37		C
ATOM	787	NE1	TRP	A	102	−16.701	−22.038	34.818	1.00	26.75		N
ATOM	788	CE2	TRP	A	102	−15.611	−21.559	35.498	1.00	23.51		C
ATOM	789	CE3	TRP	A	102	−13.819	−19.977	35.128	1.00	23.78		C
ATOM	790	CZ2	TRP	A	102	−15.134	−21.874	36.772	1.00	27.12		C
ATOM	791	CZ3	TRP	A	102	−13.346	−20.291	36.396	1.00	31.84		C
ATOM	792	CH2	TRP	A	102	−14.003	−21.232	37.202	1.00	24.60		C
ATOM	793	O	TYR	A	103	−16.560	−16.374	27.434	1.00	35.87		O
ATOM	794	N	TYR	A	103	−15.628	−19.268	29.071	1.00	23.62		N
ATOM	795	CA	TYR	A	103	−15.441	−18.444	27.884	1.00	33.88		C
ATOM	796	C	TYR	A	103	−15.723	−16.960	28.117	1.00	34.03		C
ATOM	797	CB	TYR	A	103	−16.321	−18.949	26.742	1.00	27.85		C
ATOM	798	CG	TYR	A	103	−15.988	−20.342	26.265	1.00	32.69		C
ATOM	799	CD1	TYR	A	103	−14.804	−20.601	25.588	1.00	31.32		C
ATOM	800	CD2	TYR	A	103	−16.866	−21.396	26.478	1.00	31.92		C
ATOM	801	CE1	TYR	A	103	−14.498	−21.879	25.143	1.00	32.07		C
ATOM	802	CE2	TYR	A	103	−16.571	−22.673	26.036	1.00	31.82		C
ATOM	803	CZ	TYR	A	103	−15.385	−22.908	25.370	1.00	34.61		C
ATOM	804	OH	TYR	A	103	−15.090	−24.176	24.931	1.00	37.00		O
ATOM	805	N	TYR	A	104	−15.035	−16.359	29.085	1.00	30.47		N
ATOM	806	CA	TYR	A	104	−14.929	−14.904	29.133	1.00	34.52		C
ATOM	807	C	TYR	A	104	−13.452	−14.557	28.940	1.00	37.81		C
ATOM	808	O	TYR	A	104	−12.571	−15.311	29.359	1.00	33.63		O
ATOM	809	CB	TYR	A	104	−15.488	−14.328	30.439	1.00	28.01		C
ATOM	810	CG	TYR	A	104	−14.762	−14.755	31.690	1.00	29.48		C
ATOM	811	CD2	TYR	A	104	−15.209	−15.837	32.442	1.00	31.05		C
ATOM	812	CD1	TYR	A	104	−13.639	−14.068	32.132	1.00	33.84		C
ATOM	813	CE2	TYR	A	104	−14.547	−16.227	33.600	1.00	31.77		C
ATOM	814	CE1	TYR	A	104	−12.968	−14.452	33.282	1.00	38.93		C
ATOM	815	CZ	TYR	A	104	−13.424	−15.530	34.009	1.00	35.52		C
ATOM	816	OH	TYR	A	104	−12.751	−15.905	35.147	1.00	47.88		O
ATOM	817	N	PHE	A	105	−13.180	−13.423	28.308	1.00	34.39		N
ATOM	818	CA	PHE	A	105	−11.862	−13.201	27.718	1.00	31.85		C
ATOM	819	C	PHE	A	105	−11.046	−12.124	28.419	1.00	31.30		C
ATOM	820	O	PHE	A	105	−11.367	−10.938	28.347	1.00	33.02		O
ATOM	821	CB	PHE	A	105	−12.046	−12.872	26.240	1.00	27.43		C
ATOM	822	CG	PHE	A	105	−13.093	−13.719	25.583	1.00	32.14		C
ATOM	823	CD1	PHE	A	105	−12.894	−15.083	25.423	1.00	32.34		C
ATOM	824	CD2	PHE	A	105	−14.292	−13.168	25.166	1.00	33.77		C
ATOM	825	CE1	PHE	A	105	−13.866	−15.879	24.840	1.00	28.51		C
ATOM	826	CE2	PHE	A	105	−15.267	−13.959	24.577	1.00	36.93		C
ATOM	827	CZ	PHE	A	105	−15.052	−15.317	24.413	1.00	31.65		C
ATOM	828	N	ASP	A	106	−9.981	−12.543	29.097	1.00	31.31		N
ATOM	829	CA	ASP	A	106	−9.205	−11.614	29.914	1.00	33.51		C
ATOM	830	C	ASP	A	106	−8.015	−11.014	29.167	1.00	32.69		C
ATOM	831	O	ASP	A	106	−7.485	−9.983	29.578	1.00	38.29		O
ATOM	832	CB	ASP	A	106	−8.734	−12.298	31.206	1.00	37.27		C
ATOM	833	CG	ASP	A	106	−8.078	−13.645	30.962	1.00	44.11		C
ATOM	834	OD1	ASP	A	106	−8.298	−14.243	29.886	1.00	44.95		O
ATOM	835	OD2	ASP	A	106	−7.347	−14.114	31.860	1.00	39.24		O
ATOM	836	N	TYR	A	107	−7.604	−11.645	28.069	1.00	33.81		N
ATOM	837	CA	TYR	A	107	−6.550	−11.085	27.220	1.00	31.46		C
ATOM	838	C	TYR	A	107	−6.967	−11.061	25.752	1.00	27.21		C
ATOM	839	O	TYR	A	107	−7.565	−12.015	25.256	1.00	27.70		O
ATOM	840	CB	TYR	A	107	−5.250	−11.870	27.388	1.00	34.62		C
ATOM	841	CG	TYR	A	107	−4.719	−11.830	28.802	1.00	39.20		C
ATOM	842	CD1	TYR	A	107	−4.065	−10.705	29.284	1.00	44.79		C
ATOM	843	CD2	TYR	A	107	−4.882	−12.912	29.659	1.00	42.77		C
ATOM	844	CE1	TYR	A	107	−3.584	−10.658	30.583	1.00	57.22		C
ATOM	845	CE2	TYR	A	107	−4.403	−12.875	30.957	1.00	50.96		C
ATOM	846	CZ	TYR	A	107	−3.758	−11.746	31.414	1.00	48.15		C
ATOM	847	OH	TYR	A	107	−3.279	−11.702	32.703	1.00	71.00		O
ATOM	848	N	TRP	A	108	−6.638	−9.967	25.066	1.00	27.81		N
ATOM	849	CA	TRP	A	108	−7.055	−9.741	23.679	1.00	21.18		C
ATOM	850	C	TRP	A	108	−5.892	−9.324	22.782	1.00	26.32		C
ATOM	851	O	TRP	A	108	−4.984	−8.615	23.218	1.00	29.92		O
ATOM	852	CB	TRP	A	108	−8.132	−8.654	23.610	1.00	21.90		C
ATOM	853	CG	TRP	A	108	−9.444	−9.007	24.233	1.00	27.98		C
ATOM	854	CD1	TRP	A	108	−9.700	−9.207	25.560	1.00	27.08		C
ATOM	855	CD2	TRP	A	108	−10.693	−9.171	23.554	1.00	27.01		C
ATOM	856	CE2	TRP	A	108	−11.663	−9.484	24.530	1.00	25.58		C
ATOM	857	CE3	TRP	A	108	−11.085	−9.093	22.212	1.00	25.64		C
ATOM	858	NE1	TRP	A	108	−11.032	−9.500	25.746	1.00	24.70		N
ATOM	859	CZ2	TRP	A	108	−12.999	−9.715	24.208	1.00	25.47		C
ATOM	860	CZ3	TRP	A	108	−12.414	−9.322	21.893	1.00	32.29		C
ATOM	861	CH2	TRP	A	108	−13.355	−9.630	22.889	1.00	32.24		C
ATOM	862	N	GLY	A	109	−5.928	−9.748	21.523	1.00	27.02		N
ATOM	863	CA	GLY	A	109	−5.002	−9.227	20.531	1.00	28.74		C
ATOM	864	C	GLY	A	109	−5.415	−7.812	20.159	1.00	31.88		C
ATOM	865	O	GLY	A	109	−6.476	−7.346	20.584	1.00	26.79		O
ATOM	866	N	GLN	A	110	−4.595	−7.120	19.373	1.00	28.50		N
ATOM	867	CA	GLN	A	110	−4.878	−5.721	19.055	1.00	29.47		C
ATOM	868	C	GLN	A	110	−5.904	−5.611	17.928	1.00	30.21		C
ATOM	869	O	GLN	A	110	−6.432	−4.532	17.659	1.00	36.00		O
ATOM	870	CB	GLN	A	110	−3.591	−4.966	18.683	1.00	23.57		C
ATOM	871	CG	GLN	A	110	−3.125	−5.156	17.239	1.00	29.23		C
ATOM	872	CD	GLN	A	110	−2.309	−6.419	17.032	1.00	33.10		C
ATOM	873	NE2	GLN	A	110	−1.568	−6.467	15.929	1.00	31.73		N
ATOM	874	OE1	GLN	A	110	−2.343	−7.342	17.850	1.00	35.23		O
ATOM	875	N	GLY	A	111	−6.192	−6.733	17.277	1.00	31.62		N
ATOM	876	CA	GLY	A	111	−7.188	−6.760	16.225	1.00	31.32		C
ATOM	877	C	GLY	A	111	−6.604	−6.675	14.831	1.00	34.22		C
ATOM	878	O	GLY	A	111	−5.561	−6.059	14.612	1.00	31.13		O
ATOM	879	N	THR	A	112	−7.291	−7.299	13.882	1.00	29.50		N
ATOM	880	CA	THR	A	112	−6.858	−7.300	12.494	1.00	30.89		C
ATOM	881	C	THR	A	112	−8.008	−6.901	11.587	1.00	30.69		C
ATOM	882	O	THR	A	112	−9.035	−7.577	11.551	1.00	28.68		O
ATOM	883	CB	THR	A	112	−6.334	−8.683	12.064	1.00	34.70		C
ATOM	884	CG2	THR	A	112	−5.960	−8.683	10.584	1.00	33.17		C
ATOM	885	OG1	THR	A	112	−5.182	−9.025	12.846	1.00	39.75		O
ATOM	886	N	LEU	A	113	−7.842	−5.804	10.859	1.00	28.77		N
ATOM	887	CA	LEU	A	113	−8.868	−5.372	9.917	1.00	26.18		C
ATOM	888	C	LEU	A	113	−8.801	−6.203	8.635	1.00	32.80		C
ATOM	889	O	LEU	A	113	−7.769	−6.263	7.968	1.00	31.11		O
ATOM	890	CB	LEU	A	113	−8.721	−3.883	9.587	1.00	26.67		C
ATOM	891	CG	LEU	A	113	−9.680	−3.339	8.518	1.00	32.26		C
ATOM	892	CD1	LEU	A	113	−11.139	−3.581	8.899	1.00	29.02		C
ATOM	893	CD2	LEU	A	113	−9.437	−1.855	8.262	1.00	32.24		C
ATOM	894	N	VAL	A	114	−9.904	−6.859	8.305	1.00	28.44		N
ATOM	895	CA	VAL	A	114	−10.009	−7.566	7.036	1.00	30.93		C
ATOM	896	C	VAL	A	114	−11.076	−6.899	6.188	1.00	30.62		C
ATOM	897	O	VAL	A	114	−12.233	−6.788	6.601	1.00	29.64		O
ATOM	898	CB	VAL	A	114	−10.353	−9.058	7.225	1.00	31.72		C
ATOM	899	CG1	VAL	A	114	−10.535	−9.740	5.869	1.00	33.36		C
ATOM	900	CG2	VAL	A	114	−9.265	−9.750	8.042	1.00	32.90		C
ATOM	901	N	THR	A	115	−10.676	−6.436	5.009	1.00	35.29		N
ATOM	902	CA	THR	A	115	−11.604	−5.788	4.100	1.00	34.33		C
ATOM	903	C	THR	A	115	−11.863	−6.700	2.912	1.00	36.39		C
ATOM	904	O	THR	A	115	−10.929	−7.156	2.251	1.00	35.90		O
ATOM	905	CB	THR	A	115	−11.068	−4.426	3.610	1.00	36.40		C
ATOM	906	CG2	THR	A	115	−12.038	−3.785	2.628	1.00	34.46		C
ATOM	907	OG1	THR	A	115	−10.890	−3.552	4.730	1.00	37.23		O
ATOM	908	N	VAL	A	116	−13.136	−6.976	2.657	1.00	39.45		N
ATOM	909	CA	VAL	A	116	−13.527	−7.775	1.504	1.00	34.84		C
ATOM	910	C	VAL	A	116	−14.212	−6.875	0.490	1.00	38.13		C
ATOM	911	O	VAL	A	116	−15.289	−6.339	0.755	1.00	35.45		O
ATOM	912	CB	VAL	A	116	−14.475	−8.932	1.886	1.00	39.24		C
ATOM	913	CG1	VAL	A	116	−14.679	−9.864	0.693	1.00	39.66		C
ATOM	914	CG2	VAL	A	116	−13.924	−9.705	3.075	1.00	38.07		C
ATOM	915	N	SER	A	117	−13.589	−6.706	−0.671	1.00	34.44		N
ATOM	916	CA	SER	A	117	−14.126	−5.795	−1.671	1.00	40.89		C
ATOM	917	C	SER	A	117	−13.687	−6.131	−3.091	1.00	40.89		C
ATOM	918	O	SER	A	117	−12.598	−6.661	−3.313	1.00	38.45		O
ATOM	919	CB	SER	A	117	−13.716	−4.359	−1.345	1.00	34.47		C
ATOM	920	OG	SER	A	117	−14.224	−3.460	−2.318	1.00	43.36		O
ATOM	921	O	SER	A	118	−12.636	−4.911	−6.922	1.00	43.31		O
ATOM	922	N	SER	A	118	−14.546	−5.795	−4.047	1.00	42.01		N
ATOM	923	CA	SER	A	118	−14.232	−5.940	−5.462	1.00	52.20		C
ATOM	924	C	SER	A	118	−13.391	−4.770	−5.963	1.00	47.46		C
ATOM	925	CB	SER	A	118	−15.516	−6.046	−6.287	1.00	44.49		C
ATOM	926	OG	SER	A	118	−16.364	−7.057	−5.772	1.00	64.31		O
ATOM	927	O	ALA	A	119	−10.794	−3.378	−5.023	1.00	46.60		O
ATOM	928	N	ALA	A	119	−13.530	−3.617	−5.311	1.00	44.58		N
ATOM	929	CA	ALA	A	119	−12.862	−2.393	−5.753	1.00	40.93		C
ATOM	930	C	ALA	A	119	−11.342	−2.520	−5.714	1.00	45.33		C
ATOM	931	CB	ALA	A	119	−13.312	−1.211	−4.908	1.00	36.58		C
ATOM	932	N	SER	A	120	−10.666	−1.656	−6.462	1.00	46.47		N
ATOM	933	CA	SER	A	120	−9.215	−1.709	−6.568	1.00	45.38		C
ATOM	934	C	SER	A	120	−8.519	−1.011	−5.404	1.00	40.94		C
ATOM	935	O	SER	A	120	−8.988	0.011	−4.907	1.00	41.57		O
ATOM	936	CB	SER	A	120	−8.765	−1.087	−7.888	1.00	48.55		C
ATOM	937	OG	SER	A	120	−9.353	−1.760	−8.986	1.00	60.18		O
ATOM	938	N	THR	A	121	−7.396	−1.579	−4.977	1.00	34.74		N
ATOM	939	CA	THR	A	121	−6.548	−0.974	−3.960	1.00	32.02		C
ATOM	940	C	THR	A	121	−5.820	0.246	−4.520	1.00	36.76		C
ATOM	941	O	THR	A	121	−5.170	0.163	−5.560	1.00	38.97		O
ATOM	942	CB	THR	A	121	−5.515	−1.984	−3.424	1.00	34.58		C
ATOM	943	CG2	THR	A	121	−4.467	−1.287	−2.564	1.00	34.08		C
ATOM	944	OG1	THR	A	121	−6.183	−2.982	−2.643	1.00	35.30		O
ATOM	945	N	LYS	A	122	−5.925	1.374	−3.822	1.00	38.80		N
ATOM	946	CA	LYS	A	122	−5.311	2.619	−4.276	1.00	33.51		C
ATOM	947	C	LYS	A	122	−4.612	3.348	−3.137	1.00	34.96		C
ATOM	948	O	LYS	A	122	−5.217	3.618	−2.103	1.00	36.45		O
ATOM	949	CB	LYS	A	122	−6.364	3.533	−4.907	1.00	31.35		C
ATOM	950	CG	LYS	A	122	−5.799	4.818	−5.474	1.00	41.47		C
ATOM	951	CD	LYS	A	122	−6.894	5.726	−6.013	1.00	44.52		C
ATOM	952	CE	LYS	A	122	−6.300	6.975	−6.653	1.00	45.34		C
ATOM	953	NZ	LYS	A	122	−5.380	7.695	−5.723	1.00	52.67		N
ATOM	954	N	GLY	A	123	−3.336	3.665	−3.328	1.00	34.17		N
ATOM	955	CA	GLY	A	123	−2.581	4.418	−2.344	1.00	31.92		C
ATOM	956	C	GLY	A	123	−2.957	5.889	−2.359	1.00	38.36		C
ATOM	957	O	GLY	A	123	−3.423	6.403	−3.375	1.00	39.10		O
ATOM	958	N	PRO	A	124	−2.747	6.578	−1.228	1.00	35.34		N
ATOM	959	CA	PRO	A	124	−3.181	7.963	−1.024	1.00	33.85		C
ATOM	960	C	PRO	A	124	−2.245	9.021	−1.600	1.00	38.95		C
ATOM	961	O	PRO	A	124	−1.036	8.809	−1.689	1.00	33.76		O
ATOM	962	CB	PRO	A	124	−3.209	8.084	0.497	1.00	31.61		C
ATOM	963	CG	PRO	A	124	−2.100	7.184	0.944	1.00	31.80		C
ATOM	964	CD	PRO	A	124	−2.095	6.024	−0.026	1.00	35.65		C
ATOM	965	N	SER	A	125	−2.817	10.160	−1.974	1.00	31.51		N
ATOM	966	CA	SER	A	125	−2.038	11.366	−2.216	1.00	34.17		C
ATOM	967	C	SER	A	125	−2.015	12.176	−0.926	1.00	32.77		C
ATOM	968	O	SER	A	125	−3.041	12.315	−0.261	1.00	38.58		O
ATOM	969	CB	SER	A	125	−2.631	12.189	−3.362	1.00	40.17		C
ATOM	970	OG	SER	A	125	−2.812	11.397	−4.524	1.00	45.30		O
ATOM	971	N	VAL	A	126	−0.851	12.695	−0.557	1.00	28.64		N
ATOM	972	CA	VAL	A	126	−0.734	13.466	0.674	1.00	28.98		C
ATOM	973	C	VAL	A	126	−0.444	14.927	0.363	1.00	33.93		C
ATOM	974	O	VAL	A	126	0.556	15.244	−0.279	1.00	37.76		O
ATOM	975	CB	VAL	A	126	0.367	12.905	1.593	1.00	28.89		C
ATOM	976	CG1	VAL	A	126	0.374	13.641	2.930	1.00	28.32		C
ATOM	977	CG2	VAL	A	126	0.169	11.413	1.797	1.00	24.48		C
ATOM	978	N	PHE	A	127	−1.325	15.809	0.825	1.00	29.15		N
ATOM	979	CA	PHE	A	127	−1.212	17.236	0.557	1.00	31.17		C
ATOM	980	C	PHE	A	127	−1.034	18.028	1.850	1.00	38.80		C
ATOM	981	O	PHE	A	127	−1.578	17.657	2.892	1.00	31.26		O
ATOM	982	CB	PHE	A	127	−2.448	17.739	−0.198	1.00	29.74		C
ATOM	983	CG	PHE	A	127	−2.709	17.013	−1.484	1.00	32.93		C
ATOM	984	CD1	PHE	A	127	−1.798	17.076	−2.529	1.00	36.91		C
ATOM	985	CD2	PHE	A	127	−3.869	16.275	−1.657	1.00	33.66		C
ATOM	986	CE1	PHE	A	127	−2.033	16.407	−3.718	1.00	30.94		C
ATOM	987	CE2	PHE	A	127	−4.114	15.605	−2.848	1.00	38.29		C
ATOM	988	CZ	PHE	A	127	−3.194	15.670	−3.878	1.00	33.93		C
ATOM	989	N	PRO	A	128	−0.278	19.134	1.785	1.00	38.69		N
ATOM	990	CA	PRO	A	128	−0.029	19.931	2.990	1.00	31.44		C
ATOM	991	C	PRO	A	128	−1.230	20.772	3.410	1.00	34.99		C
ATOM	992	O	PRO	A	128	−1.930	21.318	2.562	1.00	36.42		O
ATOM	993	CB	PRO	A	128	1.136	20.832	2.575	1.00	35.21		C
ATOM	994	CG	PRO	A	128	0.966	20.997	1.104	1.00	31.99		C
ATOM	995	CD	PRO	A	128	0.395	19.694	0.598	1.00	31.14		C
ATOM	996	N	LEU	A	129	−1.470	20.845	4.714	1.00	31.68		N
ATOM	997	CA	LEU	A	129	−2.354	21.853	5.280	1.00	32.81		C
ATOM	998	C	LEU	A	129	−1.451	22.903	5.908	1.00	29.54		C
ATOM	999	O	LEU	A	129	−1.054	22.777	7.063	1.00	28.79		O
ATOM	1000	CB	LEU	A	129	−3.309	21.249	6.314	1.00	28.35		C
ATOM	1001	CG	LEU	A	129	−4.272	20.181	5.787	1.00	32.12		C
ATOM	1002	CD1	LEU	A	129	−5.104	19.577	6.917	1.00	27.87		C
ATOM	1003	CD2	LEU	A	129	−5.170	20.762	4.700	1.00	27.99		C
ATOM	1004	N	ALA	A	130	−1.106	23.923	5.130	1.00	30.89		N
ATOM	1005	CA	ALA	A	130	−0.044	24.853	5.509	1.00	38.77		C
ATOM	1006	C	ALA	A	130	−0.484	25.820	6.595	1.00	37.50		C
ATOM	1007	O	ALA	A	130	−1.576	26.378	6.524	1.00	41.37		O
ATOM	1008	CB	ALA	A	130	0.445	25.624	4.286	1.00	37.41		C
ATOM	1009	N	PRO	A	131	0.381	26.031	7.599	1.00	45.74		N
ATOM	1010	CA	PRO	A	131	0.059	26.928	8.714	1.00	46.02		C
ATOM	1011	C	PRO	A	131	−0.111	28.370	8.245	1.00	52.71		C
ATOM	1012	O	PRO	A	131	0.650	28.845	7.397	1.00	47.91		O
ATOM	1013	CB	PRO	A	131	1.264	26.778	9.647	1.00	40.81		C
ATOM	1014	CG	PRO	A	131	2.376	26.354	8.764	1.00	45.92		C
ATOM	1015	CD	PRO	A	131	1.751	25.499	7.694	1.00	43.34		C
ATOM	1016	N	SER	A	132	−1.117	29.043	8.793	1.00	55.56		N
ATOM	1017	CA	SER	A	132	−1.473	30.396	8.380	1.00	71.89		C
ATOM	1018	C	SER	A	132	−0.309	31.371	8.517	1.00	74.46		C
ATOM	1019	O	SER	A	132	0.408	31.364	9.518	1.00	79.24		O
ATOM	1020	CB	SER	A	132	−2.670	30.896	9.198	1.00	76.95		C
ATOM	1021	OG	SER	A	132	−3.053	32.204	8.811	1.00	77.97		O
ATOM	1022	N	SER	A	133	−0.120	32.201	7.496	1.00	80.68		N
ATOM	1023	CA	SER	A	133	0.838	33.296	7.575	1.00	89.81		C
ATOM	1024	C	SER	A	133	0.309	34.331	8.560	1.00	95.47		C
ATOM	1025	O	SER	A	133	1.072	35.087	9.166	1.00	92.23		O
ATOM	1026	CB	SER	A	133	1.075	33.922	6.198	1.00	81.20		C
ATOM	1027	OG	SER	A	133	−0.144	34.340	5.609	1.00	74.80		O
ATOM	1028	N	LYS	A	134	−1.012	34.343	8.717	1.00	93.18		N
ATOM	1029	CA	LYS	A	134	−1.678	35.224	9.665	1.00	90.77		C
ATOM	1030	C	LYS	A	134	−1.923	34.525	11.001	1.00	94.50		C
ATOM	1031	O	LYS	A	134	−2.896	34.825	11.696	1.00	94.00		O
ATOM	1032	CB	LYS	A	134	−3.003	35.729	9.089	1.00	86.16		C
ATOM	1033	CG	LYS	A	134	−2.852	36.635	7.879	1.00	83.75		C
ATOM	1034	CD	LYS	A	134	−4.135	37.409	7.614	1.00	91.56		C
ATOM	1035	CE	LYS	A	134	−3.926	38.492	6.567	1.00	95.47		C
ATOM	1036	NZ	LYS	A	134	−5.110	39.389	6.446	1.00	88.66		N
ATOM	1037	N	SER	A	135	−1.045	33.588	11.353	1.00	96.11		N
ATOM	1038	CA	SER	A	135	−1.111	32.936	12.658	1.00	97.73		C
ATOM	1039	C	SER	A	135	−0.885	33.973	13.753	1.00	102.54		C
ATOM	1040	O	SER	A	135	−0.148	34.941	13.555	1.00	102.52		O
ATOM	1041	CB	SER	A	135	−0.077	31.810	12.768	1.00	83.08		C
ATOM	1042	OG	SER	A	135	−0.335	30.775	11.834	1.00	78.24		O
ATOM	1043	N	THR	A	136	−1.524	33.775	14.901	1.00	102.47		N
ATOM	1044	CA	THR	A	136	−1.399	34.717	16.009	1.00	105.40		C
ATOM	1045	C	THR	A	136	0.030	34.741	16.550	1.00	104.11		C
ATOM	1046	O	THR	A	136	0.518	33.744	17.085	1.00	99.44		O
ATOM	1047	CB	THR	A	136	−2.377	34.379	17.154	1.00	99.90		C
ATOM	1048	CG2	THR	A	136	−3.817	34.548	16.692	1.00	100.80		C
ATOM	1049	OG1	THR	A	136	−2.173	33.027	17.582	1.00	97.52		O
ATOM	1050	N	SER	A	137	0.696	35.883	16.395	1.00	105.35		N
ATOM	1051	CA	SER	A	137	2.071	36.049	16.858	1.00	104.45		C
ATOM	1052	C	SER	A	137	2.168	35.866	18.370	1.00	102.60		C
ATOM	1053	O	SER	A	137	1.517	36.580	19.135	1.00	98.58		O
ATOM	1054	CB	SER	A	137	2.610	37.424	16.456	1.00	105.78		C
ATOM	1055	OG	SER	A	137	2.624	37.578	15.047	1.00	96.80		O
ATOM	1056	N	GLY	A	138	2.981	34.902	18.790	1.00	97.35		N
ATOM	1057	CA	GLY	A	138	3.115	34.571	20.197	1.00	98.58		C
ATOM	1058	C	GLY	A	138	1.978	33.692	20.685	1.00	99.72		C
ATOM	1059	O	GLY	A	138	1.816	33.480	21.888	1.00	98.83		O
ATOM	1060	N	GLY	A	139	1.188	33.180	19.744	1.00	93.81		N
ATOM	1061	CA	GLY	A	139	0.044	32.348	20.066	1.00	77.07		C
ATOM	1062	C	GLY	A	139	0.181	30.926	19.557	1.00	70.80		C
ATOM	1063	O	GLY	A	139	1.247	30.316	19.662	1.00	65.42		O
ATOM	1064	N	THR	A	140	−0.904	30.398	18.998	1.00	65.95		N
ATOM	1065	CA	THR	A	140	−0.941	29.012	18.541	1.00	60.59		C
ATOM	1066	C	THR	A	140	−1.281	28.906	17.053	1.00	54.28		C
ATOM	1067	O	THR	A	140	−2.238	29.520	16.580	1.00	54.81		O
ATOM	1068	CB	THR	A	140	−1.963	28.189	19.360	1.00	57.65		C
ATOM	1069	CG2	THR	A	140	−2.218	26.832	18.719	1.00	45.39		C
ATOM	1070	OG1	THR	A	140	−1.463	27.993	20.689	1.00	65.11		O
ATOM	1071	N	ALA	A	141	−0.488	28.129	16.321	1.00	41.19		N
ATOM	1072	CA	ALA	A	141	−0.767	27.862	14.914	1.00	47.82		C
ATOM	1073	C	ALA	A	141	−1.193	26.410	14.708	1.00	39.86		C
ATOM	1074	O	ALA	A	141	−0.881	25.541	15.521	1.00	42.63		O
ATOM	1075	CB	ALA	A	141	0.447	28.181	14.059	1.00	33.31		C
ATOM	1076	N	ALA	A	142	−1.911	26.151	13.621	1.00	35.54		N
ATOM	1077	CA	ALA	A	142	−2.279	24.787	13.265	1.00	32.56		C
ATOM	1078	C	ALA	A	142	−1.747	24.446	11.885	1.00	30.50		C
ATOM	1079	O	ALA	A	142	−1.761	25.276	10.978	1.00	39.38		O
ATOM	1080	CB	ALA	A	142	−3.791	24.600	13.317	1.00	33.11		C
ATOM	1081	N	LEU	A	143	−1.267	23.220	11.735	1.00	29.03		N
ATOM	1082	CA	LEU	A	143	−0.827	22.726	10.447	1.00	27.15		C
ATOM	1083	C	LEU	A	143	−1.214	21.263	10.343	1.00	29.85		C
ATOM	1084	O	LEU	A	143	−1.577	20.643	11.340	1.00	30.37		O
ATOM	1085	CB	LEU	A	143	0.681	22.922	10.267	1.00	31.63		C
ATOM	1086	CG	LEU	A	143	1.648	22.236	11.232	1.00	36.90		C
ATOM	1087	CD1	LEU	A	143	2.145	20.915	10.665	1.00	35.87		C
ATOM	1088	CD2	LEU	A	143	2.817	23.154	11.551	1.00	37.42		C
ATOM	1089	N	GLY	A	144	−1.155	20.708	9.140	1.00	25.86		N
ATOM	1090	CA	GLY	A	144	−1.542	19.327	8.968	1.00	28.52		C
ATOM	1091	C	GLY	A	144	−1.254	18.715	7.615	1.00	24.81		C
ATOM	1092	O	GLY	A	144	−0.577	19.300	6.774	1.00	28.21		O
ATOM	1093	N	CYS	A	145	−1.779	17.511	7.428	1.00	23.50		N
ATOM	1094	CA	CYS	A	145	−1.680	16.777	6.178	1.00	26.22		C
ATOM	1095	C	CYS	A	145	−3.059	16.307	5.759	1.00	29.48		C
ATOM	1096	O	CYS	A	145	−3.828	15.820	6.587	1.00	28.29		O
ATOM	1097	CB	CYS	A	145	−0.745	15.567	6.317	1.00	32.48		C
ATOM	1098	SG	CYS	A	145	1.014	15.968	6.295	1.00	53.28		S
ATOM	1099	N	LEU	A	146	−3.364	16.447	4.475	1.00	31.34		N
ATOM	1100	CA	LEU	A	146	−4.579	15.883	3.911	1.00	25.63		C
ATOM	1101	C	LEU	A	146	−4.235	14.603	3.157	1.00	30.29		C
ATOM	1102	O	LEU	A	146	−3.490	14.627	2.177	1.00	34.41		O
ATOM	1103	CB	LEU	A	146	−5.265	16.895	2.991	1.00	30.65		C
ATOM	1104	CG	LEU	A	146	−6.575	16.493	2.311	1.00	36.27		C
ATOM	1105	CD1	LEU	A	146	−7.664	16.170	3.329	1.00	29.24		C
ATOM	1106	CD2	LEU	A	146	−7.027	17.607	1.378	1.00	36.45		C
ATOM	1107	N	VAL	A	147	−4.772	13.485	3.628	1.00	30.39		N
ATOM	1108	CA	VAL	A	147	−4.504	12.182	3.033	1.00	27.86		C
ATOM	1109	C	VAL	A	147	−5.700	11.750	2.184	1.00	27.94		C
ATOM	1110	O	VAL	A	147	−6.718	11.321	2.711	1.00	33.43		O
ATOM	1111	CB	VAL	A	147	−4.209	11.143	4.123	1.00	30.05		C
ATOM	1112	CG1	VAL	A	147	−3.807	9.811	3.509	1.00	31.17		C
ATOM	1113	CG2	VAL	A	147	−3.116	11.661	5.053	1.00	29.02		C
ATOM	1114	N	LYS	A	148	−5.579	11.870	0.866	1.00	32.05		N
ATOM	1115	CA	LYS	A	148	−6.760	11.820	0.010	1.00	38.00		C
ATOM	1116	C	LYS	A	148	−6.740	10.696	−1.026	1.00	35.47		C
ATOM	1117	O	LYS	A	148	−5.685	10.328	−1.539	1.00	38.98		O
ATOM	1118	CB	LYS	A	148	−6.935	13.172	−0.697	1.00	39.17		C
ATOM	1119	CG	LYS	A	148	−8.280	13.343	−1.383	1.00	47.97		C
ATOM	1120	CD	LYS	A	148	−8.527	14.785	−1.779	1.00	41.88		C
ATOM	1121	CE	LYS	A	148	−9.901	14.951	−2.417	1.00	51.38		C
ATOM	1122	NZ	LYS	A	148	−10.035	14.191	−3.688	1.00	52.46		N
ATOM	1123	N	ASP	A	149	−7.929	10.160	−1.309	1.00	39.61		N
ATOM	1124	CA	ASP	A	149	−8.162	9.206	−2.398	1.00	36.49		C
ATOM	1125	C	ASP	A	149	−7.423	7.886	−2.225	1.00	40.38		C
ATOM	1126	O	ASP	A	149	−6.620	7.499	−3.076	1.00	38.28		O
ATOM	1127	CB	ASP	A	149	−7.779	9.829	−3.748	1.00	35.81		C
ATOM	1128	CG	ASP	A	149	−8.690	10.975	−4.139	1.00	44.23		C
ATOM	1129	OD1	ASP	A	149	−9.834	11.014	−3.642	1.00	45.39		O
ATOM	1130	OD2	ASP	A	149	−8.265	11.835	−4.940	1.00	51.78		O
ATOM	1131	N	TYR	A	150	−7.702	7.185	−1.133	1.00	28.61		N
ATOM	1132	CA	TYR	A	150	−7.115	5.872	−0.950	1.00	31.03		C
ATOM	1133	C	TYR	A	150	−8.197	4.827	−0.728	1.00	38.37		C
ATOM	1134	O	TYR	A	150	−9.354	5.159	−0.456	1.00	36.04		O
ATOM	1135	CB	TYR	A	150	−6.113	5.872	0.212	1.00	29.48		C
ATOM	1136	CG	TYR	A	150	−6.713	6.143	1.571	1.00	32.63		C
ATOM	1137	CD1	TYR	A	150	−6.837	7.439	2.051	1.00	31.16		C
ATOM	1138	CD2	TYR	A	150	−7.145	5.100	2.380	1.00	34.56		C
ATOM	1139	CE1	TYR	A	150	−7.381	7.689	3.295	1.00	26.37		C
ATOM	1140	CE2	TYR	A	150	−7.691	5.340	3.625	1.00	30.49		C
ATOM	1141	CZ	TYR	A	150	−7.804	6.633	4.079	1.00	32.92		C
ATOM	1142	OH	TYR	A	150	−8.347	6.865	5.322	1.00	33.53		O
ATOM	1143	N	PHE	A	151	−7.807	3.565	−0.866	1.00	30.04		N
ATOM	1144	CA	PHE	A	151	−8.699	2.437	−0.650	1.00	32.42		C
ATOM	1145	C	PHE	A	151	−7.861	1.173	−0.518	1.00	32.34		C
ATOM	1146	O	PHE	A	151	−6.895	0.992	−1.258	1.00	38.41		O
ATOM	1147	CB	PHE	A	151	−9.708	2.298	−1.799	1.00	32.75		C
ATOM	1148	CG	PHE	A	151	−10.788	1.287	−1.535	1.00	35.46		C
ATOM	1149	CD2	PHE	A	151	−11.978	1.669	−0.936	1.00	38.75		C
ATOM	1150	CD1	PHE	A	151	−10.605	−0.047	−1.863	1.00	36.37		C
ATOM	1151	CE2	PHE	A	151	−12.969	0.743	−0.676	1.00	37.03		C
ATOM	1152	CE1	PHE	A	151	−11.595	−0.981	−1.605	1.00	36.99		C
ATOM	1153	CZ	PHE	A	151	−12.777	−0.584	−1.013	1.00	38.87		C
ATOM	1154	N	PRO	A	152	−8.207	0.307	0.446	1.00	36.93		N
ATOM	1155	CA	PRO	A	152	−9.241	0.535	1.456	1.00	33.39		C
ATOM	1156	C	PRO	A	152	−8.638	1.119	2.726	1.00	36.06		C
ATOM	1157	O	PRO	A	152	−7.493	1.579	2.706	1.00	30.72		O
ATOM	1158	CB	PRO	A	152	−9.775	−0.869	1.707	1.00	35.39		C
ATOM	1159	CG	PRO	A	152	−8.534	−1.711	1.609	1.00	34.66		C
ATOM	1160	CD	PRO	A	152	−7.652	−1.056	0.552	1.00	34.24		C
ATOM	1161	N	GLU	A	153	−9.400	1.095	3.816	1.00	31.54		N
ATOM	1162	CA	GLU	A	153	−8.855	1.413	5.132	1.00	35.20		C
ATOM	1163	C	GLU	A	153	−7.853	0.323	5.528	1.00	30.90		C
ATOM	1164	O	GLU	A	153	−7.918	−0.790	5.012	1.00	30.88		O
ATOM	1165	CB	GLU	A	153	−9.979	1.531	6.170	1.00	34.19		C
ATOM	1166	CG	GLU	A	153	−10.884	2.735	5.978	1.00	30.47		C
ATOM	1167	CD	GLU	A	153	−10.607	3.838	6.980	1.00	49.19		C
ATOM	1168	OE1	GLU	A	153	−11.550	4.226	7.705	1.00	56.79		O
ATOM	1169	OE2	GLU	A	153	−9.452	4.323	7.042	1.00	53.78		O
ATOM	1170	N	PRO	A	154	−6.923	0.634	6.444	1.00	31.40		N
ATOM	1171	CA	PRO	A	154	−6.719	1.915	7.118	1.00	33.58		C
ATOM	1172	C	PRO	A	154	−5.436	2.624	6.692	1.00	34.09		C
ATOM	1173	O	PRO	A	154	−4.576	2.024	6.047	1.00	33.03		O
ATOM	1174	CB	PRO	A	154	−6.614	1.494	8.576	1.00	27.86		C
ATOM	1175	CG	PRO	A	154	−5.808	0.210	8.476	1.00	30.94		C
ATOM	1176	CD	PRO	A	154	−6.178	−0.435	7.133	1.00	33.22		C
ATOM	1177	N	VAL	A	155	−5.306	3.892	7.059	1.00	34.38		N
ATOM	1178	CA	VAL	A	155	−4.006	4.540	7.013	1.00	35.85		C
ATOM	1179	C	VAL	A	155	−3.648	4.982	8.420	1.00	35.04		C
ATOM	1180	O	VAL	A	155	−4.525	5.310	9.219	1.00	34.51		O
ATOM	1181	CB	VAL	A	155	−3.966	5.755	6.060	1.00	36.38		C
ATOM	1182	CG1	VAL	A	155	−4.367	5.351	4.656	1.00	37.19		C
ATOM	1183	CG2	VAL	A	155	−4.850	6.870	6.572	1.00	41.10		C
ATOM	1184	N	THR	A	156	−2.358	4.966	8.730	1.00	32.78		N
ATOM	1185	CA	THR	A	156	−1.887	5.503	9.994	1.00	29.21		C
ATOM	1186	C	THR	A	156	−1.074	6.759	9.733	1.00	35.34		C
ATOM	1187	O	THR	A	156	−0.448	6.916	8.675	1.00	29.04		O
ATOM	1188	CB	THR	A	156	−1.034	4.487	10.785	1.00	34.00		C
ATOM	1189	CG2	THR	A	156	−1.843	3.230	11.088	1.00	33.80		C
ATOM	1190	OG1	THR	A	156	0.132	4.140	10.028	1.00	35.62		O
ATOM	1191	N	VAL	A	157	−1.099	7.665	10.700	1.00	27.89		N
ATOM	1192	CA	VAL	A	157	−0.375	8.916	10.582	1.00	33.47		C
ATOM	1193	C	VAL	A	157	0.370	9.197	11.867	1.00	28.46		C
ATOM	1194	O	VAL	A	157	−0.216	9.168	12.949	1.00	36.97		O
ATOM	1195	CB	VAL	A	157	−1.319	10.100	10.276	1.00	28.34		C
ATOM	1196	CG1	VAL	A	157	−0.523	11.395	10.154	1.00	28.04		C
ATOM	1197	CG2	VAL	A	157	−2.120	9.833	9.011	1.00	26.05		C
ATOM	1198	N	SER	A	158	1.665	9.455	11.752	1.00	30.73		N
ATOM	1199	CA	SER	A	158	2.429	9.964	12.880	1.00	36.51		C
ATOM	1200	C	SER	A	158	3.087	11.267	12.461	1.00	32.08		C
ATOM	1201	O	SER	A	158	3.162	11.571	11.270	1.00	30.98		O
ATOM	1202	CB	SER	A	158	3.476	8.951	13.347	1.00	35.17		C
ATOM	1203	OG	SER	A	158	4.538	8.848	12.419	1.00	40.81		O
ATOM	1204	N	TRP	A	159	3.546	12.040	13.440	1.00	27.85		N
ATOM	1205	CA	TRP	A	159	4.263	13.276	13.166	1.00	30.67		C
ATOM	1206	C	TRP	A	159	5.684	13.207	13.707	1.00	31.39		C
ATOM	1207	O	TRP	A	159	5.900	12.792	14.845	1.00	30.84		O
ATOM	1208	CB	TRP	A	159	3.519	14.470	13.761	1.00	28.15		C
ATOM	1209	CG	TRP	A	159	2.278	14.795	13.004	1.00	35.31		C
ATOM	1210	CD1	TRP	A	159	1.049	14.237	13.170	1.00	31.91		C
ATOM	1211	CD2	TRP	A	159	2.149	15.745	11.942	1.00	33.46		C
ATOM	1212	CE2	TRP	A	159	0.807	15.716	11.518	1.00	32.34		C
ATOM	1213	CE3	TRP	A	159	3.038	16.620	11.310	1.00	33.99		C
ATOM	1214	NE1	TRP	A	159	0.157	14.784	12.283	1.00	31.36		N
ATOM	1215	CZ2	TRP	A	159	0.331	16.526	10.489	1.00	30.53		C
ATOM	1216	CZ3	TRP	A	159	2.565	17.423	10.289	1.00	30.89		C
ATOM	1217	CH2	TRP	A	159	1.223	17.372	9.890	1.00	33.28		C
ATOM	1218	N	ASN	A	160	6.639	13.617	12.875	1.00	26.79		N
ATOM	1219	CA	ASN	A	160	8.061	13.584	13.208	1.00	28.03		C
ATOM	1220	C	ASN	A	160	8.491	12.236	13.778	1.00	33.44		C
ATOM	1221	O	ASN	A	160	9.200	12.171	14.784	1.00	32.52		O
ATOM	1222	CB	ASN	A	160	8.405	14.708	14.185	1.00	27.50		C
ATOM	1223	CG	ASN	A	160	8.269	16.078	13.559	1.00	30.24		C
ATOM	1224	ND2	ASN	A	160	8.292	17.119	14.385	1.00	34.83		N
ATOM	1225	OD1	ASN	A	160	8.153	16.199	12.342	1.00	37.06		O
ATOM	1226	N	SER	A	161	8.026	11.168	13.135	1.00	32.54		N
ATOM	1227	CA	SER	A	161	8.394	9.801	13.492	1.00	38.63		C
ATOM	1228	C	SER	A	161	7.988	9.425	14.916	1.00	37.84		C
ATOM	1229	O	SER	A	161	8.601	8.556	15.530	1.00	36.85		O
ATOM	1230	CB	SER	A	161	9.901	9.598	13.310	1.00	33.00		C
ATOM	1231	OG	SER	A	161	10.292	9.901	11.983	1.00	36.60		O
ATOM	1232	N	GLY	A	162	6.951	10.074	15.434	1.00	33.46		N
ATOM	1233	CA	GLY	A	162	6.456	9.771	16.764	1.00	33.72		C
ATOM	1234	C	GLY	A	162	7.005	10.686	17.843	1.00	35.30		C
ATOM	1235	O	GLY	A	162	6.639	10.568	19.011	1.00	42.69		O
ATOM	1236	N	ALA	A	163	7.885	11.602	17.457	1.00	37.22		N
ATOM	1237	CA	ALA	A	163	8.439	12.561	18.405	1.00	36.88		C
ATOM	1238	C	ALA	A	163	7.428	13.661	18.725	1.00	41.59		C
ATOM	1239	O	ALA	A	163	7.524	14.318	19.762	1.00	40.49		O
ATOM	1240	CB	ALA	A	163	9.725	13.165	17.865	1.00	30.59		C
ATOM	1241	N	LEU	A	164	6.460	13.858	17.833	1.00	36.52		N
ATOM	1242	CA	LEU	A	164	5.423	14.863	18.052	1.00	35.71		C
ATOM	1243	C	LEU	A	164	4.089	14.180	18.333	1.00	36.12		C
ATOM	1244	O	LEU	A	164	3.517	13.513	17.468	1.00	35.37		O
ATOM	1245	CB	LEU	A	164	5.316	15.802	16.849	1.00	30.79		C
ATOM	1246	CG	LEU	A	164	4.328	16.965	16.961	1.00	36.59		C
ATOM	1247	CD1	LEU	A	164	4.537	17.756	18.256	1.00	36.35		C
ATOM	1248	CD2	LEU	A	164	4.450	17.875	15.752	1.00	33.18		C
ATOM	1249	N	THR	A	165	3.601	14.359	19.555	1.00	33.05		N
ATOM	1250	CA	THR	A	165	2.442	13.623	20.048	1.00	39.48		C
ATOM	1251	C	THR	A	165	1.347	14.555	20.562	1.00	39.43		C
ATOM	1252	O	THR	A	165	0.164	14.353	20.285	1.00	39.07		O
ATOM	1253	CB	THR	A	165	2.864	12.646	21.174	1.00	34.92		C
ATOM	1254	CG2	THR	A	165	1.693	12.309	22.089	1.00	52.65		C
ATOM	1255	OG1	THR	A	165	3.367	11.442	20.588	1.00	50.23		O
ATOM	1256	N	SER	A	166	1.750	15.577	21.308	1.00	33.38		N
ATOM	1257	CA	SER	A	166	0.804	16.495	21.930	1.00	35.48		C
ATOM	1258	C	SER	A	166	0.202	17.452	20.915	1.00	34.11		C
ATOM	1259	O	SER	A	166	0.920	18.061	20.123	1.00	37.38		O
ATOM	1260	CB	SER	A	166	1.487	17.285	23.047	1.00	37.23		C
ATOM	1261	OG	SER	A	166	2.094	16.406	23.982	1.00	58.12		O
ATOM	1262	N	GLY	A	167	−1.120	17.583	20.945	1.00	36.94		N
ATOM	1263	CA	GLY	A	167	−1.809	18.532	20.090	1.00	35.05		C
ATOM	1264	C	GLY	A	167	−2.196	17.943	18.750	1.00	38.60		C
ATOM	1265	O	GLY	A	167	−2.701	18.650	17.879	1.00	38.31		O
ATOM	1266	N	VAL	A	168	−1.965	16.643	18.586	1.00	35.11		N
ATOM	1267	CA	VAL	A	168	−2.262	15.968	17.328	1.00	34.52		C
ATOM	1268	C	VAL	A	168	−3.690	15.438	17.297	1.00	33.72		C
ATOM	1269	O	VAL	A	168	−4.145	14.801	18.242	1.00	33.06		O
ATOM	1270	CB	VAL	A	168	−1.295	14.792	17.074	1.00	34.33		C
ATOM	1271	CG1	VAL	A	168	−1.662	14.059	15.783	1.00	32.11		C
ATOM	1272	CG2	VAL	A	168	0.141	15.285	17.027	1.00	30.55		C
ATOM	1273	N	HIS	A	169	−4.392	15.712	16.203	1.00	34.59		N
ATOM	1274	CA	HIS	A	169	−5.693	15.108	15.953	1.00	33.15		C
ATOM	1275	C	HIS	A	169	−5.701	14.463	14.577	1.00	34.43		C
ATOM	1276	O	HIS	A	169	−5.556	15.147	13.561	1.00	32.61		O
ATOM	1277	CB	HIS	A	169	−6.822	16.140	16.039	1.00	33.41		C
ATOM	1278	CG	HIS	A	169	−7.036	16.702	17.409	1.00	38.03		C
ATOM	1279	CD2	HIS	A	169	−6.891	17.961	17.887	1.00	35.39		C
ATOM	1280	ND1	HIS	A	169	−7.482	15.940	18.467	1.00	45.83		N
ATOM	1281	CE1	HIS	A	169	−7.592	16.702	19.541	1.00	37.15		C
ATOM	1282	NE2	HIS	A	169	−7.240	17.933	19.215	1.00	39.39		N
ATOM	1283	N	THR	A	170	−5.857	13.145	14.551	1.00	33.36		N
ATOM	1284	CA	THR	A	170	−6.059	12.424	13.304	1.00	31.63		C
ATOM	1285	C	THR	A	170	−7.525	12.030	13.217	1.00	32.95		C
ATOM	1286	O	THR	A	170	−8.032	11.288	14.056	1.00	37.08		O
ATOM	1287	CB	THR	A	170	−5.168	11.178	13.200	1.00	35.35		C
ATOM	1288	CG2	THR	A	170	−5.437	10.439	11.895	1.00	29.64		C
ATOM	1289	OG1	THR	A	170	−3.792	11.576	13.246	1.00	35.66		O
ATOM	1290	N	PHE	A	171	−8.202	12.553	12.204	1.00	30.34		N
ATOM	1291	CA	PHE	A	171	−9.641	12.398	12.076	1.00	30.60		C
ATOM	1292	C	PHE	A	171	−10.036	11.082	11.422	1.00	29.79		C
ATOM	1293	O	PHE	A	171	−9.297	10.551	10.597	1.00	31.35		O
ATOM	1294	CB	PHE	A	171	−10.214	13.574	11.286	1.00	23.31		C
ATOM	1295	CG	PHE	A	171	−10.141	14.874	12.024	1.00	25.50		C
ATOM	1296	CD2	PHE	A	171	−11.197	15.295	12.810	1.00	29.91		C
ATOM	1297	CD1	PHE	A	171	−9.004	15.662	11.957	1.00	31.55		C
ATOM	1298	CE2	PHE	A	171	−11.133	16.488	13.502	1.00	30.68		C
ATOM	1299	CE1	PHE	A	171	−8.931	16.856	12.647	1.00	36.15		C
ATOM	1300	CZ	PHE	A	171	−10.001	17.269	13.422	1.00	30.59		C
ATOM	1301	N	PRO	A	172	−11.204	10.546	11.805	1.00	35.35		N
ATOM	1302	CA	PRO	A	172	−11.781	9.388	11.117	1.00	36.50		C
ATOM	1303	C	PRO	A	172	−11.928	9.670	9.627	1.00	36.86		C
ATOM	1304	O	PRO	A	172	−12.265	10.794	9.253	1.00	33.48		O
ATOM	1305	CB	PRO	A	172	−13.151	9.225	11.784	1.00	32.84		C
ATOM	1306	CG	PRO	A	172	−12.979	9.826	13.137	1.00	36.13		C
ATOM	1307	CD	PRO	A	172	−12.018	10.968	12.961	1.00	33.84		C
ATOM	1308	N	ALA	A	173	−11.661	8.675	8.791	1.00	32.35		N
ATOM	1309	CA	ALA	A	173	−11.783	8.850	7.349	1.00	35.00		C
ATOM	1310	C	ALA	A	173	−13.237	9.021	6.930	1.00	34.52		C
ATOM	1311	O	ALA	A	173	−14.132	8.415	7.516	1.00	37.71		O
ATOM	1312	CB	ALA	A	173	−11.168	7.666	6.618	1.00	34.54		C
ATOM	1313	N	VAL	A	174	−13.473	9.849	5.920	1.00	33.54		N
ATOM	1314	CA	VAL	A	174	−14.792	9.909	5.307	1.00	33.28		C
ATOM	1315	C	VAL	A	174	−14.737	9.250	3.939	1.00	35.09		C
ATOM	1316	O	VAL	A	174	−13.734	9.348	3.223	1.00	34.87		O
ATOM	1317	CB	VAL	A	174	−15.320	11.360	5.171	1.00	32.47		C
ATOM	1318	CG1	VAL	A	174	−15.378	12.032	6.534	1.00	40.37		C
ATOM	1319	CG2	VAL	A	174	−14.469	12.168	4.196	1.00	37.12		C
ATOM	1320	N	LEU	A	175	−15.809	8.550	3.591	1.00	40.76		N
ATOM	1321	CA	LEU	A	175	−15.921	7.932	2.280	1.00	38.53		C
ATOM	1322	C	LEU	A	175	−16.501	8.941	1.300	1.00	37.30		C
ATOM	1323	O	LEU	A	175	−17.605	9.447	1.494	1.00	43.25		O
ATOM	1324	CB	LEU	A	175	−16.788	6.669	2.344	1.00	37.54		C
ATOM	1325	CG	LEU	A	175	−16.905	5.864	1.047	1.00	40.58		C
ATOM	1326	CD1	LEU	A	175	−15.529	5.519	0.504	1.00	37.07		C
ATOM	1327	CD2	LEU	A	175	−17.733	4.598	1.258	1.00	43.41		C
ATOM	1328	N	GLN	A	176	−15.744	9.239	0.252	1.00	44.15		N
ATOM	1329	CA	GLN	A	176	−16.163	10.211	−0.746	1.00	37.45		C
ATOM	1330	C	GLN	A	176	−17.095	9.569	−1.769	1.00	44.09		C
ATOM	1331	O	GLN	A	176	−17.298	8.356	−1.756	1.00	44.31		O
ATOM	1332	CB	GLN	A	176	−14.941	10.815	−1.439	1.00	39.61		C
ATOM	1333	CG	GLN	A	176	−13.940	11.448	−0.480	1.00	41.98		C
ATOM	1334	CD	GLN	A	176	−12.634	11.818	−1.160	1.00	45.48		C
ATOM	1335	NE2	GLN	A	176	−11.917	10.813	−1.655	1.00	33.19		N
ATOM	1336	OE1	GLN	A	176	−12.270	12.993	−1.231	1.00	52.08		O
ATOM	1337	N	SER	A	177	−17.655	10.390	−2.655	1.00	43.50		N
ATOM	1338	CA	SER	A	177	−18.571	9.913	−3.690	1.00	44.39		C
ATOM	1339	C	SER	A	177	−17.886	8.978	−4.679	1.00	42.75		C
ATOM	1340	O	SER	A	177	−18.534	8.157	−5.323	1.00	48.60		O
ATOM	1341	CB	SER	A	177	−19.180	11.096	−4.443	1.00	49.14		C
ATOM	1342	OG	SER	A	177	−19.961	11.895	−3.575	1.00	52.77		O
ATOM	1343	N	SER	A	178	−16.571	9.116	−4.793	1.00	39.08		N
ATOM	1344	CA	SER	A	178	−15.780	8.312	−5.714	1.00	38.13		C
ATOM	1345	C	SER	A	178	−15.542	6.890	−5.215	1.00	39.53		C
ATOM	1346	O	SER	A	178	−14.972	6.064	−5.930	1.00	46.28		O
ATOM	1347	CB	SER	A	178	−14.435	8.991	−5.957	1.00	43.23		C
ATOM	1348	OG	SER	A	178	−13.792	9.255	−4.720	1.00	49.71		O
ATOM	1349	N	GLY	A	179	−15.960	6.608	−3.985	1.00	41.09		N
ATOM	1350	CA	GLY	A	179	−15.696	5.317	−3.379	1.00	35.99		C
ATOM	1351	C	GLY	A	179	−14.316	5.259	−2.746	1.00	41.20		C
ATOM	1352	O	GLY	A	179	−13.882	4.210	−2.266	1.00	37.34		O
ATOM	1353	N	LEU	A	180	−13.623	6.393	−2.742	1.00	37.81		N
ATOM	1354	CA	LEU	A	180	−12.302	6.482	−2.127	1.00	39.78		C
ATOM	1355	C	LEU	A	180	−12.370	7.247	−0.808	1.00	38.81		C
ATOM	1356	O	LEU	A	180	−13.165	8.179	−0.659	1.00	34.97		O
ATOM	1357	CB	LEU	A	180	−11.310	7.152	−3.082	1.00	38.31		C
ATOM	1358	CG	LEU	A	180	−11.181	6.507	−4.470	1.00	38.11		C
ATOM	1359	CD1	LEU	A	180	−10.351	7.381	−5.408	1.00	33.95		C
ATOM	1360	CD2	LEU	A	180	−10.577	5.119	−4.359	1.00	35.65		C
ATOM	1361	N	TYR	A	181	−11.534	6.849	0.147	1.00	33.32		N
ATOM	1362	CA	TYR	A	181	−11.492	7.494	1.457	1.00	34.27		C
ATOM	1363	C	TYR	A	181	−10.628	8.746	1.466	1.00	36.24		C
ATOM	1364	O	TYR	A	181	−9.805	8.964	0.573	1.00	31.81		O
ATOM	1365	CB	TYR	A	181	−10.969	6.527	2.524	1.00	29.72		C
ATOM	1366	CG	TYR	A	181	−11.916	5.396	2.837	1.00	35.89		C
ATOM	1367	CD1	TYR	A	181	−12.985	5.582	3.707	1.00	33.01		C
ATOM	1368	CD2	TYR	A	181	−11.743	4.140	2.267	1.00	31.28		C
ATOM	1369	CE1	TYR	A	181	−13.859	4.547	4.002	1.00	34.04		C
ATOM	1370	CE2	TYR	A	181	−12.614	3.095	2.560	1.00	35.99		C
ATOM	1371	CZ	TYR	A	181	−13.669	3.306	3.427	1.00	35.87		C
ATOM	1372	OH	TYR	A	181	−14.539	2.278	3.721	1.00	42.84		O
ATOM	1373	N	SER	A	182	−10.815	9.555	2.503	1.00	33.72		N
ATOM	1374	CA	SER	A	182	−9.993	10.731	2.727	1.00	30.09		C
ATOM	1375	C	SER	A	182	−9.965	11.071	4.214	1.00	35.24		C
ATOM	1376	O	SER	A	182	−10.975	10.941	4.907	1.00	35.29		O
ATOM	1377	CB	SER	A	182	−10.521	11.913	1.917	1.00	35.11		C
ATOM	1378	OG	SER	A	182	−9.824	13.099	2.239	1.00	44.24		O
ATOM	1379	N	LEU	A	183	−8.809	11.488	4.713	1.00	24.60		N
ATOM	1380	CA	LEU	A	183	−8.745	11.992	6.077	1.00	33.42		C
ATOM	1381	C	LEU	A	183	−7.713	13.095	6.223	1.00	28.32		C
ATOM	1382	O	LEU	A	183	−6.855	13.293	5.365	1.00	35.46		O
ATOM	1383	CB	LEU	A	183	−8.455	10.858	7.075	1.00	32.60		C
ATOM	1384	CG	LEU	A	183	−7.132	10.092	7.186	1.00	38.46		C
ATOM	1385	CD1	LEU	A	183	−6.003	10.910	7.815	1.00	32.89		C
ATOM	1386	CD2	LEU	A	183	−7.377	8.845	8.013	1.00	35.96		C
ATOM	1387	N	SER	A	184	−7.801	13.812	7.329	1.00	28.07		N
ATOM	1388	CA	SER	A	184	−6.803	14.806	7.644	1.00	30.87		C
ATOM	1389	C	SER	A	184	−6.202	14.512	9.009	1.00	36.19		C
ATOM	1390	O	SER	A	184	−6.846	13.908	9.869	1.00	32.31		O
ATOM	1391	CB	SER	A	184	−7.411	16.198	7.619	1.00	27.57		C
ATOM	1392	OG	SER	A	184	−8.437	16.292	8.586	1.00	37.02		O
ATOM	1393	N	SER	A	185	−4.958	14.930	9.190	1.00	29.68		N
ATOM	1394	CA	SER	A	185	−4.309	14.883	10.487	1.00	27.58		C
ATOM	1395	C	SER	A	185	−3.733	16.254	10.747	1.00	29.16		C
ATOM	1396	O	SER	A	185	−3.023	16.799	9.908	1.00	34.94		O
ATOM	1397	CB	SER	A	185	−3.211	13.822	10.533	1.00	29.89		C
ATOM	1398	OG	SER	A	185	−2.506	13.889	11.762	1.00	33.01		O
ATOM	1399	N	VAL	A	186	−4.051	16.825	11.898	1.00	31.07		N
ATOM	1400	CA	VAL	A	186	−3.573	18.158	12.209	1.00	32.17		C
ATOM	1401	C	VAL	A	186	−2.863	18.166	13.545	1.00	30.53		C
ATOM	1402	O	VAL	A	186	−3.002	17.244	14.347	1.00	29.86		O
ATOM	1403	CB	VAL	A	186	−4.719	19.179	12.231	1.00	30.64		C
ATOM	1404	CG1	VAL	A	186	−5.443	19.180	10.890	1.00	27.44		C
ATOM	1405	CG2	VAL	A	186	−5.684	18.868	13.369	1.00	31.93		C
ATOM	1406	N	VAL	A	187	−2.082	19.211	13.765	1.00	28.24		N
ATOM	1407	CA	VAL	A	187	−1.402	19.397	15.028	1.00	29.57		C
ATOM	1408	C	VAL	A	187	−1.341	20.894	15.298	1.00	33.56		C
ATOM	1409	O	VAL	A	187	−1.156	21.689	14.377	1.00	33.65		O
ATOM	1410	CB	VAL	A	187	0.013	18.764	15.013	1.00	32.42		C
ATOM	1411	CG1	VAL	A	187	0.854	19.335	13.875	1.00	35.03		C
ATOM	1412	CG2	VAL	A	187	0.712	18.946	16.361	1.00	32.60		C
ATOM	1413	N	THR	A	188	−1.553	21.282	16.549	1.00	31.74		N
ATOM	1414	CA	THR	A	188	−1.405	22.674	16.943	1.00	36.08		C
ATOM	1415	C	THR	A	188	−0.048	22.862	17.608	1.00	40.20		C
ATOM	1416	O	THR	A	188	0.332	22.092	18.488	1.00	42.98		O
ATOM	1417	CB	THR	A	188	−2.526	23.122	17.898	1.00	35.80		C
ATOM	1418	CG2	THR	A	188	−3.810	23.379	17.124	1.00	36.31		C
ATOM	1419	OG1	THR	A	188	−2.765	22.093	18.865	1.00	43.98		O
ATOM	1420	N	VAL	A	189	0.685	23.878	17.166	1.00	34.48		N
ATOM	1421	CA	VAL	A	189	2.034	24.144	17.655	1.00	36.93		C
ATOM	1422	C	VAL	A	189	2.205	25.642	17.918	1.00	45.71		C
ATOM	1423	O	VAL	A	189	1.428	26.453	17.409	1.00	48.89		O
ATOM	1424	CB	VAL	A	189	3.105	23.673	16.645	1.00	39.16		C
ATOM	1425	CG1	VAL	A	189	2.983	22.178	16.378	1.00	36.29		C
ATOM	1426	CG2	VAL	A	189	2.999	24.470	15.354	1.00	30.72		C
ATOM	1427	N	PRO	A	190	3.216	26.018	18.719	1.00	45.89		N
ATOM	1428	CA	PRO	A	190	3.473	27.449	18.936	1.00	50.63		C
ATOM	1429	C	PRO	A	190	3.852	28.173	17.644	1.00	48.93		C
ATOM	1430	O	PRO	A	190	4.637	27.643	16.858	1.00	44.98		O
ATOM	1431	CB	PRO	A	190	4.645	27.450	19.924	1.00	48.82		C
ATOM	1432	CG	PRO	A	190	4.553	26.131	20.620	1.00	46.27		C
ATOM	1433	CD	PRO	A	190	4.067	25.170	19.574	1.00	42.43		C
ATOM	1434	N	SER	A	191	3.297	29.364	17.433	1.00	48.29		N
ATOM	1435	CA	SER	A	191	3.581	30.147	16.231	1.00	50.08		C
ATOM	1436	C	SER	A	191	5.068	30.440	16.074	1.00	50.39		C
ATOM	1437	O	SER	A	191	5.585	30.495	14.959	1.00	44.82		O
ATOM	1438	CB	SER	A	191	2.802	31.463	16.249	1.00	57.90		C
ATOM	1439	OG	SER	A	191	1.415	31.239	16.078	1.00	74.28		O
ATOM	1440	N	SER	A	192	5.753	30.618	17.200	1.00	46.04		N
ATOM	1441	CA	SER	A	192	7.169	30.965	17.193	1.00	48.53		C
ATOM	1442	C	SER	A	192	8.062	29.808	16.739	1.00	53.82		C
ATOM	1443	O	SER	A	192	9.241	30.009	16.445	1.00	58.88		O
ATOM	1444	CB	SER	A	192	7.598	31.447	18.582	1.00	52.00		C
ATOM	1445	OG	SER	A	192	7.184	30.541	19.592	1.00	49.57		O
ATOM	1446	N	SER	A	193	7.507	28.601	16.671	1.00	54.17		N
ATOM	1447	CA	SER	A	193	8.299	27.443	16.260	1.00	50.73		C
ATOM	1448	C	SER	A	193	8.291	27.260	14.741	1.00	50.16		C
ATOM	1449	O	SER	A	193	9.128	26.541	14.197	1.00	53.54		O
ATOM	1450	CB	SER	A	193	7.795	26.168	16.944	1.00	44.93		C
ATOM	1451	OG	SER	A	193	6.626	25.670	16.317	1.00	46.77		O
ATOM	1452	N	LEU	A	194	7.349	27.907	14.060	1.00	45.24		N
ATOM	1453	CA	LEU	A	194	7.292	27.842	12.602	1.00	46.01		C
ATOM	1454	C	LEU	A	194	8.520	28.519	12.007	1.00	55.53		C
ATOM	1455	O	LEU	A	194	8.857	29.643	12.376	1.00	62.86		O
ATOM	1456	CB	LEU	A	194	6.021	28.502	12.073	1.00	39.49		C
ATOM	1457	CG	LEU	A	194	4.678	28.001	12.599	1.00	46.53		C
ATOM	1458	CD1	LEU	A	194	3.550	28.840	12.024	1.00	43.35		C
ATOM	1459	CD2	LEU	A	194	4.476	26.535	12.261	1.00	44.15		C
ATOM	1460	N	GLY	A	195	9.195	27.832	11.091	1.00	59.38		N
ATOM	1461	CA	GLY	A	195	10.422	28.355	10.519	1.00	62.95		C
ATOM	1462	C	GLY	A	195	11.653	27.847	11.246	1.00	59.76		C
ATOM	1463	O	GLY	A	195	12.729	27.733	10.660	1.00	64.18		O
ATOM	1464	N	THR	A	196	11.493	27.540	12.529	1.00	59.45		N
ATOM	1465	CA	THR	A	196	12.570	26.958	13.320	1.00	58.51		C
ATOM	1466	C	THR	A	196	12.448	25.434	13.387	1.00	60.43		C
ATOM	1467	O	THR	A	196	13.414	24.713	13.138	1.00	61.86		O
ATOM	1468	CB	THR	A	196	12.583	27.522	14.754	1.00	61.27		C
ATOM	1469	CG2	THR	A	196	13.706	26.891	15.568	1.00	57.43		C
ATOM	1470	OG1	THR	A	196	12.767	28.942	14.708	1.00	68.83		O
ATOM	1471	N	GLN	A	197	11.254	24.954	13.725	1.00	49.07		N
ATOM	1472	CA	GLN	A	197	11.009	23.525	13.894	1.00	41.26		C
ATOM	1473	C	GLN	A	197	10.473	22.872	12.619	1.00	42.46		C
ATOM	1474	O	GLN	A	197	9.577	23.400	11.963	1.00	40.55		O
ATOM	1475	CB	GLN	A	197	10.030	23.290	15.049	1.00	44.12		C
ATOM	1476	CG	GLN	A	197	9.629	21.833	15.242	1.00	47.27		C
ATOM	1477	CD	GLN	A	197	10.769	20.968	15.751	1.00	57.04		C
ATOM	1478	NE2	GLN	A	197	10.939	19.790	15.150	1.00	43.31		N
ATOM	1479	OE1	GLN	A	197	11.490	21.354	16.673	1.00	51.73		O
ATOM	1480	N	THR	A	198	11.034	21.719	12.273	1.00	41.32		N
ATOM	1481	CA	THR	A	198	10.577	20.958	11.121	1.00	35.03		C
ATOM	1482	C	THR	A	198	9.365	20.113	11.502	1.00	36.05		C
ATOM	1483	O	THR	A	198	9.359	19.468	12.550	1.00	35.98		O
ATOM	1484	CB	THR	A	198	11.705	20.058	10.565	1.00	33.49		C
ATOM	1485	CG2	THR	A	198	11.153	19.010	9.620	1.00	33.33		C
ATOM	1486	OG1	THR	A	198	12.644	20.870	9.848	1.00	47.14		O
ATOM	1487	N	TYR	A	199	8.334	20.141	10.660	1.00	34.82		N
ATOM	1488	CA	TYR	A	199	7.135	19.338	10.882	1.00	33.85		C
ATOM	1489	C	TYR	A	199	6.877	18.409	9.704	1.00	31.69		C
ATOM	1490	O	TYR	A	199	6.644	18.859	8.582	1.00	34.22		O
ATOM	1491	CB	TYR	A	199	5.924	20.238	11.129	1.00	28.42		C
ATOM	1492	CG	TYR	A	199	6.043	21.030	12.407	1.00	33.72		C
ATOM	1493	CD1	TYR	A	199	5.935	20.405	13.640	1.00	27.74		C
ATOM	1494	CD2	TYR	A	199	6.288	22.398	12.385	1.00	27.12		C
ATOM	1495	CE1	TYR	A	199	6.058	21.120	14.822	1.00	37.15		C
ATOM	1496	CE2	TYR	A	199	6.412	23.122	13.561	1.00	35.98		C
ATOM	1497	CZ	TYR	A	199	6.294	22.477	14.776	1.00	33.49		C
ATOM	1498	OH	TYR	A	199	6.414	23.184	15.948	1.00	40.19		O
ATOM	1499	N	ILE	A	200	6.935	17.108	9.969	1.00	30.26		N
ATOM	1500	CA	ILE	A	200	6.768	16.097	8.933	1.00	31.27		C
ATOM	1501	C	ILE	A	200	5.710	15.089	9.347	1.00	33.53		C
ATOM	1502	O	ILE	A	200	5.768	14.546	10.452	1.00	32.98		O
ATOM	1503	CB	ILE	A	200	8.093	15.352	8.644	1.00	32.27		C
ATOM	1504	CG1	ILE	A	200	9.164	16.333	8.160	1.00	37.70		C
ATOM	1505	CG2	ILE	A	200	7.880	14.236	7.619	1.00	26.84		C
ATOM	1506	CD1	ILE	A	200	10.495	15.689	7.860	1.00	36.87		C
ATOM	1507	N	CYS	A	201	4.739	14.842	8.470	1.00	28.73		N
ATOM	1508	CA	CYS	A	201	3.747	13.812	8.746	1.00	31.40		C
ATOM	1509	C	CYS	A	201	4.129	12.523	8.032	1.00	31.76		C
ATOM	1510	O	CYS	A	201	4.442	12.518	6.837	1.00	30.36		O
ATOM	1511	CB	CYS	A	201	2.338	14.264	8.341	1.00	29.40		C
ATOM	1512	SG	CYS	A	201	1.974	14.198	6.581	1.00	46.24		S
ATOM	1513	N	ASN	A	202	4.123	11.434	8.788	1.00	32.10		N
ATOM	1514	CA	ASN	A	202	4.479	10.126	8.262	1.00	32.09		C
ATOM	1515	C	ASN	A	202	3.216	9.332	7.990	1.00	30.31		C
ATOM	1516	O	ASN	A	202	2.476	8.990	8.908	1.00	34.67		O
ATOM	1517	CB	ASN	A	202	5.384	9.380	9.243	1.00	31.62		C
ATOM	1518	CG	ASN	A	202	6.445	10.276	9.849	1.00	34.57		C
ATOM	1519	ND2	ASN	A	202	7.425	10.661	9.041	1.00	31.78		N
ATOM	1520	OD1	ASN	A	202	6.382	10.621	11.030	1.00	37.73		O
ATOM	1521	N	VAL	A	203	2.958	9.057	6.722	1.00	31.29		N
ATOM	1522	CA	VAL	A	203	1.730	8.384	6.341	1.00	29.99		C
ATOM	1523	C	VAL	A	203	2.037	6.982	5.860	1.00	29.95		C
ATOM	1524	O	VAL	A	203	2.962	6.775	5.079	1.00	32.94		O
ATOM	1525	CB	VAL	A	203	0.981	9.163	5.243	1.00	35.04		C
ATOM	1526	CG1	VAL	A	203	−0.314	8.459	4.876	1.00	28.65		C
ATOM	1527	CG2	VAL	A	203	0.710	10.592	5.707	1.00	26.66		C
ATOM	1528	N	ASN	A	204	1.264	6.019	6.345	1.00	29.35		N
ATOM	1529	CA	ASN	A	204	1.449	4.631	5.961	1.00	31.31		C
ATOM	1530	C	ASN	A	204	0.127	4.003	5.525	1.00	33.24		C
ATOM	1531	O	ASN	A	204	−0.888	4.112	6.214	1.00	34.37		O
ATOM	1532	CB	ASN	A	204	2.073	3.843	7.117	1.00	37.45		C
ATOM	1533	CG	ASN	A	204	2.259	2.373	6.789	1.00	54.72		C
ATOM	1534	ND2	ASN	A	204	3.039	2.091	5.754	1.00	50.83		N
ATOM	1535	OD1	ASN	A	204	1.698	1.501	7.455	1.00	73.44		O
ATOM	1536	N	HIS	A	205	0.141	3.373	4.358	1.00	31.18		N
ATOM	1537	CA	HIS	A	205	−1.028	2.675	3.844	1.00	37.56		C
ATOM	1538	C	HIS	A	205	−0.605	1.286	3.413	1.00	34.89		C
ATOM	1539	O	HIS	A	205	−0.256	1.068	2.253	1.00	36.52		O
ATOM	1540	CB	HIS	A	205	−1.658	3.433	2.675	1.00	27.77		C
ATOM	1541	CG	HIS	A	205	−2.917	2.803	2.155	1.00	35.56		C
ATOM	1542	CD2	HIS	A	205	−4.104	2.562	2.753	1.00	33.13		C
ATOM	1543	ND1	HIS	A	205	−3.037	2.344	0.859	1.00	35.44		N
ATOM	1544	CE1	HIS	A	205	−4.248	1.846	0.686	1.00	33.94		C
ATOM	1545	NE2	HIS	A	205	−4.919	1.967	1.815	1.00	29.56		N
ATOM	1546	N	LYS	A	206	−0.623	0.353	4.358	1.00	34.52		N
ATOM	1547	CA	LYS	A	206	−0.155	−1.008	4.104	1.00	41.43		C
ATOM	1548	C	LYS	A	206	−0.833	−1.754	2.942	1.00	35.74		C
ATOM	1549	O	LYS	A	206	−0.155	−2.493	2.231	1.00	39.67		O
ATOM	1550	CB	LYS	A	206	−0.277	−1.846	5.379	1.00	47.00		C
ATOM	1551	CG	LYS	A	206	0.830	−1.575	6.386	1.00	57.13		C
ATOM	1552	CD	LYS	A	206	0.895	−2.659	7.452	1.00	81.12		C
ATOM	1553	CE	LYS	A	206	2.103	−2.473	8.361	1.00	81.79		C
ATOM	1554	NZ	LYS	A	206	2.106	−1.138	9.024	1.00	63.36		N
ATOM	1555	N	PRO	A	207	−2.158	−1.589	2.748	1.00	37.38		N
ATOM	1556	CA	PRO	A	207	−2.759	−2.328	1.624	1.00	32.27		C
ATOM	1557	C	PRO	A	207	−2.137	−2.030	0.252	1.00	38.84		C
ATOM	1558	O	PRO	A	207	−2.064	−2.930	−0.578	1.00	37.23		O
ATOM	1559	CB	PRO	A	207	−4.218	−1.876	1.655	1.00	34.91		C
ATOM	1560	CG	PRO	A	207	−4.471	−1.559	3.085	1.00	40.39		C
ATOM	1561	CD	PRO	A	207	−3.192	−0.955	3.590	1.00	32.89		C
ATOM	1562	N	SER	A	208	−1.696	−0.797	0.020	1.00	38.69		N
ATOM	1563	CA	SER	A	208	−1.064	−0.446	−1.250	1.00	34.52		C
ATOM	1564	C	SER	A	208	0.454	−0.414	−1.115	1.00	40.84		C
ATOM	1565	O	SER	A	208	1.157	−0.044	−2.056	1.00	41.36		O
ATOM	1566	CB	SER	A	208	−1.565	0.911	−1.751	1.00	37.36		C
ATOM	1567	OG	SER	A	208	−1.111	1.961	−0.912	1.00	32.83		O
ATOM	1568	N	ASN	A	209	0.942	−0.792	0.065	1.00	38.90		N
ATOM	1569	CA	ASN	A	209	2.367	−0.729	0.389	1.00	42.99		C
ATOM	1570	C	ASN	A	209	2.941	0.680	0.177	1.00	43.61		C
ATOM	1571	O	ASN	A	209	4.051	0.841	−0.327	1.00	47.92		O
ATOM	1572	CB	ASN	A	209	3.147	−1.756	−0.441	1.00	48.09		C
ATOM	1573	CG	ASN	A	209	4.502	−2.086	0.159	1.00	71.77		C
ATOM	1574	ND2	ASN	A	209	5.502	−2.260	−0.700	1.00	76.92		N
ATOM	1575	OD1	ASN	A	209	4.649	−2.177	1.379	1.00	76.40		O
ATOM	1576	N	THR	A	210	2.174	1.692	0.575	1.00	40.46		N
ATOM	1577	CA	THR	A	210	2.546	3.090	0.371	1.00	38.21		C
ATOM	1578	C	THR	A	210	3.020	3.766	1.656	1.00	38.99		C
ATOM	1579	O	THR	A	210	2.320	3.746	2.670	1.00	38.40		O
ATOM	1580	CB	THR	A	210	1.361	3.901	−0.200	1.00	38.96		C
ATOM	1581	CG2	THR	A	210	1.720	5.376	−0.316	1.00	37.56		C
ATOM	1582	OG1	THR	A	210	1.006	3.395	−1.494	1.00	42.32		O
ATOM	1583	N	LYS	A	211	4.214	4.353	1.607	1.00	32.28		N
ATOM	1584	CA	LYS	A	211	4.716	5.195	2.693	1.00	35.66		C
ATOM	1585	C	LYS	A	211	5.072	6.573	2.155	1.00	33.89		C
ATOM	1586	O	LYS	A	211	5.786	6.698	1.158	1.00	32.27		O
ATOM	1587	CB	LYS	A	211	5.940	4.569	3.370	1.00	36.77		C
ATOM	1588	CG	LYS	A	211	5.624	3.421	4.316	1.00	45.64		C
ATOM	1589	CD	LYS	A	211	6.864	2.974	5.086	1.00	52.89		C
ATOM	1590	CE	LYS	A	211	7.970	2.513	4.143	1.00	58.66		C
ATOM	1591	NZ	LYS	A	211	9.223	2.152	4.870	1.00	61.89		N
ATOM	1592	N	VAL	A	212	4.564	7.608	2.811	1.00	27.70		N
ATOM	1593	CA	VAL	A	212	4.861	8.978	2.416	1.00	34.14		C
ATOM	1594	C	VAL	A	212	5.294	9.800	3.623	1.00	33.04		C
ATOM	1595	O	VAL	A	212	4.657	9.748	4.677	1.00	34.67		O
ATOM	1596	CB	VAL	A	212	3.640	9.659	1.741	1.00	28.22		C
ATOM	1597	CG1	VAL	A	212	3.944	11.111	1.424	1.00	26.60		C
ATOM	1598	CG2	VAL	A	212	3.236	8.911	0.475	1.00	33.62		C
ATOM	1599	N	ASP	A	213	6.387	10.544	3.469	1.00	31.96		N
ATOM	1600	CA	ASP	A	213	6.802	11.535	4.460	1.00	31.89		C
ATOM	1601	C	ASP	A	213	6.622	12.935	3.886	1.00	34.24		C
ATOM	1602	O	ASP	A	213	7.286	13.306	2.918	1.00	32.65		O
ATOM	1603	CB	ASP	A	213	8.258	11.323	4.883	1.00	35.66		C
ATOM	1604	CG	ASP	A	213	8.479	9.985	5.572	1.00	47.44		C
ATOM	1605	OD1	ASP	A	213	7.659	9.616	6.445	1.00	42.96		O
ATOM	1606	OD2	ASP	A	213	9.475	9.302	5.238	1.00	43.88		O
ATOM	1607	N	LYS	A	214	5.728	13.708	4.492	1.00	33.17		N
ATOM	1608	CA	LYS	A	214	5.361	15.016	3.967	1.00	30.01		C
ATOM	1609	C	LYS	A	214	5.791	16.138	4.906	1.00	30.73		C
ATOM	1610	O	LYS	A	214	5.254	16.286	6.004	1.00	29.64		O
ATOM	1611	CB	LYS	A	214	3.849	15.082	3.727	1.00	28.75		C
ATOM	1612	CG	LYS	A	214	3.356	16.407	3.174	1.00	34.59		C
ATOM	1613	CD	LYS	A	214	3.879	16.624	1.767	1.00	33.64		C
ATOM	1614	CE	LYS	A	214	3.468	17.978	1.222	1.00	44.70		C
ATOM	1615	NZ	LYS	A	214	4.102	18.251	−0.100	1.00	46.18		N
ATOM	1616	N	LYS	A	215	6.760	16.932	4.469	1.00	31.30		N
ATOM	1617	CA	LYS	A	215	7.181	18.086	5.247	1.00	29.47		C
ATOM	1618	C	LYS	A	215	6.197	19.230	5.031	1.00	34.25		C
ATOM	1619	O	LYS	A	215	5.887	19.587	3.895	1.00	30.95		O
ATOM	1620	CB	LYS	A	215	8.597	18.521	4.870	1.00	32.87		C
ATOM	1621	CG	LYS	A	215	9.076	19.731	5.657	1.00	32.92		C
ATOM	1622	CD	LYS	A	215	10.523	20.071	5.351	1.00	42.60		C
ATOM	1623	CE	LYS	A	215	10.950	21.339	6.087	1.00	41.79		C
ATOM	1624	NZ	LYS	A	215	12.411	21.587	5.969	1.00	52.69		N
ATOM	1625	N	VAL	A	216	5.697	19.798	6.121	1.00	27.91		N
ATOM	1626	CA	VAL	A	216	4.736	20.883	6.011	1.00	31.50		C
ATOM	1627	C	VAL	A	216	5.346	22.189	6.512	1.00	35.76		C
ATOM	1628	O	VAL	A	216	5.803	22.282	7.654	1.00	31.10		O
ATOM	1629	CB	VAL	A	216	3.443	20.567	6.782	1.00	32.04		C
ATOM	1630	CG1	VAL	A	216	2.447	21.716	6.650	1.00	29.56		C
ATOM	1631	CG2	VAL	A	216	2.833	19.265	6.271	1.00	28.39		C
ATOM	1632	N	GLU	A	217	5.357	23.187	5.634	1.00	39.92		N
ATOM	1633	CA	GLU	A	217	5.937	24.497	5.924	1.00	46.47		C
ATOM	1634	C	GLU	A	217	4.917	25.604	5.714	1.00	44.08		C
ATOM	1635	O	GLU	A	217	3.980	25.443	4.933	1.00	41.16		O
ATOM	1636	CB	GLU	A	217	7.149	24.764	5.026	1.00	44.32		C
ATOM	1637	CG	GLU	A	217	8.396	23.976	5.365	1.00	58.93		C
ATOM	1638	CD	GLU	A	217	9.501	24.188	4.344	1.00	64.35		C
ATOM	1639	OE1	GLU	A	217	10.678	24.300	4.750	1.00	75.54		O
ATOM	1640	OE2	GLU	A	217	9.192	24.239	3.135	1.00	64.80		O
ATOM	1641	N	PRO	A	218	5.099	26.740	6.406	1.00	48.25		N
ATOM	1642	CA	PRO	A	218	4.315	27.925	6.039	1.00	50.69		C
ATOM	1643	C	PRO	A	218	4.667	28.339	4.615	1.00	57.06		C
ATOM	1644	O	PRO	A	218	5.822	28.177	4.218	1.00	55.63		O
ATOM	1645	CB	PRO	A	218	4.757	28.979	7.060	1.00	50.18		C
ATOM	1646	CG	PRO	A	218	6.087	28.500	7.561	1.00	50.76		C
ATOM	1647	CD	PRO	A	218	6.027	27.005	7.521	1.00	42.82		C
ATOM	1648	N	LYS	A	219	3.703	28.834	3.846	1.00	55.24		N
ATOM	1649	CA	LYS	A	219	3.998	29.214	2.468	1.00	72.58		C
ATOM	1650	C	LYS	A	219	4.426	30.679	2.392	1.00	77.04		C
ATOM	1651	O	LYS	A	219	3.946	31.522	3.156	1.00	71.74		O
ATOM	1652	CB	LYS	A	219	2.796	28.952	1.553	1.00	66.67		C
ATOM	1653	CG	LYS	A	219	3.147	29.002	0.068	1.00	73.26		C
ATOM	1654	CD	LYS	A	219	2.190	28.182	−0.790	1.00	78.60		C
ATOM	1655	CE	LYS	A	219	0.862	28.890	−1.001	1.00	76.20		C
ATOM	1656	NZ	LYS	A	219	0.010	28.168	−1.992	1.00	70.66		N
ATOM	1657	N	SER	A	220	5.346	30.969	1.477	1.00	78.80		N
ATOM	1658	CA	SER	A	220	5.870	32.319	1.306	1.00	86.14		C
ATOM	1659	C	SER	A	220	5.245	33.004	0.096	1.00	76.66		C
ATOM	1660	O	SER	A	220	4.778	32.339	−0.829	1.00	76.17		O
ATOM	1661	CB	SER	A	220	7.394	32.284	1.164	1.00	88.61		C
ATOM	1662	OG	SER	A	220	7.787	31.375	0.150	1.00	79.58		O
TER
ATOM	1663	N	ASP	B	1	−30.071	−19.770	21.044	1.00	55.86		N
ATOM	1664	CA	ASP	B	1	−28.959	−18.907	21.429	1.00	51.10		C
ATOM	1665	C	ASP	B	1	−29.427	−17.792	22.359	1.00	49.42		C
ATOM	1666	O	ASP	B	1	−30.475	−17.185	22.139	1.00	43.10		O
ATOM	1667	CB	ASP	B	1	−28.287	−18.316	20.190	1.00	44.13		C
ATOM	1668	CG	ASP	B	1	−27.652	−19.377	19.308	1.00	61.47		C
ATOM	1669	OD2	ASP	B	1	−26.859	−19.009	18.415	1.00	60.15		O
ATOM	1670	OD1	ASP	B	1	−27.951	−20.577	19.503	1.00	63.76		O
ATOM	1671	N	ILE	B	2	−28.649	−17.533	23.404	1.00	43.87		N
ATOM	1672	CA	ILE	B	2	−29.004	−16.506	24.372	1.00	42.91		C
ATOM	1673	C	ILE	B	2	−28.769	−15.115	23.794	1.00	45.05		C
ATOM	1674	O	ILE	B	2	−27.663	−14.787	23.359	1.00	46.40		O
ATOM	1675	CB	ILE	B	2	−28.207	−16.666	25.675	1.00	39.78		C
ATOM	1676	CG1	ILE	B	2	−28.476	−18.041	26.288	1.00	37.36		C
ATOM	1677	CG2	ILE	B	2	−28.563	−15.558	26.659	1.00	35.94		C
ATOM	1678	CD1	ILE	B	2	−27.665	−18.321	27.537	1.00	32.11		C
ATOM	1679	N	VAL	B	3	−29.824	−14.306	23.783	1.00	41.92		N
ATOM	1680	CA	VAL	B	3	−29.759	−12.953	23.249	1.00	38.55		C
ATOM	1681	C	VAL	B	3	−29.539	−11.943	24.372	1.00	39.90		C
ATOM	1682	O	VAL	B	3	−30.258	−11.945	25.372	1.00	40.51		O
ATOM	1683	CB	VAL	B	3	−31.042	−12.599	22.476	1.00	39.53		C
ATOM	1684	CG1	VAL	B	3	−30.987	−11.169	21.965	1.00	34.86		C
ATOM	1685	CG2	VAL	B	3	−31.241	−13.570	21.324	1.00	38.27		C
ATOM	1686	N	MET	B	4	−28.528	−11.094	24.214	1.00	35.54		N
ATOM	1687	CA	MET	B	4	−28.248	−10.063	25.208	1.00	37.31		C
ATOM	1688	C	MET	B	4	−28.677	−8.695	24.687	1.00	34.89		C
ATOM	1689	O	MET	B	4	−28.362	−8.327	23.559	1.00	35.92		O
ATOM	1690	CB	MET	B	4	−26.760	−10.043	25.570	1.00	29.00		C
ATOM	1691	CG	MET	B	4	−26.173	−11.410	25.886	1.00	32.64		C
ATOM	1692	SD	MET	B	4	−26.854	−12.116	27.401	1.00	36.18		S
ATOM	1693	CE	MET	B	4	−26.247	−10.945	28.614	1.00	29.96		C
ATOM	1694	N	THR	B	5	−29.405	−7.953	25.510	1.00	36.75		N
ATOM	1695	CA	THR	B	5	−29.788	−6.591	25.170	1.00	36.17		C
ATOM	1696	C	THR	B	5	−29.273	−5.640	26.238	1.00	38.85		C
ATOM	1697	O	THR	B	5	−29.080	−6.029	27.392	1.00	40.10		O
ATOM	1698	CB	THR	B	5	−31.315	−6.436	25.040	1.00	33.68		C
ATOM	1699	CG2	THR	B	5	−31.853	−7.309	23.910	1.00	30.80		C
ATOM	1700	OG1	THR	B	5	−31.938	−6.816	26.270	1.00	36.62		O
ATOM	1701	N	GLN	B	6	−29.038	−4.394	25.848	1.00	33.36		N
ATOM	1702	CA	GLN	B	6	−28.602	−3.376	26.788	1.00	33.06		C
ATOM	1703	C	GLN	B	6	−29.438	−2.119	26.620	1.00	31.88		C
ATOM	1704	O	GLN	B	6	−30.040	−1.899	25.571	1.00	35.73		O
ATOM	1705	CB	GLN	B	6	−27.116	−3.048	26.599	1.00	33.60		C
ATOM	1706	CG	GLN	B	6	−26.169	−4.214	26.870	1.00	36.92		C
ATOM	1707	CD	GLN	B	6	−24.721	−3.883	26.533	1.00	38.24		C
ATOM	1708	NE2	GLN	B	6	−24.272	−2.702	26.941	1.00	30.52		N
ATOM	1709	OE1	GLN	B	6	−24.017	−4.682	25.915	1.00	36.39		O
ATOM	1710	N	SER	B	7	−29.470	−1.302	27.665	1.00	32.38		N
ATOM	1711	CA	SER	B	7	−30.103	0.006	27.606	1.00	37.23		C
ATOM	1712	C	SER	B	7	−29.416	0.933	28.601	1.00	36.04		C
ATOM	1713	O	SER	B	7	−28.976	0.485	29.662	1.00	39.38		O
ATOM	1714	CB	SER	B	7	−31.602	−0.096	27.901	1.00	37.67		C
ATOM	1715	OG	SER	B	7	−31.826	−0.591	29.208	1.00	50.24		O
ATOM	1716	N	PRO	B	8	−29.296	2.226	28.258	1.00	38.41		N
ATOM	1717	CA	PRO	B	8	−29.712	2.835	26.989	1.00	38.28		C
ATOM	1718	C	PRO	B	8	−28.708	2.568	25.872	1.00	44.42		C
ATOM	1719	O	PRO	B	8	−27.687	1.924	26.117	1.00	41.31		O
ATOM	1720	CB	PRO	B	8	−29.766	4.326	27.325	1.00	41.32		C
ATOM	1721	CG	PRO	B	8	−28.725	4.492	28.383	1.00	37.24		C
ATOM	1722	CD	PRO	B	8	−28.754	3.226	29.197	1.00	31.36		C
ATOM	1723	N	ASP	B	9	−28.994	3.049	24.667	1.00	42.66		N
ATOM	1724	CA	ASP	B	9	−28.037	2.952	23.570	1.00	44.47		C
ATOM	1725	C	ASP	B	9	−26.850	3.863	23.842	1.00	46.92		C
ATOM	1726	O	ASP	B	9	−25.699	3.503	23.588	1.00	38.54		O
ATOM	1727	CB	ASP	B	9	−28.687	3.322	22.236	1.00	44.64		C
ATOM	1728	CG	ASP	B	9	−29.773	2.349	21.827	1.00	70.41		C
ATOM	1729	OD1	ASP	B	9	−29.730	1.181	22.272	1.00	74.55		O
ATOM	1730	OD2	ASP	B	9	−30.671	2.753	21.057	1.00	80.56		O
ATOM	1731	N	SER	B	10	−27.150	5.044	24.371	1.00	42.57		N
ATOM	1732	CA	SER	B	10	−26.146	6.061	24.628	1.00	39.96		C
ATOM	1733	C	SER	B	10	−26.395	6.721	25.978	1.00	42.60		C
ATOM	1734	O	SER	B	10	−27.522	6.742	26.475	1.00	43.39		O
ATOM	1735	CB	SER	B	10	−26.149	7.110	23.515	1.00	29.15		C
ATOM	1736	OG	SER	B	10	−25.012	7.943	23.611	1.00	55.37		O
ATOM	1737	N	LEU	B	11	−25.342	7.286	26.553	1.00	38.86		N
ATOM	1738	CA	LEU	B	11	−25.384	7.756	27.927	1.00	39.26		C
ATOM	1739	C	LEU	B	11	−24.310	8.819	28.132	1.00	33.06		C
ATOM	1740	O	LEU	B	11	−23.172	8.636	27.709	1.00	43.59		O
ATOM	1741	CB	LEU	B	11	−25.186	6.564	28.875	1.00	46.93		C
ATOM	1742	CG	LEU	B	11	−25.354	6.653	30.391	1.00	40.86		C
ATOM	1743	CD1	LEU	B	11	−24.122	7.245	31.054	1.00	49.46		C
ATOM	1744	CD2	LEU	B	11	−26.602	7.452	30.735	1.00	58.72		C
ATOM	1745	N	ALA	B	12	−24.668	9.930	28.768	1.00	34.90		N
ATOM	1746	CA	ALA	B	12	−23.695	10.979	29.078	1.00	32.04		C
ATOM	1747	C	ALA	B	12	−23.942	11.565	30.460	1.00	35.38		C
ATOM	1748	O	ALA	B	12	−25.070	11.894	30.813	1.00	40.40		O
ATOM	1749	CB	ALA	B	12	−23.733	12.076	28.027	1.00	39.73		C
ATOM	1750	N	VAL	B	13	−22.874	11.709	31.235	1.00	38.02		N
ATOM	1751	CA	VAL	B	13	−22.987	12.114	32.629	1.00	32.52		C
ATOM	1752	C	VAL	B	13	−21.794	12.994	33.009	1.00	41.29		C
ATOM	1753	O	VAL	B	13	−20.707	12.841	32.450	1.00	40.66		O
ATOM	1754	CB	VAL	B	13	−23.098	10.856	33.537	1.00	47.79		C
ATOM	1755	CG1	VAL	B	13	−22.187	10.934	34.752	1.00	44.21		C
ATOM	1756	CG2	VAL	B	13	−24.548	10.619	33.939	1.00	43.75		C
ATOM	1757	N	SER	B	14	−21.999	13.933	33.931	1.00	41.23		N
ATOM	1758	CA	SER	B	14	−20.938	14.857	34.333	1.00	36.91		C
ATOM	1759	C	SER	B	14	−19.862	14.158	35.162	1.00	39.93		C
ATOM	1760	O	SER	B	14	−20.125	13.118	35.766	1.00	42.44		O
ATOM	1761	CB	SER	B	14	−21.528	16.030	35.121	1.00	46.50		C
ATOM	1762	OG	SER	B	14	−22.570	16.660	34.393	1.00	52.97		O
ATOM	1763	N	LEU	B	15	−18.656	14.729	35.182	1.00	35.81		N
ATOM	1764	CA	LEU	B	15	−17.549	14.188	35.975	1.00	41.19		C
ATOM	1765	C	LEU	B	15	−17.949	13.897	37.417	1.00	46.73		C
ATOM	1766	O	LEU	B	15	−18.711	14.651	38.022	1.00	44.31		O
ATOM	1767	CB	LEU	B	15	−16.356	15.148	35.990	1.00	42.78		C
ATOM	1768	CG	LEU	B	15	−15.368	15.192	34.825	1.00	60.55		C
ATOM	1769	CD1	LEU	B	15	−15.877	16.103	33.716	1.00	58.51		C
ATOM	1770	CD2	LEU	B	15	−13.996	15.648	35.316	1.00	59.55		C
ATOM	1771	N	GLY	B	16	−17.431	12.800	37.960	1.00	41.51		N
ATOM	1772	CA	GLY	B	16	−17.639	12.466	39.355	1.00	38.32		C
ATOM	1773	C	GLY	B	16	−19.048	12.012	39.675	1.00	37.62		C
ATOM	1774	O	GLY	B	16	−19.362	11.730	40.829	1.00	45.46		O
ATOM	1775	N	GLU	B	17	−19.902	11.938	38.661	1.00	40.92		N
ATOM	1776	CA	GLU	B	17	−21.273	11.496	38.876	1.00	41.65		C
ATOM	1777	C	GLU	B	17	−21.458	10.032	38.491	1.00	45.71		C
ATOM	1778	O	GLU	B	17	−20.568	9.404	37.912	1.00	38.54		O
ATOM	1779	CB	GLU	B	17	−22.256	12.378	38.104	1.00	42.09		C
ATOM	1780	CG	GLU	B	17	−22.365	13.791	38.659	1.00	48.23		C
ATOM	1781	CD	GLU	B	17	−23.478	14.596	38.011	1.00	66.55		C
ATOM	1782	OE1	GLU	B	17	−23.909	14.234	36.894	1.00	71.11		O
ATOM	1783	OE2	GLU	B	17	−23.923	15.591	38.624	1.00	74.03		O
ATOM	1784	N	ARG	B	18	−22.627	9.500	38.823	1.00	45.65		N
ATOM	1785	CA	ARG	B	18	−22.899	8.077	38.701	1.00	45.58		C
ATOM	1786	C	ARG	B	18	−23.508	7.729	37.346	1.00	40.92		C
ATOM	1787	O	ARG	B	18	−24.379	8.436	36.843	1.00	38.35		O
ATOM	1788	CB	ARG	B	18	−23.826	7.638	39.838	1.00	43.55		C
ATOM	1789	CG	ARG	B	18	−24.162	6.165	39.879	1.00	54.20		C
ATOM	1790	CD	ARG	B	18	−24.969	5.853	41.132	1.00	66.41		C
ATOM	1791	NE	ARG	B	18	−25.394	4.459	41.181	1.00	84.38		N
ATOM	1792	CZ	ARG	B	18	−26.076	3.921	42.186	1.00	83.62		C
ATOM	1793	NH1	ARG	B	18	−26.412	4.662	43.234	1.00	81.35		N
ATOM	1794	NH2	ARG	B	18	−26.420	2.640	42.142	1.00	85.37		N
ATOM	1795	N	ALA	B	19	−23.030	6.643	36.751	1.00	35.20		N
ATOM	1796	CA	ALA	B	19	−23.584	6.161	35.491	1.00	34.46		C
ATOM	1797	C	ALA	B	19	−23.980	4.696	35.617	1.00	39.57		C
ATOM	1798	O	ALA	B	19	−23.276	3.904	36.247	1.00	38.45		O
ATOM	1799	CB	ALA	B	19	−22.588	6.351	34.356	1.00	36.85		C
ATOM	1800	N	THR	B	20	−25.105	4.344	35.004	1.00	33.06		N
ATOM	1801	CA	THR	B	20	−25.654	3.001	35.107	1.00	35.98		C
ATOM	1802	C	THR	B	20	−26.066	2.452	33.742	1.00	38.75		C
ATOM	1803	O	THR	B	20	−26.762	3.118	32.979	1.00	37.55		O
ATOM	1804	CB	THR	B	20	−26.866	2.987	36.062	1.00	38.02		C
ATOM	1805	CG2	THR	B	20	−27.718	1.757	35.842	1.00	44.22		C
ATOM	1806	OG1	THR	B	20	−26.398	3.008	37.419	1.00	45.86		O
ATOM	1807	N	ILE	B	21	−25.622	1.235	33.441	1.00	37.58		N
ATOM	1808	CA	ILE	B	21	−25.973	0.559	32.196	1.00	35.14		C
ATOM	1809	C	ILE	B	21	−26.661	−0.765	32.507	1.00	37.66		C
ATOM	1810	O	ILE	B	21	−26.193	−1.527	33.350	1.00	32.81		O
ATOM	1811	CB	ILE	B	21	−24.733	0.284	31.326	1.00	38.29		C
ATOM	1812	CG1	ILE	B	21	−23.964	1.573	31.057	1.00	37.46		C
ATOM	1813	CG2	ILE	B	21	−25.127	−0.395	30.018	1.00	45.60		C
ATOM	1814	CD1	ILE	B	21	−22.717	1.348	30.238	1.00	41.15		C
ATOM	1815	N	ASN	B	22	−27.761	−1.046	31.819	1.00	30.24		N
ATOM	1816	CA	ASN	B	22	−28.521	−2.260	32.084	1.00	37.10		C
ATOM	1817	C	ASN	B	22	−28.270	−3.358	31.050	1.00	40.28		C
ATOM	1818	O	ASN	B	22	−28.041	−3.081	29.870	1.00	35.19		O
ATOM	1819	CB	ASN	B	22	−30.013	−1.932	32.157	1.00	36.20		C
ATOM	1820	CG	ASN	B	22	−30.308	−0.788	33.121	1.00	60.60		C
ATOM	1821	OD1	ASN	B	22	−30.309	−0.974	34.341	1.00	57.11		O
ATOM	1822	ND2	ASN	B	22	−30.547	0.407	32.576	1.00	55.17		N
ATOM	1823	N	CYS	B	23	−28.315	−4.604	31.509	1.00	36.70		N
ATOM	1824	CA	CYS	B	23	−28.121	−5.762	30.647	1.00	34.30		C
ATOM	1825	C	CYS	B	23	−29.231	−6.791	30.872	1.00	38.13		C
ATOM	1826	O	CYS	B	23	−29.570	−7.107	32.012	1.00	40.38		O
ATOM	1827	CB	CYS	B	23	−26.748	−6.391	30.913	1.00	37.80		C
ATOM	1828	SG	CYS	B	23	−26.222	−7.657	29.735	1.00	53.67		S
ATOM	1829	N	LYS	B	24	−29.794	−7.312	29.786	1.00	33.98		N
ATOM	1830	CA	LYS	B	24	−30.813	−8.356	29.871	1.00	36.97		C
ATOM	1831	C	LYS	B	24	−30.440	−9.564	29.024	1.00	42.52		C
ATOM	1832	O	LYS	B	24	−29.979	−9.419	27.890	1.00	38.82		O
ATOM	1833	CB	LYS	B	24	−32.181	−7.831	29.425	1.00	43.72		C
ATOM	1834	CG	LYS	B	24	−33.084	−7.356	30.550	1.00	55.35		C
ATOM	1835	CD	LYS	B	24	−34.508	−7.143	30.045	1.00	61.25		C
ATOM	1836	CE	LYS	B	24	−35.433	−6.673	31.155	1.00	65.56		C
ATOM	1837	NZ	LYS	B	24	−35.055	−5.323	31.656	1.00	61.27		N
ATOM	1838	N	SER	B	25	−30.644	−10.755	29.580	1.00	37.96		N
ATOM	1839	CA	SER	B	25	−30.438	−11.991	28.835	1.00	41.49		C
ATOM	1840	C	SER	B	25	−31.782	−12.646	28.540	1.00	40.87		C
ATOM	1841	O	SER	B	25	−32.677	−12.640	29.379	1.00	42.24		O
ATOM	1842	CB	SER	B	25	−29.524	−12.949	29.603	1.00	33.20		C
ATOM	1843	OG	SER	B	25	−29.974	−13.149	30.931	1.00	36.26		O
ATOM	1844	N	SER	B	26	−31.915	−13.209	27.342	1.00	38.29		N
ATOM	1845	CA	SER	B	26	−33.176	−13.790	26.895	1.00	38.35		C
ATOM	1846	C	SER	B	26	−33.605	−14.975	27.759	1.00	43.66		C
ATOM	1847	O	SER	B	26	−34.760	−15.394	27.720	1.00	40.54		O
ATOM	1848	CB	SER	B	26	−33.067	−14.224	25.434	1.00	35.59		C
ATOM	1849	OG	SER	B	26	−32.037	−15.182	25.272	1.00	38.41		O
ATOM	1850	N	GLN	B	27	−32.666	−15.519	28.527	1.00	42.85		N
ATOM	1851	CA	GLN	B	27	−32.979	−16.560	29.498	1.00	39.30		C
ATOM	1852	C	GLN	B	27	−32.004	−16.465	30.660	1.00	43.02		C
ATOM	1853	O	GLN	B	27	−31.011	−15.745	30.581	1.00	38.87		O
ATOM	1854	CB	GLN	B	27	−32.926	−17.946	28.858	1.00	40.88		C
ATOM	1855	CG	GLN	B	27	−31.538	−18.387	28.447	1.00	44.20		C
ATOM	1856	CD	GLN	B	27	−31.549	−19.707	27.705	1.00	51.33		C
ATOM	1857	NE2	GLN	B	27	−31.158	−20.776	28.393	1.00	42.28		N
ATOM	1858	OE1	GLN	B	27	−31.906	−19.769	26.525	1.00	47.83		O
ATOM	1859	N	SER	B	28	−32.291	−17.187	31.738	1.00	40.20		N
ATOM	1860	CA	SER	B	28	−31.473	−17.109	32.941	1.00	36.91		C
ATOM	1861	C	SER	B	28	−30.065	−17.631	32.699	1.00	41.10		C
ATOM	1862	O	SER	B	28	−29.871	−18.659	32.048	1.00	36.62		O
ATOM	1863	CB	SER	B	28	−32.120	−17.889	34.087	1.00	41.70		C
ATOM	1864	OG	SER	B	28	−31.399	−17.700	35.294	1.00	42.03		O
ATOM	1865	N	ILE	B	29	−29.084	−16.906	33.227	1.00	36.07		N
ATOM	1866	CA	ILE	B	29	−27.692	−17.320	33.149	1.00	34.98		C
ATOM	1867	C	ILE	B	29	−27.143	−17.474	34.564	1.00	36.30		C
ATOM	1868	O	ILE	B	29	−25.934	−17.400	34.795	1.00	34.45		O
ATOM	1869	CB	ILE	B	29	−26.846	−16.316	32.344	1.00	31.71		C
ATOM	1870	CG1	ILE	B	29	−26.947	−14.916	32.949	1.00	29.95		C
ATOM	1871	CG2	ILE	B	29	−27.310	−16.276	30.898	1.00	29.61		C
ATOM	1872	CD1	ILE	B	29	−26.198	−13.855	32.145	1.00	31.42		C
ATOM	1873	O	LEU	B	30	−28.655	−20.230	36.655	1.00	44.52		O
ATOM	1874	N	LEU	B	30	−28.058	−17.672	35.508	1.00	33.91		N
ATOM	1875	CA	LEU	B	30	−27.709	−18.044	36.873	1.00	39.31		C
ATOM	1876	C	LEU	B	30	−27.673	−19.563	36.977	1.00	38.06		C
ATOM	1877	CB	LEU	B	30	−28.716	−17.465	37.872	1.00	37.18		C
ATOM	1878	CG	LEU	B	30	−28.589	−17.932	39.327	1.00	39.11		C
ATOM	1879	CD2	LEU	B	30	−29.827	−17.558	40.128	1.00	36.35		C
ATOM	1880	CD1	LEU	B	30	−27.331	−17.378	39.987	1.00	36.12		C
ATOM	1881	O	HIS	B	31	−26.681	−21.536	39.965	1.00	38.61		O
ATOM	1882	N	HIS	B	31	−26.546	−20.117	37.411	1.00	33.48		N
ATOM	1883	CA	HIS	B	31	−26.464	−21.562	37.580	1.00	38.93		C
ATOM	1884	C	HIS	B	31	−27.113	−21.968	38.897	1.00	39.33		C
ATOM	1885	CB	HIS	B	31	−25.018	−22.046	37.533	1.00	38.09		C
ATOM	1886	CG	HIS	B	31	−24.889	−23.538	37.446	1.00	39.11		C
ATOM	1887	ND1	HIS	B	31	−24.604	−24.190	36.272	1.00	42.93		N
ATOM	1888	CD2	HIS	B	31	−25.028	−24.496	38.394	1.00	37.40		C
ATOM	1889	CE1	HIS	B	31	−24.560	−25.497	36.497	1.00	40.76		C
ATOM	1890	NE2	HIS	B	31	−24.816	−25.705	37.772	1.00	41.52		N
ATOM	1891	O	SER	B	32	−28.568	−23.745	42.260	1.00	57.25		O
ATOM	1892	N	SER	B	32	−28.140	−22.809	38.812	1.00	43.81		N
ATOM	1893	CA	SER	B	32	−28.969	−23.149	39.972	1.00	49.61		C
ATOM	1894	C	SER	B	32	−28.209	−23.866	41.089	1.00	43.17		C
ATOM	1895	CB	SER	B	32	−30.159	−24.004	39.530	1.00	47.25		C
ATOM	1896	OG	SER	B	32	−29.731	−25.115	38.758	1.00	56.93		O
ATOM	1897	O	SER	B	33	−25.191	−24.612	43.655	1.00	47.19		O
ATOM	1898	N	SER	B	33	−27.155	−24.596	40.737	1.00	40.34		N
ATOM	1899	CA	SER	B	33	−26.407	−25.373	41.729	1.00	50.61		C
ATOM	1900	C	SER	B	33	−25.300	−24.578	42.428	1.00	46.45		C
ATOM	1901	CB	SER	B	33	−25.807	−26.621	41.079	1.00	46.34		C
ATOM	1902	OG	SER	B	33	−26.825	−27.469	40.581	1.00	54.71		O
ATOM	1903	O	ASN	B	34	−22.973	−20.977	43.235	1.00	37.27		O
ATOM	1904	N	ASN	B	34	−24.470	−23.875	41.661	1.00	42.95		N
ATOM	1905	CA	ASN	B	34	−23.365	−23.137	42.269	1.00	42.26		C
ATOM	1906	C	ASN	B	34	−23.735	−21.686	42.578	1.00	34.30		C
ATOM	1907	CB	ASN	B	34	−22.112	−23.195	41.378	1.00	39.81		C
ATOM	1908	CG	ASN	B	34	−22.306	−22.519	40.027	1.00	38.01		C
ATOM	1909	OD1	ASN	B	34	−22.552	−21.313	39.949	1.00	35.29		O
ATOM	1910	ND2	ASN	B	34	−22.163	−23.292	38.952	1.00	32.57		N
ATOM	1911	O	ASN	B	35	−24.573	−17.694	42.495	1.00	38.12		O
ATOM	1912	N	ASN	B	35	−24.900	−21.256	42.095	1.00	36.64		N
ATOM	1913	CA	ASN	B	35	−25.455	−19.936	42.414	1.00	41.38		C
ATOM	1914	C	ASN	B	35	−24.612	−18.762	41.888	1.00	38.67		C
ATOM	1915	CB	ASN	B	35	−25.650	−19.805	43.936	1.00	38.07		C
ATOM	1916	CG	ASN	B	35	−26.644	−18.719	44.315	1.00	52.73		C
ATOM	1917	OD1	ASN	B	35	−27.611	−18.462	43.594	1.00	51.71		O
ATOM	1918	ND2	ASN	B	35	−26.403	−18.069	45.452	1.00	46.79		N
ATOM	1919	O	ASN	B	36	−24.385	−18.267	38.068	1.00	37.24		O
ATOM	1920	N	ASN	B	36	−23.947	−18.955	40.752	1.00	32.67		N
ATOM	1921	CA	ASN	B	36	−23.207	−17.863	40.120	1.00	35.30		C
ATOM	1922	C	ASN	B	36	−23.838	−17.439	38.801	1.00	30.07		C
ATOM	1923	CB	ASN	B	36	−21.743	−18.252	39.888	1.00	30.99		C
ATOM	1924	CG	ASN	B	36	−20.922	−18.234	41.165	1.00	39.65		C
ATOM	1925	OD1	ASN	B	36	−20.340	−17.210	41.526	1.00	36.59		O
ATOM	1926	ND2	ASN	B	36	−20.870	−19.369	41.854	1.00	34.78		N
ATOM	1927	O	ASN	B	37	−22.048	−14.928	36.474	1.00	26.67		O
ATOM	1928	N	ASN	B	37	−23.761	−16.144	38.510	1.00	28.56		N
ATOM	1929	CA	ASN	B	37	−24.222	−15.603	37.237	1.00	32.35		C
ATOM	1930	C	ASN	B	37	−23.090	−15.540	36.217	1.00	35.69		C
ATOM	1931	CB	ASN	B	37	−24.817	−14.214	37.437	1.00	33.21		C
ATOM	1932	CG	ASN	B	37	−25.996	−14.219	38.386	1.00	35.83		C
ATOM	1933	OD1	ASN	B	37	−25.854	−13.922	39.573	1.00	39.01		O
ATOM	1934	ND2	ASN	B	37	−27.166	−14.566	37.868	1.00	28.90		N
ATOM	1935	N	TYR	B	38	−23.306	−16.156	35.059	1.00	26.80		N
ATOM	1936	CA	TYR	B	38	−22.251	−16.313	34.063	1.00	31.80		C
ATOM	1937	C	TYR	B	38	−22.234	−15.119	33.118	1.00	29.97		C
ATOM	1938	O	TYR	B	38	−22.505	−15.241	31.924	1.00	29.53		O
ATOM	1939	CB	TYR	B	38	−22.431	−17.628	33.295	1.00	28.25		C
ATOM	1940	CG	TYR	B	38	−22.072	−18.859	34.115	1.00	31.67		C
ATOM	1941	CD2	TYR	B	38	−21.149	−19.792	33.649	1.00	32.47		C
ATOM	1942	CD1	TYR	B	38	−22.656	−19.083	35.358	1.00	26.38		C
ATOM	1943	CE2	TYR	B	38	−20.816	−20.912	34.406	1.00	31.96		C
ATOM	1944	CE1	TYR	B	38	−22.327	−20.190	36.118	1.00	30.74		C
ATOM	1945	CZ	TYR	B	38	−21.414	−21.102	35.639	1.00	32.95		C
ATOM	1946	OH	TYR	B	38	−21.096	−22.200	36.403	1.00	33.05		O
ATOM	1947	N	LEU	B	39	−21.905	−13.963	33.680	1.00	29.02		N
ATOM	1948	CA	LEU	B	39	−21.932	−12.703	32.957	1.00	26.70		C
ATOM	1949	C	LEU	B	39	−20.623	−11.945	33.112	1.00	25.80		C
ATOM	1950	O	LEU	B	39	−20.043	−11.912	34.202	1.00	29.17		O
ATOM	1951	CB	LEU	B	39	−23.082	−11.829	33.457	1.00	30.90		C
ATOM	1952	CG	LEU	B	39	−23.219	−10.510	32.698	1.00	33.97		C
ATOM	1953	CD1	LEU	B	39	−24.064	−10.714	31.458	1.00	27.79		C
ATOM	1954	CD2	LEU	B	39	−23.785	−9.419	33.577	1.00	33.15		C
ATOM	1955	N	ALA	B	40	−20.168	−11.330	32.025	1.00	28.13		N
ATOM	1956	CA	ALA	B	40	−18.989	−10.470	32.068	1.00	25.92		C
ATOM	1957	C	ALA	B	40	−19.287	−9.078	31.501	1.00	26.60		C
ATOM	1958	O	ALA	B	40	−20.162	−8.917	30.648	1.00	25.73		O
ATOM	1959	CB	ALA	B	40	−17.836	−11.111	31.309	1.00	26.93		C
ATOM	1960	N	TRP	B	41	−18.556	−8.079	31.986	1.00	26.55		N
ATOM	1961	CA	TRP	B	41	−18.651	−6.720	31.455	1.00	30.35		C
ATOM	1962	C	TRP	B	41	−17.325	−6.293	30.832	1.00	29.83		C
ATOM	1963	O	TRP	B	41	−16.261	−6.507	31.415	1.00	26.54		O
ATOM	1964	CB	TRP	B	41	−19.042	−5.723	32.549	1.00	25.43		C
ATOM	1965	CG	TRP	B	41	−20.484	−5.762	32.956	1.00	30.44		C
ATOM	1966	CD1	TRP	B	41	−21.014	−6.405	34.039	1.00	30.19		C
ATOM	1967	CD2	TRP	B	41	−21.581	−5.116	32.297	1.00	28.45		C
ATOM	1968	CE2	TRP	B	41	−22.747	−5.418	33.032	1.00	31.50		C
ATOM	1969	CE3	TRP	B	41	−21.692	−4.318	31.154	1.00	33.61		C
ATOM	1970	NE1	TRP	B	41	−22.372	−6.204	34.090	1.00	28.08		N
ATOM	1971	CZ2	TRP	B	41	−24.008	−4.946	32.664	1.00	32.35		C
ATOM	1972	CZ3	TRP	B	41	−22.947	−3.846	30.787	1.00	31.41		C
ATOM	1973	CH2	TRP	B	41	−24.087	−4.163	31.541	1.00	36.76		C
ATOM	1974	N	PHE	B	42	−17.400	−5.679	29.655	1.00	25.32		N
ATOM	1975	CA	PHE	B	42	−16.220	−5.212	28.939	1.00	27.15		C
ATOM	1976	C	PHE	B	42	−16.271	−3.715	28.680	1.00	31.54		C
ATOM	1977	O	PHE	B	42	−17.338	−3.154	28.431	1.00	31.28		O
ATOM	1978	CB	PHE	B	42	−16.073	−5.944	27.601	1.00	23.42		C
ATOM	1979	CG	PHE	B	42	−15.772	−7.405	27.739	1.00	26.14		C
ATOM	1980	CD1	PHE	B	42	−14.462	−7.847	27.845	1.00	24.13		C
ATOM	1981	CD2	PHE	B	42	−16.794	−8.337	27.758	1.00	29.43		C
ATOM	1982	CE1	PHE	B	42	−14.181	−9.195	27.976	1.00	28.57		C
ATOM	1983	CE2	PHE	B	42	−16.518	−9.690	27.887	1.00	26.26		C
ATOM	1984	CZ	PHE	B	42	−15.212	−10.116	27.997	1.00	25.92		C
ATOM	1985	N	GLN	B	43	−15.109	−3.076	28.723	1.00	27.61		N
ATOM	1986	CA	GLN	B	43	−14.976	−1.691	28.289	1.00	26.82		C
ATOM	1987	C	GLN	B	43	−14.148	−1.643	27.004	1.00	32.12		C
ATOM	1988	O	GLN	B	43	−13.062	−2.221	26.945	1.00	29.12		O
ATOM	1989	CB	GLN	B	43	−14.317	−0.842	29.375	1.00	23.34		C
ATOM	1990	CG	GLN	B	43	−14.190	0.629	29.022	1.00	24.31		C
ATOM	1991	CD	GLN	B	43	−13.172	1.345	29.891	1.00	29.32		C
ATOM	1992	NE2	GLN	B	43	−13.650	2.131	30.851	1.00	31.37		N
ATOM	1993	OE1	GLN	B	43	−11.970	1.192	29.701	1.00	31.73		O
ATOM	1994	N	GLN	B	44	−14.656	−0.977	25.972	1.00	20.12		N
ATOM	1995	CA	GLN	B	44	−13.869	−0.810	24.754	1.00	26.13		C
ATOM	1996	C	GLN	B	44	−13.601	0.662	24.464	1.00	26.14		C
ATOM	1997	O	GLN	B	44	−14.477	1.377	23.977	1.00	29.23		O
ATOM	1998	CB	GLN	B	44	−14.559	−1.470	23.556	1.00	24.46		C
ATOM	1999	CG	GLN	B	44	−13.755	−1.359	22.263	1.00	26.38		C
ATOM	2000	CD	GLN	B	44	−14.303	−2.228	21.137	1.00	28.28		C
ATOM	2001	NE2	GLN	B	44	−13.407	−2.827	20.355	1.00	28.01		N
ATOM	2002	OE1	GLN	B	44	−15.512	−2.363	20.977	1.00	28.62		O
ATOM	2003	N	LYS	B	45	−12.388	1.103	24.786	1.00	27.16		N
ATOM	2004	CA	LYS	B	45	−11.913	2.448	24.466	1.00	35.42		C
ATOM	2005	C	LYS	B	45	−11.696	2.581	22.963	1.00	35.66		C
ATOM	2006	O	LYS	B	45	−11.493	1.577	22.281	1.00	35.60		O
ATOM	2007	CB	LYS	B	45	−10.602	2.752	25.205	1.00	33.99		C
ATOM	2008	CG	LYS	B	45	−10.694	2.701	26.707	1.00	42.68		C
ATOM	2009	CD	LYS	B	45	−9.353	3.040	27.351	1.00	41.29		C
ATOM	2010	CE	LYS	B	45	−8.230	2.156	26.828	1.00	41.00		C
ATOM	2011	NZ	LYS	B	45	−7.078	2.115	27.785	1.00	34.96		N
ATOM	2012	N	PRO	B	46	−11.726	3.820	22.440	1.00	38.26		N
ATOM	2013	CA	PRO	B	46	−11.508	4.031	21.001	1.00	37.25		C
ATOM	2014	C	PRO	B	46	−10.173	3.470	20.504	1.00	36.36		C
ATOM	2015	O	PRO	B	46	−9.125	3.762	21.087	1.00	35.60		O
ATOM	2016	CB	PRO	B	46	−11.537	5.559	20.865	1.00	41.28		C
ATOM	2017	CG	PRO	B	46	−12.362	6.021	22.009	1.00	39.45		C
ATOM	2018	CD	PRO	B	46	−12.046	5.080	23.138	1.00	35.28		C
ATOM	2019	N	GLY	B	47	−10.225	2.664	19.447	1.00	34.42		N
ATOM	2020	CA	GLY	B	47	−9.034	2.100	18.835	1.00	31.31		C
ATOM	2021	C	GLY	B	47	−8.501	0.849	19.517	1.00	42.85		C
ATOM	2022	O	GLY	B	47	−7.507	0.270	19.074	1.00	30.21		O
ATOM	2023	N	GLN	B	48	−9.163	0.425	20.589	1.00	29.62		N
ATOM	2024	CA	GLN	B	48	−8.662	−0.672	21.411	1.00	33.47		C
ATOM	2025	C	GLN	B	48	−9.588	−1.887	21.411	1.00	33.23		C
ATOM	2026	O	GLN	B	48	−10.787	−1.757	21.171	1.00	26.94		O
ATOM	2027	CB	GLN	B	48	−8.451	−0.187	22.850	1.00	32.23		C
ATOM	2028	CG	GLN	B	48	−7.391	0.893	22.990	1.00	33.96		C
ATOM	2029	CD	GLN	B	48	−6.011	0.404	22.590	1.00	43.63		C
ATOM	2030	OE1	GLN	B	48	−5.276	1.095	21.885	1.00	42.98		O
ATOM	2031	NE2	GLN	B	48	−5.652	−0.796	23.042	1.00	39.16		N
ATOM	2032	N	PRO	B	49	−9.032	−3.077	21.691	1.00	30.89		N
ATOM	2033	CA	PRO	B	49	−9.885	−4.246	21.918	1.00	26.27		C
ATOM	2034	C	PRO	B	49	−10.687	−4.069	23.203	1.00	27.88		C
ATOM	2035	O	PRO	B	49	−10.290	−3.264	24.045	1.00	27.50		O
ATOM	2036	CB	PRO	B	49	−8.883	−5.396	22.049	1.00	26.15		C
ATOM	2037	CG	PRO	B	49	−7.629	−4.740	22.538	1.00	28.99		C
ATOM	2038	CD	PRO	B	49	−7.602	−3.394	21.865	1.00	32.59		C
ATOM	2039	N	PRO	B	50	−11.803	−4.799	23.351	1.00	25.78		N
ATOM	2040	CA	PRO	B	50	−12.539	−4.746	24.621	1.00	23.59		C
ATOM	2041	C	PRO	B	50	−11.625	−5.113	25.793	1.00	30.73		C
ATOM	2042	O	PRO	B	50	−10.661	−5.859	25.608	1.00	26.96		O
ATOM	2043	CB	PRO	B	50	−13.643	−5.791	24.438	1.00	24.85		C
ATOM	2044	CG	PRO	B	50	−13.817	−5.908	22.949	1.00	25.66		C
ATOM	2045	CD	PRO	B	50	−12.441	−5.694	22.370	1.00	25.19		C
ATOM	2046	N	LYS	B	51	−11.909	−4.574	26.972	1.00	27.75		N
ATOM	2047	CA	LYS	B	51	−11.131	−4.899	28.158	1.00	25.94		C
ATOM	2048	C	LYS	B	51	−12.052	−5.420	29.251	1.00	30.23		C
ATOM	2049	O	LYS	B	51	−13.083	−4.818	29.547	1.00	25.89		O
ATOM	2050	CB	LYS	B	51	−10.351	−3.680	28.654	1.00	29.25		C
ATOM	2051	CG	LYS	B	51	−9.163	−4.045	29.535	1.00	32.02		C
ATOM	2052	CD	LYS	B	51	−9.469	−3.859	31.001	1.00	37.80		C
ATOM	2053	CE	LYS	B	51	−8.409	−4.533	31.869	1.00	37.22		C
ATOM	2054	NZ	LYS	B	51	−8.655	−5.999	32.014	1.00	34.08		N
ATOM	2055	N	LEU	B	52	−11.680	−6.547	29.845	1.00	24.57		N
ATOM	2056	CA	LEU	B	52	−12.514	−7.177	30.860	1.00	28.11		C
ATOM	2057	C	LEU	B	52	−12.555	−6.335	32.130	1.00	24.97		C
ATOM	2058	O	LEU	B	52	−11.514	−5.962	32.663	1.00	30.29		O
ATOM	2059	CB	LEU	B	52	−11.998	−8.583	31.172	1.00	26.30		C
ATOM	2060	CG	LEU	B	52	−12.775	−9.420	32.190	1.00	32.39		C
ATOM	2061	CD1	LEU	B	52	−14.222	−9.597	31.751	1.00	25.02		C
ATOM	2062	CD2	LEU	B	52	−12.099	−10.772	32.378	1.00	30.83		C
ATOM	2063	N	LEU	B	53	−13.760	−6.030	32.600	1.00	27.61		N
ATOM	2064	CA	LEU	B	53	−13.938	−5.297	33.854	1.00	30.52		C
ATOM	2065	C	LEU	B	53	−14.434	−6.219	34.956	1.00	31.29		C
ATOM	2066	O	LEU	B	53	−13.913	−6.226	36.068	1.00	30.02		O
ATOM	2067	CB	LEU	B	53	−14.936	−4.153	33.688	1.00	25.25		C
ATOM	2068	CG	LEU	B	53	−14.711	−3.080	32.627	1.00	33.70		C
ATOM	2069	CD1	LEU	B	53	−15.917	−2.149	32.611	1.00	26.80		C
ATOM	2070	CD2	LEU	B	53	−13.432	−2.308	32.907	1.00	32.50		C
ATOM	2071	N	LEU	B	54	−15.460	−6.993	34.631	1.00	28.48		N
ATOM	2072	CA	LEU	B	54	−16.169	−7.782	35.623	1.00	30.79		C
ATOM	2073	C	LEU	B	54	−16.516	−9.152	35.071	1.00	28.54		C
ATOM	2074	O	LEU	B	54	−16.791	−9.294	33.883	1.00	26.65		O
ATOM	2075	CB	LEU	B	54	−17.448	−7.055	36.059	1.00	31.42		C
ATOM	2076	CG	LEU	B	54	−17.289	−5.722	36.798	1.00	33.30		C
ATOM	2077	CD1	LEU	B	54	−18.529	−4.870	36.615	1.00	32.48		C
ATOM	2078	CD2	LEU	B	54	−17.052	−5.971	38.268	1.00	34.07		C
ATOM	2079	N	TYR	B	55	−16.502	−10.158	35.938	1.00	29.20		N
ATOM	2080	CA	TYR	B	55	−17.005	−11.475	35.580	1.00	29.74		C
ATOM	2081	C	TYR	B	55	−17.755	−12.043	36.791	1.00	32.63		C
ATOM	2082	O	TYR	B	55	−17.726	−11.449	37.872	1.00	31.32		O
ATOM	2083	CB	TYR	B	55	−15.869	−12.393	35.101	1.00	28.86		C
ATOM	2084	CG	TYR	B	55	−14.714	−12.558	36.065	1.00	30.07		C
ATOM	2085	CD1	TYR	B	55	−13.746	−11.572	36.204	1.00	31.15		C
ATOM	2086	CD2	TYR	B	55	−14.578	−13.717	36.814	1.00	30.26		C
ATOM	2087	CE1	TYR	B	55	−12.686	−11.728	37.088	1.00	34.78		C
ATOM	2088	CE2	TYR	B	55	−13.525	−13.886	37.695	1.00	33.93		C
ATOM	2089	CZ	TYR	B	55	−12.582	−12.889	37.828	1.00	36.44		C
ATOM	2090	OH	TYR	B	55	−11.534	−13.059	38.705	1.00	37.42		O
ATOM	2091	N	TRP	B	56	−18.448	−13.165	36.599	1.00	28.09		N
ATOM	2092	CA	TRP	B	56	−19.439	−13.657	37.566	1.00	26.67		C
ATOM	2093	C	TRP	B	56	−20.387	−12.528	37.984	1.00	27.89		C
ATOM	2094	O	TRP	B	56	−20.767	−12.420	39.151	1.00	24.63		O
ATOM	2095	CB	TRP	B	56	−18.769	−14.276	38.799	1.00	22.01		C
ATOM	2096	CG	TRP	B	56	−17.799	−15.367	38.462	1.00	27.09		C
ATOM	2097	CD1	TRP	B	56	−16.475	−15.402	38.777	1.00	26.84		C
ATOM	2098	CD2	TRP	B	56	−18.068	−16.569	37.720	1.00	23.97		C
ATOM	2099	NE1	TRP	B	56	−15.901	−16.551	38.286	1.00	28.86		N
ATOM	2100	CE2	TRP	B	56	−16.857	−17.284	37.633	1.00	25.06		C
ATOM	2101	CE3	TRP	B	56	−19.214	−17.112	37.131	1.00	23.47		C
ATOM	2102	CZ2	TRP	B	56	−16.758	−18.514	36.983	1.00	28.72		C
ATOM	2103	CZ3	TRP	B	56	−19.117	−18.334	36.486	1.00	28.66		C
ATOM	2104	CH2	TRP	B	56	−17.896	−19.021	36.414	1.00	29.03		C
ATOM	2105	N	ALA	B	57	−20.734	−11.686	37.009	1.00	26.41		N
ATOM	2106	CA	ALA	B	57	−21.626	−10.531	37.167	1.00	29.78		C
ATOM	2107	C	ALA	B	57	−21.083	−9.421	38.079	1.00	31.22		C
ATOM	2108	O	ALA	B	57	−21.331	−8.242	37.817	1.00	35.13		O
ATOM	2109	CB	ALA	B	57	−23.008	−10.985	37.667	1.00	27.19		C
ATOM	2110	N	SER	B	58	−20.344	−9.767	39.132	1.00	32.27		N
ATOM	2111	CA	SER	B	58	−19.992	−8.748	40.125	1.00	31.56		C
ATOM	2112	C	SER	B	58	−18.563	−8.741	40.672	1.00	32.07		C
ATOM	2113	O	SER	B	58	−18.251	−7.901	41.517	1.00	37.30		O
ATOM	2114	CB	SER	B	58	−20.955	−8.849	41.315	1.00	36.25		C
ATOM	2115	OG	SER	B	58	−20.817	−10.091	41.985	1.00	37.37		O
ATOM	2116	N	THR	B	59	−17.687	−9.640	40.229	1.00	31.17		N
ATOM	2117	CA	THR	B	59	−16.319	−9.596	40.759	1.00	29.77		C
ATOM	2118	C	THR	B	59	−15.365	−8.910	39.770	1.00	30.97		C
ATOM	2119	O	THR	B	59	−15.367	−9.201	38.575	1.00	31.74		O
ATOM	2120	CB	THR	B	59	−15.786	−11.014	41.142	1.00	36.77		C
ATOM	2121	OG1	THR	B	59	−14.721	−11.403	40.269	1.00	41.80		O
ATOM	2122	CG2	THR	B	59	−16.890	−12.053	41.102	1.00	28.98		C
ATOM	2123	N	ARG	B	60	−14.565	−7.978	40.284	1.00	32.62		N
ATOM	2124	CA	ARG	B	60	−13.693	−7.159	39.449	1.00	36.43		C
ATOM	2125	C	ARG	B	60	−12.441	−7.902	39.022	1.00	35.37		C
ATOM	2126	O	ARG	B	60	−11.819	−8.588	39.825	1.00	33.08		O
ATOM	2127	CB	ARG	B	60	−13.278	−5.877	40.182	1.00	33.09		C
ATOM	2128	CG	ARG	B	60	−14.342	−4.796	40.212	1.00	39.07		C
ATOM	2129	CD	ARG	B	60	−13.752	−3.436	40.558	1.00	37.50		C
ATOM	2130	NE	ARG	B	60	−12.854	−3.495	41.707	1.00	43.68		N
ATOM	2131	CZ	ARG	B	60	−13.259	−3.551	42.971	1.00	51.03		C
ATOM	2132	NH1	ARG	B	60	−14.555	−3.560	43.254	1.00	53.34		N
ATOM	2133	NH2	ARG	B	60	−12.368	−3.603	43.952	1.00	52.19		N
ATOM	2134	N	GLU	B	61	−12.061	−7.747	37.759	1.00	30.40		N
ATOM	2135	CA	GLU	B	61	−10.764	−8.235	37.310	1.00	35.70		C
ATOM	2136	C	GLU	B	61	−9.659	−7.523	38.077	1.00	35.51		C
ATOM	2137	O	GLU	B	61	−9.863	−6.424	38.598	1.00	36.52		O
ATOM	2138	CB	GLU	B	61	−10.582	−8.023	35.805	1.00	30.95		C
ATOM	2139	CG	GLU	B	61	−10.406	−9.307	35.015	1.00	51.01		C
ATOM	2140	CD	GLU	B	61	−9.084	−10.015	35.278	1.00	47.16		C
ATOM	2141	OE1	GLU	B	61	−8.884	−10.535	36.397	1.00	57.21		O
ATOM	2142	OE2	GLU	B	61	−8.245	−10.063	34.354	1.00	55.45		O
ATOM	2143	N	SER	B	62	−8.491	−8.148	38.143	1.00	36.53		N
ATOM	2144	CA	SER	B	62	−7.352	−7.559	38.838	1.00	37.86		C
ATOM	2145	C	SER	B	62	−6.959	−6.222	38.211	1.00	35.62		C
ATOM	2146	O	SER	B	62	−6.919	−6.086	36.992	1.00	34.27		O
ATOM	2147	CB	SER	B	62	−6.166	−8.527	38.822	1.00	40.55		C
ATOM	2148	OG	SER	B	62	−5.113	−8.060	39.646	1.00	56.20		O
ATOM	2149	N	GLY	B	63	−6.690	−5.228	39.049	1.00	32.40		N
ATOM	2150	CA	GLY	B	63	−6.280	−3.924	38.561	1.00	32.97		C
ATOM	2151	C	GLY	B	63	−7.413	−2.971	38.213	1.00	38.33		C
ATOM	2152	O	GLY	B	63	−7.194	−1.767	38.099	1.00	40.50		O
ATOM	2153	N	VAL	B	64	−8.624	−3.498	38.045	1.00	31.70		N
ATOM	2154	CA	VAL	B	64	−9.780	−2.664	37.711	1.00	30.42		C
ATOM	2155	C	VAL	B	64	−10.188	−1.782	38.894	1.00	34.52		C
ATOM	2156	O	VAL	B	64	−10.378	−2.279	40.004	1.00	36.24		O
ATOM	2157	CB	VAL	B	64	−10.988	−3.525	37.269	1.00	33.44		C
ATOM	2158	CG1	VAL	B	64	−12.241	−2.668	37.101	1.00	31.47		C
ATOM	2159	CG2	VAL	B	64	−10.668	−4.271	35.985	1.00	30.34		C
ATOM	2160	N	PRO	B	65	−10.326	−0.466	38.655	1.00	35.36		N
ATOM	2161	CA	PRO	B	65	−10.693	0.500	39.701	1.00	33.81		C
ATOM	2162	C	PRO	B	65	−12.039	0.170	40.344	1.00	36.63		C
ATOM	2163	O	PRO	B	65	−12.940	−0.301	39.649	1.00	30.63		O
ATOM	2164	CB	PRO	B	65	−10.765	1.831	38.946	1.00	31.15		C
ATOM	2165	CG	PRO	B	65	−9.947	1.623	37.710	1.00	35.40		C
ATOM	2166	CD	PRO	B	65	−10.131	0.182	37.347	1.00	33.17		C
ATOM	2167	N	ASP	B	66	−12.177	0.421	41.645	1.00	33.02		N
ATOM	2168	CA	ASP	B	66	−13.408	0.069	42.357	1.00	39.73		C
ATOM	2169	C	ASP	B	66	−14.599	0.965	41.998	1.00	39.77		C
ATOM	2170	O	ASP	B	66	−15.703	0.752	42.499	1.00	35.02		O
ATOM	2171	CB	ASP	B	66	−13.180	0.093	43.874	1.00	38.87		C
ATOM	2172	CG	ASP	B	66	−12.527	1.374	44.354	1.00	46.60		C
ATOM	2173	OD1	ASP	B	66	−12.535	2.376	43.608	1.00	57.95		O
ATOM	2174	OD2	ASP	B	66	−12.004	1.377	45.489	1.00	64.41		O
ATOM	2175	N	ARG	B	67	−14.376	1.953	41.129	1.00	35.35		N
ATOM	2176	CA	ARG	B	67	−15.470	2.752	40.569	1.00	31.85		C
ATOM	2177	C	ARG	B	67	−16.456	1.880	39.807	1.00	34.69		C
ATOM	2178	O	ARG	B	67	−17.638	2.209	39.698	1.00	35.56		O
ATOM	2179	CB	ARG	B	67	−14.947	3.828	39.614	1.00	39.18		C
ATOM	2180	CG	ARG	B	67	−13.752	4.611	40.095	1.00	51.83		C
ATOM	2181	CD	ARG	B	67	−13.589	5.861	39.242	1.00	57.84		C
ATOM	2182	NE	ARG	B	67	−13.490	5.570	37.810	1.00	38.84		N
ATOM	2183	CZ	ARG	B	67	−12.335	5.389	37.179	1.00	42.20		C
ATOM	2184	NH1	ARG	B	67	−11.197	5.458	37.859	1.00	41.09		N
ATOM	2185	NH2	ARG	B	67	−12.314	5.140	35.878	1.00	37.06		N
ATOM	2186	N	PHE	B	68	−15.948	0.785	39.245	1.00	28.82		N
ATOM	2187	CA	PHE	B	68	−16.759	−0.122	38.443	1.00	36.23		C
ATOM	2188	C	PHE	B	68	−17.314	−1.232	39.308	1.00	34.50		C
ATOM	2189	O	PHE	B	68	−16.564	−1.931	39.995	1.00	31.34		O
ATOM	2190	CB	PHE	B	68	−15.941	−0.727	37.297	1.00	30.38		C
ATOM	2191	CG	PHE	B	68	−15.401	0.287	36.337	1.00	34.41		C
ATOM	2192	CD1	PHE	B	68	−16.127	0.651	35.215	1.00	31.80		C
ATOM	2193	CD2	PHE	B	68	−14.163	0.874	36.551	1.00	34.95		C
ATOM	2194	CE1	PHE	B	68	−15.629	1.586	34.328	1.00	29.96		C
ATOM	2195	CE2	PHE	B	68	−13.661	1.807	35.666	1.00	35.32		C
ATOM	2196	CZ	PHE	B	68	−14.396	2.163	34.554	1.00	31.86		C
ATOM	2197	N	SER	B	69	−18.627	−1.408	39.275	1.00	30.82		N
ATOM	2198	CA	SER	B	69	−19.228	−2.482	40.044	1.00	30.92		C
ATOM	2199	C	SER	B	69	−20.364	−3.114	39.268	1.00	34.45		C
ATOM	2200	O	SER	B	69	−20.998	−2.468	38.430	1.00	35.02		O
ATOM	2201	CB	SER	B	69	−19.724	−1.970	41.397	1.00	32.49		C
ATOM	2202	OG	SER	B	69	−20.797	−1.062	41.230	1.00	37.05		O
ATOM	2203	N	GLY	B	70	−20.610	−4.387	39.550	1.00	30.93		N
ATOM	2204	CA	GLY	B	70	−21.673	−5.116	38.896	1.00	28.03		C
ATOM	2205	C	GLY	B	70	−22.689	−5.620	39.898	1.00	38.68		C
ATOM	2206	O	GLY	B	70	−22.361	−5.887	41.056	1.00	36.13		O
ATOM	2207	N	SER	B	71	−23.932	−5.737	39.449	1.00	35.97		N
ATOM	2208	CA	SER	B	71	−24.996	−6.282	40.276	1.00	32.81		C
ATOM	2209	C	SER	B	71	−26.038	−6.927	39.380	1.00	36.09		C
ATOM	2210	O	SER	B	71	−25.980	−6.798	38.157	1.00	36.12		O
ATOM	2211	CB	SER	B	71	−25.632	−5.193	41.136	1.00	38.54		C
ATOM	2212	OG	SER	B	71	−26.284	−4.232	40.322	1.00	42.67		O
ATOM	2213	N	GLY	B	72	−26.996	−7.612	39.992	1.00	35.53		N
ATOM	2214	CA	GLY	B	72	−28.054	−8.256	39.242	1.00	32.26		C
ATOM	2215	C	GLY	B	72	−28.025	−9.760	39.411	1.00	33.08		C
ATOM	2216	O	GLY	B	72	−27.109	−10.312	40.020	1.00	37.03		O
ATOM	2217	N	SER	B	73	−29.038	−10.420	38.869	1.00	35.95		N
ATOM	2218	CA	SER	B	73	−29.166	−11.861	38.993	1.00	39.04		C
ATOM	2219	C	SER	B	73	−30.132	−12.395	37.946	1.00	40.07		C
ATOM	2220	O	SER	B	73	−31.042	−11.691	37.512	1.00	40.54		O
ATOM	2221	CB	SER	B	73	−29.643	−12.235	40.398	1.00	44.78		C
ATOM	2222	OG	SER	B	73	−29.753	−13.638	40.538	1.00	50.73		O
ATOM	2223	N	GLY	B	74	−29.920	−13.638	37.531	1.00	41.84		N
ATOM	2224	CA	GLY	B	74	−30.816	−14.291	36.597	1.00	37.63		C
ATOM	2225	C	GLY	B	74	−30.776	−13.743	35.182	1.00	41.67		C
ATOM	2226	O	GLY	B	74	−29.999	−14.211	34.347	1.00	37.99		O
ATOM	2227	N	THR	B	75	−31.628	−12.761	34.907	1.00	34.80		N
ATOM	2228	CA	THR	B	75	−31.767	−12.239	33.553	1.00	38.56		C
ATOM	2229	C	THR	B	75	−31.515	−10.733	33.475	1.00	38.78		C
ATOM	2230	O	THR	B	75	−31.439	−10.173	32.384	1.00	44.01		O
ATOM	2231	CB	THR	B	75	−33.176	−12.534	32.980	1.00	38.87		C
ATOM	2232	CG2	THR	B	75	−33.477	−14.025	33.021	1.00	37.18		C
ATOM	2233	OG1	THR	B	75	−34.163	−11.838	33.749	1.00	46.98		O
ATOM	2234	N	ASP	B	76	−31.389	−10.083	34.629	1.00	37.55		N
ATOM	2235	CA	ASP	B	76	−31.244	−8.628	34.678	1.00	38.55		C
ATOM	2236	C	ASP	B	76	−29.989	−8.211	35.414	1.00	30.72		C
ATOM	2237	O	ASP	B	76	−29.767	−8.605	36.557	1.00	39.41		O
ATOM	2238	CB	ASP	B	76	−32.463	−7.978	35.340	1.00	39.46		C
ATOM	2239	CG	ASP	B	76	−33.567	−7.680	34.352	1.00	54.19		C
ATOM	2240	OD2	ASP	B	76	−34.444	−8.548	34.149	1.00	61.43		O
ATOM	2241	OD1	ASP	B	76	−33.553	−6.575	33.770	1.00	68.17		O
ATOM	2242	N	PHE	B	77	−29.173	−7.397	34.756	1.00	32.93		N
ATOM	2243	CA	PHE	B	77	−27.890	−6.999	35.314	1.00	34.16		C
ATOM	2244	C	PHE	B	77	−27.608	−5.540	35.021	1.00	28.32		C
ATOM	2245	O	PHE	B	77	−28.054	−5.005	34.010	1.00	34.43		O
ATOM	2246	CB	PHE	B	77	−26.769	−7.870	34.748	1.00	33.65		C
ATOM	2247	CG	PHE	B	77	−27.008	−9.340	34.908	1.00	31.73		C
ATOM	2248	CD1	PHE	B	77	−26.584	−10.004	36.050	1.00	34.33		C
ATOM	2249	CD2	PHE	B	77	−27.663	−10.061	33.924	1.00	30.60		C
ATOM	2250	CE1	PHE	B	77	−26.807	−11.363	36.204	1.00	28.94		C
ATOM	2251	CE2	PHE	B	77	−27.892	−11.420	34.078	1.00	32.18		C
ATOM	2252	CZ	PHE	B	77	−27.463	−12.067	35.215	1.00	28.31		C
ATOM	2253	N	THR	B	78	−26.864	−4.894	35.909	1.00	33.91		N
ATOM	2254	CA	THR	B	78	−26.454	−3.520	35.673	1.00	36.80		C
ATOM	2255	C	THR	B	78	−24.972	−3.332	35.956	1.00	35.53		C
ATOM	2256	O	THR	B	78	−24.429	−3.893	36.909	1.00	33.42		O
ATOM	2257	CB	THR	B	78	−27.250	−2.514	36.536	1.00	36.13		C
ATOM	2258	CG2	THR	B	78	−28.744	−2.790	36.465	1.00	35.39		C
ATOM	2259	OG1	THR	B	78	−26.815	−2.600	37.896	1.00	52.08		O
ATOM	2260	N	LEU	B	79	−24.321	−2.546	35.108	1.00	33.37		N
ATOM	2261	CA	LEU	B	79	−22.978	−2.072	35.382	1.00	32.04		C
ATOM	2262	C	LEU	B	79	−23.082	−0.689	36.000	1.00	35.99		C
ATOM	2263	O	LEU	B	79	−23.805	0.166	35.494	1.00	30.23		O
ATOM	2264	CB	LEU	B	79	−22.138	−2.030	34.105	1.00	32.75		C
ATOM	2265	CG	LEU	B	79	−20.814	−1.269	34.215	1.00	31.00		C
ATOM	2266	CD1	LEU	B	79	−19.875	−1.948	35.189	1.00	30.67		C
ATOM	2267	CD2	LEU	B	79	−20.151	−1.129	32.853	1.00	29.83		C
ATOM	2268	N	THR	B	80	−22.379	−0.467	37.102	1.00	37.73		N
ATOM	2269	CA	THR	B	80	−22.390	0.852	37.711	1.00	37.01		C
ATOM	2270	C	THR	B	80	−20.999	1.468	37.726	1.00	37.89		C
ATOM	2271	O	THR	B	80	−20.044	0.876	38.229	1.00	33.52		O
ATOM	2272	CB	THR	B	80	−22.938	0.816	39.152	1.00	47.22		C
ATOM	2273	CG2	THR	B	80	−22.815	2.194	39.802	1.00	42.48		C
ATOM	2274	OG1	THR	B	80	−24.316	0.427	39.130	1.00	44.17		O
ATOM	2275	N	ILE	B	81	−20.893	2.659	37.152	1.00	36.66		N
ATOM	2276	CA	ILE	B	81	−19.699	3.464	37.321	1.00	35.94		C
ATOM	2277	C	ILE	B	81	−20.013	4.576	38.308	1.00	41.22		C
ATOM	2278	O	ILE	B	81	−20.729	5.527	37.984	1.00	39.45		O
ATOM	2279	CB	ILE	B	81	−19.206	4.068	35.997	1.00	29.74		C
ATOM	2280	CG1	ILE	B	81	−19.077	2.986	34.927	1.00	31.37		C
ATOM	2281	CG2	ILE	B	81	−17.875	4.784	36.204	1.00	37.10		C
ATOM	2282	CD1	ILE	B	81	−18.674	3.527	33.563	1.00	36.05		C
ATOM	2283	N	SER	B	82	−19.506	4.442	39.525	1.00	36.61		N
ATOM	2284	CA	SER	B	82	−19.621	5.521	40.489	1.00	47.92		C
ATOM	2285	C	SER	B	82	−18.478	6.491	40.221	1.00	54.74		C
ATOM	2286	O	SER	B	82	−17.328	6.069	40.079	1.00	68.40		O
ATOM	2287	CB	SER	B	82	−19.571	4.991	41.921	1.00	38.83		C
ATOM	2288	OG	SER	B	82	−18.240	4.674	42.287	1.00	41.65		O
ATOM	2289	N	SER	B	83	−18.803	7.776	40.124	1.00	52.26		N
ATOM	2290	CA	SER	B	83	−17.818	8.825	39.853	1.00	47.12		C
ATOM	2291	C	SER	B	83	−17.144	8.663	38.481	1.00	47.93		C
ATOM	2292	O	SER	B	83	−15.999	8.217	38.381	1.00	37.39		O
ATOM	2293	CB	SER	B	83	−16.763	8.864	40.962	1.00	42.74		C
ATOM	2294	OG	SER	B	83	−15.929	10.003	40.831	1.00	61.34		O
ATOM	2295	N	LEU	B	84	−17.862	9.054	37.432	1.00	39.91		N
ATOM	2296	CA	LEU	B	84	−17.373	8.932	36.061	1.00	40.35		C
ATOM	2297	C	LEU	B	84	−16.120	9.777	35.825	1.00	43.92		C
ATOM	2298	O	LEU	B	84	−16.079	10.954	36.188	1.00	32.91		O
ATOM	2299	CB	LEU	B	84	−18.470	9.334	35.072	1.00	36.00		C
ATOM	2300	CG	LEU	B	84	−18.281	8.902	33.616	1.00	40.11		C
ATOM	2301	CD1	LEU	B	84	−18.455	7.396	33.472	1.00	34.46		C
ATOM	2302	CD2	LEU	B	84	−19.246	9.639	32.702	1.00	39.38		C
ATOM	2303	N	GLN	B	85	−15.103	9.166	35.221	1.00	35.37		N
ATOM	2304	CA	GLN	B	85	−13.839	9.844	34.940	1.00	35.03		C
ATOM	2305	C	GLN	B	85	−13.682	10.088	33.432	1.00	35.85		C
ATOM	2306	O	GLN	B	85	−14.311	9.400	32.627	1.00	30.69		O
ATOM	2307	CB	GLN	B	85	−12.665	9.023	35.484	1.00	33.69		C
ATOM	2308	CG	GLN	B	85	−12.719	8.782	36.990	1.00	39.42		C
ATOM	2309	CD	GLN	B	85	−12.651	10.069	37.795	1.00	43.01		C
ATOM	2310	NE2	GLN	B	85	−13.732	10.386	38.500	1.00	38.02		N
ATOM	2311	OE1	GLN	B	85	−11.640	10.772	37.778	1.00	40.65		O
ATOM	2312	N	PRO	B	86	−12.857	11.082	33.046	1.00	33.28		N
ATOM	2313	CA	PRO	B	86	−12.643	11.413	31.631	1.00	31.64		C
ATOM	2314	C	PRO	B	86	−12.220	10.209	30.792	1.00	35.32		C
ATOM	2315	O	PRO	B	86	−12.635	10.093	29.641	1.00	30.64		O
ATOM	2316	CB	PRO	B	86	−11.520	12.456	31.681	1.00	34.31		C
ATOM	2317	CG	PRO	B	86	−11.690	13.108	33.001	1.00	42.02		C
ATOM	2318	CD	PRO	B	86	−12.146	12.020	33.936	1.00	35.55		C
ATOM	2319	N	GLU	B	87	−11.423	9.316	31.373	1.00	32.17		N
ATOM	2320	CA	GLU	B	87	−10.921	8.161	30.637	1.00	31.69		C
ATOM	2321	C	GLU	B	87	−11.975	7.063	30.470	1.00	31.13		C
ATOM	2322	O	GLU	B	87	−11.744	6.086	29.761	1.00	31.02		O
ATOM	2323	CB	GLU	B	87	−9.681	7.583	31.327	1.00	32.83		C
ATOM	2324	CG	GLU	B	87	−9.941	6.983	32.703	1.00	34.70		C
ATOM	2325	CD	GLU	B	87	−9.628	7.950	33.834	1.00	47.47		C
ATOM	2326	OE1	GLU	B	87	−9.890	9.166	33.681	1.00	39.21		O
ATOM	2327	OE2	GLU	B	87	−9.111	7.486	34.876	1.00	49.29		O
ATOM	2328	N	ASP	B	88	−13.131	7.227	31.108	1.00	28.67		N
ATOM	2329	CA	ASP	B	88	−14.175	6.210	31.053	1.00	29.26		C
ATOM	2330	C	ASP	B	88	−15.032	6.315	29.787	1.00	31.41		C
ATOM	2331	O	ASP	B	88	−15.961	5.532	29.602	1.00	31.09		O
ATOM	2332	CB	ASP	B	88	−15.070	6.293	32.295	1.00	32.59		C
ATOM	2333	CG	ASP	B	88	−14.287	6.153	33.595	1.00	39.45		C
ATOM	2334	OD1	ASP	B	88	−13.166	5.597	33.565	1.00	34.75		O
ATOM	2335	OD2	ASP	B	88	−14.794	6.595	34.650	1.00	40.00		O
ATOM	2336	N	VAL	B	89	−14.725	7.276	28.920	1.00	27.74		N
ATOM	2337	CA	VAL	B	89	−15.437	7.395	27.648	1.00	29.97		C
ATOM	2338	C	VAL	B	89	−15.162	6.169	26.783	1.00	26.75		C
ATOM	2339	O	VAL	B	89	−14.020	5.928	26.391	1.00	32.52		O
ATOM	2340	CB	VAL	B	89	−15.029	8.662	26.862	1.00	36.47		C
ATOM	2341	CG1	VAL	B	89	−15.785	8.732	25.538	1.00	36.88		C
ATOM	2342	CG2	VAL	B	89	−15.281	9.908	27.681	1.00	41.88		C
ATOM	2343	N	ALA	B	90	−16.209	5.410	26.479	1.00	25.10		N
ATOM	2344	CA	ALA	B	90	−16.063	4.149	25.764	1.00	28.51		C
ATOM	2345	C	ALA	B	90	−17.410	3.508	25.491	1.00	30.70		C
ATOM	2346	O	ALA	B	90	−18.448	3.995	25.943	1.00	27.64		O
ATOM	2347	CB	ALA	B	90	−15.185	3.178	26.561	1.00	30.46		C
ATOM	2348	N	VAL	B	91	−17.377	2.401	24.755	1.00	29.92		N
ATOM	2349	CA	VAL	B	91	−18.539	1.542	24.606	1.00	28.27		C
ATOM	2350	C	VAL	B	91	−18.425	0.364	25.573	1.00	33.48		C
ATOM	2351	O	VAL	B	91	−17.368	−0.265	25.684	1.00	25.89		O
ATOM	2352	CB	VAL	B	91	−18.683	1.024	23.172	1.00	28.97		C
ATOM	2353	CG1	VAL	B	91	−19.940	0.178	23.045	1.00	28.55		C
ATOM	2354	CG2	VAL	B	91	−18.723	2.194	22.196	1.00	29.32		C
ATOM	2355	N	TYR	B	92	−19.511	0.077	26.281	1.00	29.51		N
ATOM	2356	CA	TYR	B	92	−19.509	−0.993	27.267	1.00	29.47		C
ATOM	2357	C	TYR	B	92	−20.379	−2.148	26.793	1.00	33.18		C
ATOM	2358	O	TYR	B	92	−21.477	−1.945	26.267	1.00	29.29		O
ATOM	2359	CB	TYR	B	92	−19.978	−0.472	28.630	1.00	23.56		C
ATOM	2360	CG	TYR	B	92	−19.010	0.510	29.254	1.00	27.95		C
ATOM	2361	CD2	TYR	B	92	−18.114	0.104	30.236	1.00	31.49		C
ATOM	2362	CD1	TYR	B	92	−18.978	1.841	28.848	1.00	28.41		C
ATOM	2363	CE2	TYR	B	92	−17.222	0.995	30.808	1.00	26.89		C
ATOM	2364	CE1	TYR	B	92	−18.086	2.740	29.411	1.00	25.28		C
ATOM	2365	CZ	TYR	B	92	−17.213	2.309	30.387	1.00	27.09		C
ATOM	2366	OH	TYR	B	92	−16.325	3.190	30.940	1.00	27.92		O
ATOM	2367	N	TYR	B	93	−19.863	−3.361	26.962	1.00	27.67		N
ATOM	2368	CA	TYR	B	93	−20.548	−4.569	26.524	1.00	26.66		C
ATOM	2369	C	TYR	B	93	−20.725	−5.548	27.673	1.00	29.56		C
ATOM	2370	O	TYR	B	93	−19.802	−5.759	28.458	1.00	27.75		O
ATOM	2371	CB	TYR	B	93	−19.765	−5.270	25.412	1.00	25.28		C
ATOM	2372	CG	TYR	B	93	−19.615	−4.503	24.125	1.00	28.54		C
ATOM	2373	CD2	TYR	B	93	−20.529	−4.662	23.090	1.00	26.88		C
ATOM	2374	CD1	TYR	B	93	−18.540	−3.644	23.928	1.00	27.13		C
ATOM	2375	CE2	TYR	B	93	−20.386	−3.973	21.899	1.00	32.89		C
ATOM	2376	CE1	TYR	B	93	−18.385	−2.955	22.743	1.00	29.51		C
ATOM	2377	CZ	TYR	B	93	−19.309	−3.123	21.731	1.00	32.69		C
ATOM	2378	OH	TYR	B	93	−19.161	−2.436	20.550	1.00	33.36		O
ATOM	2379	N	CYS	B	94	−21.901	−6.157	27.762	1.00	25.68		N
ATOM	2380	CA	CYS	B	94	−22.079	−7.300	28.644	1.00	25.53		C
ATOM	2381	C	CYS	B	94	−21.899	−8.557	27.810	1.00	28.07		C
ATOM	2382	O	CYS	B	94	−22.013	−8.516	26.585	1.00	28.25		O
ATOM	2383	CB	CYS	B	94	−23.450	−7.282	29.329	1.00	30.94		C
ATOM	2384	SG	CYS	B	94	−24.873	−7.383	28.210	1.00	35.78		S
ATOM	2385	N	GLN	B	95	−21.606	−9.671	28.468	1.00	25.81		N
ATOM	2386	CA	GLN	B	95	−21.373	−10.920	27.758	1.00	28.41		C
ATOM	2387	C	GLN	B	95	−21.819	−12.093	28.612	1.00	24.10		C
ATOM	2388	O	GLN	B	95	−21.476	−12.169	29.789	1.00	33.33		O
ATOM	2389	CB	GLN	B	95	−19.891	−11.065	27.391	1.00	24.57		C
ATOM	2390	CG	GLN	B	95	−19.574	−12.277	26.523	1.00	27.70		C
ATOM	2391	CD	GLN	B	95	−18.497	−13.168	27.121	1.00	30.66		C
ATOM	2392	NE2	GLN	B	95	−18.756	−14.468	27.147	1.00	41.67		N
ATOM	2393	OE1	GLN	B	95	−17.452	−12.695	27.557	1.00	36.39		O
ATOM	2394	N	GLN	B	96	−22.584	−13.008	28.031	1.00	30.99		N
ATOM	2395	CA	GLN	B	96	−22.926	−14.232	28.748	1.00	28.28		C
ATOM	2396	C	GLN	B	96	−21.986	−15.347	28.313	1.00	31.50		C
ATOM	2397	O	GLN	B	96	−21.612	−15.447	27.141	1.00	27.92		O
ATOM	2398	CB	GLN	B	96	−24.392	−14.630	28.517	1.00	24.83		C
ATOM	2399	CG	GLN	B	96	−24.737	−15.108	27.104	1.00	28.68		C
ATOM	2400	CD	GLN	B	96	−24.439	−16.586	26.876	1.00	32.36		C
ATOM	2401	NE2	GLN	B	96	−24.396	−16.992	25.611	1.00	32.40		N
ATOM	2402	OE1	GLN	B	96	−24.241	−17.348	27.826	1.00	32.56		O
ATOM	2403	N	TYR	B	97	−21.592	−16.182	29.261	1.00	26.53		N
ATOM	2404	CA	TYR	B	97	−20.838	−17.370	28.918	1.00	30.75		C
ATOM	2405	C	TYR	B	97	−21.465	−18.571	29.608	1.00	31.37		C
ATOM	2406	O	TYR	B	97	−20.778	−19.519	29.989	1.00	28.22		O
ATOM	2407	CB	TYR	B	97	−19.367	−17.209	29.294	1.00	27.16		C
ATOM	2408	CG	TYR	B	97	−19.121	−16.745	30.714	1.00	30.11		C
ATOM	2409	CD2	TYR	B	97	−18.893	−17.661	31.737	1.00	25.04		C
ATOM	2410	CD1	TYR	B	97	−19.093	−15.390	31.026	1.00	26.12		C
ATOM	2411	CE2	TYR	B	97	−18.650	−17.239	33.033	1.00	26.05		C
ATOM	2412	CE1	TYR	B	97	−18.856	−14.960	32.316	1.00	30.26		C
ATOM	2413	CZ	TYR	B	97	−18.634	−15.887	33.314	1.00	28.89		C
ATOM	2414	OH	TYR	B	97	−18.396	−15.458	34.597	1.00	29.84		O
ATOM	2415	N	TYR	B	98	−22.784	−18.510	29.762	1.00	37.70		N
ATOM	2416	CA	TYR	B	98	−23.553	−19.601	30.349	1.00	32.36		C
ATOM	2417	C	TYR	B	98	−23.579	−20.801	29.410	1.00	37.08		C
ATOM	2418	O	TYR	B	98	−23.446	−21.942	29.849	1.00	37.43		O
ATOM	2419	CB	TYR	B	98	−24.981	−19.153	30.672	1.00	32.63		C
ATOM	2420	CG	TYR	B	98	−25.769	−20.191	31.440	1.00	40.80		C
ATOM	2421	CD1	TYR	B	98	−25.434	−20.511	32.750	1.00	39.01		C
ATOM	2422	CD2	TYR	B	98	−26.844	−20.853	30.857	1.00	44.09		C
ATOM	2423	CE1	TYR	B	98	−26.146	−21.462	33.461	1.00	46.24		C
ATOM	2424	CE2	TYR	B	98	−27.566	−21.807	31.563	1.00	46.44		C
ATOM	2425	CZ	TYR	B	98	−27.209	−22.107	32.864	1.00	48.82		C
ATOM	2426	OH	TYR	B	98	−27.913	−23.052	33.574	1.00	61.88		O
ATOM	2427	N	ASN	B	99	−23.758	−20.542	28.117	1.00	36.19		N
ATOM	2428	CA	ASN	B	99	−23.611	−21.596	27.119	1.00	44.15		C
ATOM	2429	C	ASN	B	99	−23.116	−21.074	25.778	1.00	42.06		C
ATOM	2430	O	ASN	B	99	−23.118	−19.868	25.521	1.00	43.16		O
ATOM	2431	CB	ASN	B	99	−24.927	−22.361	26.924	1.00	49.30		C
ATOM	2432	CG	ASN	B	99	−26.102	−21.455	26.600	1.00	51.38		C
ATOM	2433	OD1	ASN	B	99	−27.134	−21.508	27.271	1.00	68.12		O
ATOM	2434	ND2	ASN	B	99	−25.959	−20.628	25.568	1.00	49.12		N
ATOM	2435	N	THR	B	100	−22.700	−22.001	24.924	1.00	38.31		N
ATOM	2436	CA	THR	B	100	−22.195	−21.657	23.607	1.00	37.71		C
ATOM	2437	C	THR	B	100	−23.339	−21.679	22.601	1.00	36.72		C
ATOM	2438	O	THR	B	100	−24.243	−22.506	22.713	1.00	45.21		O
ATOM	2439	CB	THR	B	100	−21.076	−22.618	23.173	1.00	40.81		C
ATOM	2440	OG1	THR	B	100	−21.540	−23.966	23.286	1.00	41.71		O
ATOM	2441	CG2	THR	B	100	−19.855	−22.442	24.069	1.00	34.33		C
ATOM	2442	N	PRO	B	101	−23.313	−20.765	21.617	1.00	37.91		N
ATOM	2443	CA	PRO	B	101	−22.253	−19.773	21.404	1.00	35.04		C
ATOM	2444	C	PRO	B	101	−22.295	−18.613	22.395	1.00	38.94		C
ATOM	2445	O	PRO	B	101	−23.368	−18.135	22.774	1.00	33.27		O
ATOM	2446	CB	PRO	B	101	−22.526	−19.273	19.983	1.00	36.11		C
ATOM	2447	CG	PRO	B	101	−24.004	−19.394	19.839	1.00	36.49		C
ATOM	2448	CD	PRO	B	101	−24.388	−20.638	20.615	1.00	42.27		C
ATOM	2449	N	VAL	B	102	−21.111	−18.192	22.823	1.00	35.40		N
ATOM	2450	CA	VAL	B	102	−20.943	−16.980	23.610	1.00	34.45		C
ATOM	2451	C	VAL	B	102	−21.531	−15.794	22.858	1.00	35.11		C
ATOM	2452	O	VAL	B	102	−21.300	−15.643	21.659	1.00	30.87		O
ATOM	2453	CB	VAL	B	102	−19.454	−16.735	23.911	1.00	38.34		C
ATOM	2454	CG1	VAL	B	102	−19.155	−15.250	24.058	1.00	41.39		C
ATOM	2455	CG2	VAL	B	102	−19.046	−17.509	25.142	1.00	38.42		C
ATOM	2456	N	THR	B	103	−22.307	−14.966	23.549	1.00	28.91		N
ATOM	2457	CA	THR	B	103	−22.929	−13.817	22.901	1.00	32.04		C
ATOM	2458	C	THR	B	103	−22.740	−12.532	23.711	1.00	33.94		C
ATOM	2459	O	THR	B	103	−22.715	−12.554	24.945	1.00	30.64		O
ATOM	2460	CB	THR	B	103	−24.437	−14.054	22.659	1.00	33.42		C
ATOM	2461	CG2	THR	B	103	−24.658	−15.178	21.636	1.00	30.57		C
ATOM	2462	OG1	THR	B	103	−25.068	−14.415	23.890	1.00	35.52		O
ATOM	2463	N	PHE	B	104	−22.594	−11.419	22.996	1.00	27.76		N
ATOM	2464	CA	PHE	B	104	−22.429	−10.102	23.604	1.00	32.55		C
ATOM	2465	C	PHE	B	104	−23.693	−9.274	23.430	1.00	34.05		C
ATOM	2466	O	PHE	B	104	−24.481	−9.520	22.519	1.00	32.37		O
ATOM	2467	CB	PHE	B	104	−21.257	−9.342	22.971	1.00	30.42		C
ATOM	2468	CG	PHE	B	104	−19.915	−9.986	23.175	1.00	30.59		C
ATOM	2469	CD1	PHE	B	104	−19.531	−11.079	22.417	1.00	27.18		C
ATOM	2470	CD2	PHE	B	104	−19.019	−9.467	24.094	1.00	30.39		C
ATOM	2471	CE1	PHE	B	104	−18.289	−11.660	22.590	1.00	31.59		C
ATOM	2472	CE2	PHE	B	104	−17.775	−10.044	24.274	1.00	31.20		C
ATOM	2473	CZ	PHE	B	104	−17.411	−11.144	23.519	1.00	33.50		C
ATOM	2474	N	GLY	B	105	−23.873	−8.278	24.291	1.00	34.23		N
ATOM	2475	CA	GLY	B	105	−24.878	−7.258	24.057	1.00	26.27		C
ATOM	2476	C	GLY	B	105	−24.415	−6.334	22.941	1.00	34.89		C
ATOM	2477	O	GLY	B	105	−23.264	−6.413	22.509	1.00	31.29		O
ATOM	2478	N	PRO	B	106	−25.307	−5.447	22.470	1.00	35.38		N
ATOM	2479	CA	PRO	B	106	−25.028	−4.559	21.336	1.00	33.90		C
ATOM	2480	C	PRO	B	106	−24.100	−3.399	21.689	1.00	32.12		C
ATOM	2481	O	PRO	B	106	−23.610	−2.715	20.794	1.00	34.27		O
ATOM	2482	CB	PRO	B	106	−26.417	−4.037	20.956	1.00	29.01		C
ATOM	2483	CG	PRO	B	106	−27.173	−4.053	22.248	1.00	37.44		C
ATOM	2484	CD	PRO	B	106	−26.676	−5.267	22.989	1.00	33.03		C
ATOM	2485	N	GLY	B	107	−23.874	−3.177	22.978	1.00	34.23		N
ATOM	2486	CA	GLY	B	107	−22.984	−2.120	23.415	1.00	34.20		C
ATOM	2487	C	GLY	B	107	−23.701	−0.843	23.807	1.00	34.29		C
ATOM	2488	O	GLY	B	107	−24.725	−0.489	23.230	1.00	37.38		O
ATOM	2489	N	THR	B	108	−23.149	−0.148	24.795	1.00	33.98		N
ATOM	2490	CA	THR	B	108	−23.695	1.121	25.256	1.00	35.86		C
ATOM	2491	C	THR	B	108	−22.617	2.190	25.231	1.00	33.06		C
ATOM	2492	O	THR	B	108	−21.586	2.039	25.886	1.00	33.05		O
ATOM	2493	CB	THR	B	108	−24.251	1.016	26.690	1.00	31.62		C
ATOM	2494	CG2	THR	B	108	−24.619	2.395	27.221	1.00	36.86		C
ATOM	2495	OG1	THR	B	108	−25.406	0.174	26.702	1.00	36.12		O
ATOM	2496	N	LYS	B	109	−22.847	3.271	24.493	1.00	28.00		N
ATOM	2497	CA	LYS	B	109	−21.850	4.337	24.418	1.00	33.62		C
ATOM	2498	C	LYS	B	109	−21.956	5.254	25.634	1.00	38.15		C
ATOM	2499	O	LYS	B	109	−23.026	5.786	25.931	1.00	41.81		O
ATOM	2500	CB	LYS	B	109	−22.008	5.142	23.124	1.00	36.39		C
ATOM	2501	CG	LYS	B	109	−22.625	4.343	21.980	1.00	56.96		C
ATOM	2502	CD	LYS	B	109	−21.807	4.421	20.696	1.00	56.13		C
ATOM	2503	CE	LYS	B	109	−21.884	5.792	20.054	1.00	62.08		C
ATOM	2504	NZ	LYS	B	109	−21.138	5.822	18.763	1.00	74.82		N
ATOM	2505	N	VAL	B	110	−20.848	5.420	26.348	1.00	32.23		N
ATOM	2506	CA	VAL	B	110	−20.804	6.345	27.474	1.00	29.73		C
ATOM	2507	C	VAL	B	110	−19.884	7.524	27.185	1.00	32.33		C
ATOM	2508	O	VAL	B	110	−18.699	7.340	26.904	1.00	33.08		O
ATOM	2509	CB	VAL	B	110	−20.328	5.659	28.765	1.00	31.47		C
ATOM	2510	CG1	VAL	B	110	−20.223	6.678	29.886	1.00	29.96		C
ATOM	2511	CG2	VAL	B	110	−21.270	4.525	29.142	1.00	34.90		C
ATOM	2512	N	GLY	B	111	−20.440	8.730	27.249	1.00	29.76		N
ATOM	2513	CA	GLY	B	111	−19.666	9.945	27.076	1.00	29.88		C
ATOM	2514	C	GLY	B	111	−19.749	10.757	28.351	1.00	39.68		C
ATOM	2515	O	GLY	B	111	−20.459	10.374	29.280	1.00	39.37		O
ATOM	2516	N	ILE	B	112	−19.030	11.872	28.416	1.00	31.76		N
ATOM	2517	CA	ILE	B	112	−19.082	12.697	29.613	1.00	36.49		C
ATOM	2518	C	ILE	B	112	−19.508	14.132	29.295	1.00	41.86		C
ATOM	2519	O	ILE	B	112	−19.221	14.665	28.216	1.00	33.11		O
ATOM	2520	CB	ILE	B	112	−17.720	12.704	30.366	1.00	36.62		C
ATOM	2521	CG1	ILE	B	112	−16.745	13.711	29.766	1.00	42.34		C
ATOM	2522	CG2	ILE	B	112	−17.105	11.311	30.403	1.00	53.62		C
ATOM	2523	CD1	ILE	B	112	−16.711	15.042	30.519	1.00	54.93		C
ATOM	2524	O	LYS	B	113	−19.210	16.754	32.044	1.00	44.16		O
ATOM	2525	N	LYS	B	113	−20.201	14.744	30.251	1.00	37.92		N
ATOM	2526	CA	LYS	B	113	−20.582	16.147	30.170	1.00	39.34		C
ATOM	2527	C	LYS	B	113	−19.560	17.015	30.892	1.00	43.78		C
ATOM	2528	CB	LYS	B	113	−21.965	16.381	30.778	1.00	41.17		C
ATOM	2529	CG	LYS	B	113	−23.120	15.740	30.040	1.00	40.99		C
ATOM	2530	CD	LYS	B	113	−24.434	16.062	30.750	1.00	46.55		C
ATOM	2531	CE	LYS	B	113	−25.614	15.365	30.094	1.00	50.82		C
ATOM	2532	NZ	LYS	B	113	−26.868	15.545	30.882	1.00	66.34		N
ATOM	2533	O	ARG	B	114	−19.706	20.614	29.907	1.00	33.63		O
ATOM	2534	N	ARG	B	114	−19.080	18.045	30.208	1.00	37.75		N
ATOM	2535	CA	ARG	B	114	−18.179	19.009	30.821	1.00	32.69		C
ATOM	2536	C	ARG	B	114	−18.661	20.423	30.526	1.00	32.37		C
ATOM	2537	CB	ARG	B	114	−16.747	18.815	30.316	1.00	29.43		C
ATOM	2538	CG	ARG	B	114	−16.605	18.850	28.801	1.00	32.96		C
ATOM	2539	CD	ARG	B	114	−15.228	19.372	28.400	1.00	29.78		C
ATOM	2540	NE	ARG	B	114	−15.053	20.768	28.793	1.00	30.75		N
ATOM	2541	CZ	ARG	B	114	−13.893	21.418	28.775	1.00	35.05		C
ATOM	2542	NH1	ARG	B	114	−13.841	22.691	29.144	1.00	37.02		N
ATOM	2543	NH2	ARG	B	114	−12.784	20.801	28.392	1.00	37.36		N
ATOM	2544	O	THR	B	115	−17.390	22.466	28.475	1.00	30.86		O
ATOM	2545	N	THR	B	115	−17.898	21.413	30.968	1.00	34.13		N
ATOM	2546	CA	THR	B	115	−18.244	22.800	30.701	1.00	37.77		C
ATOM	2547	C	THR	B	115	−18.146	23.108	29.207	1.00	38.67		C
ATOM	2548	CB	THR	B	115	−17.336	23.763	31.484	1.00	35.59		C
ATOM	2549	OG1	THR	B	115	−15.972	23.545	31.106	1.00	34.24		O
ATOM	2550	CG2	THR	B	115	−17.485	23.531	32.986	1.00	28.14		C
ATOM	2551	N	VAL	B	116	−18.932	24.080	28.762	1.00	39.57		N
ATOM	2552	CA	VAL	B	116	−18.884	24.545	27.383	1.00	35.06		C
ATOM	2553	C	VAL	B	116	−17.491	25.075	27.047	1.00	35.92		C
ATOM	2554	O	VAL	B	116	−16.872	25.772	27.855	1.00	32.43		O
ATOM	2555	CB	VAL	B	116	−19.938	25.649	27.133	1.00	35.82		C
ATOM	2556	CG1	VAL	B	116	−19.734	26.295	25.778	1.00	33.41		C
ATOM	2557	CG2	VAL	B	116	−21.347	25.082	27.253	1.00	29.35		C
ATOM	2558	N	ALA	B	117	−16.991	24.725	25.865	1.00	29.09		N
ATOM	2559	CA	ALA	B	117	−15.719	25.259	25.387	1.00	27.87		C
ATOM	2560	C	ALA	B	117	−15.829	25.618	23.913	1.00	34.19		C
ATOM	2561	O	ALA	B	117	−16.203	24.779	23.088	1.00	29.90		O
ATOM	2562	CB	ALA	B	117	−14.589	24.258	25.615	1.00	30.76		C
ATOM	2563	N	ALA	B	118	−15.522	26.870	23.588	1.00	32.82		N
ATOM	2564	CA	ALA	B	118	−15.615	27.347	22.212	1.00	34.29		C
ATOM	2565	C	ALA	B	118	−14.474	26.788	21.370	1.00	29.81		C
ATOM	2566	O	ALA	B	118	−13.357	26.625	21.858	1.00	31.85		O
ATOM	2567	CB	ALA	B	118	−15.614	28.877	22.173	1.00	29.49		C
ATOM	2568	N	PRO	B	119	−14.753	26.481	20.097	1.00	31.49		N
ATOM	2569	CA	PRO	B	119	−13.680	25.979	19.237	1.00	32.80		C
ATOM	2570	C	PRO	B	119	−12.745	27.089	18.790	1.00	34.11		C
ATOM	2571	O	PRO	B	119	−13.190	28.218	18.601	1.00	30.89		O
ATOM	2572	CB	PRO	B	119	−14.436	25.404	18.039	1.00	29.59		C
ATOM	2573	CG	PRO	B	119	−15.668	26.247	17.957	1.00	33.03		C
ATOM	2574	CD	PRO	B	119	−16.043	26.559	19.386	1.00	30.58		C
ATOM	2575	N	SER	B	120	−11.467	26.769	18.635	1.00	29.42		N
ATOM	2576	CA	SER	B	120	−10.567	27.624	17.878	1.00	36.74		C
ATOM	2577	C	SER	B	120	−10.661	27.181	16.418	1.00	34.59		C
ATOM	2578	O	SER	B	120	−10.687	25.983	16.131	1.00	33.48		O
ATOM	2579	CB	SER	B	120	−9.135	27.531	18.407	1.00	31.92		C
ATOM	2580	OG	SER	B	120	−8.627	26.219	18.245	1.00	50.83		O
ATOM	2581	N	VAL	B	121	−10.734	28.139	15.499	1.00	34.03		N
ATOM	2582	CA	VAL	B	121	−11.015	27.831	14.096	1.00	29.08		C
ATOM	2583	C	VAL	B	121	−9.845	28.195	13.179	1.00	31.62		C
ATOM	2584	O	VAL	B	121	−9.239	29.257	13.314	1.00	33.72		O
ATOM	2585	CB	VAL	B	121	−12.300	28.560	13.616	1.00	30.04		C
ATOM	2586	CG1	VAL	B	121	−12.663	28.158	12.193	1.00	30.45		C
ATOM	2587	CG2	VAL	B	121	−13.460	28.259	14.551	1.00	31.72		C
ATOM	2588	N	PHE	B	122	−9.534	27.295	12.251	1.00	27.86		N
ATOM	2589	CA	PHE	B	122	−8.463	27.498	11.283	1.00	29.57		C
ATOM	2590	C	PHE	B	122	−8.935	27.084	9.890	1.00	39.92		C
ATOM	2591	O	PHE	B	122	−9.622	26.068	9.734	1.00	34.52		O
ATOM	2592	CB	PHE	B	122	−7.215	26.689	11.663	1.00	36.36		C
ATOM	2593	CG	PHE	B	122	−6.747	26.906	13.078	1.00	32.19		C
ATOM	2594	CD1	PHE	B	122	−7.271	26.158	14.117	1.00	36.97		C
ATOM	2595	CD2	PHE	B	122	−5.770	27.847	13.362	1.00	34.40		C
ATOM	2596	CE1	PHE	B	122	−6.836	26.352	15.419	1.00	41.91		C
ATOM	2597	CE2	PHE	B	122	−5.330	28.044	14.661	1.00	36.84		C
ATOM	2598	CZ	PHE	B	122	−5.864	27.294	15.689	1.00	37.49		C
ATOM	2599	N	ILE	B	123	−8.566	27.862	8.879	1.00	28.07		N
ATOM	2600	CA	ILE	B	123	−8.915	27.528	7.505	1.00	32.41		C
ATOM	2601	C	ILE	B	123	−7.636	27.277	6.701	1.00	32.00		C
ATOM	2602	O	ILE	B	123	−6.622	27.942	6.907	1.00	31.75		O
ATOM	2603	CB	ILE	B	123	−9.777	28.646	6.846	1.00	28.87		C
ATOM	2604	CG1	ILE	B	123	−10.347	28.183	5.502	1.00	32.47		C
ATOM	2605	CG2	ILE	B	123	−8.985	29.938	6.700	1.00	28.48		C
ATOM	2606	CD1	ILE	B	123	−11.358	29.154	4.896	1.00	31.95		C
ATOM	2607	N	PHE	B	124	−7.679	26.291	5.811	1.00	31.26		N
ATOM	2608	CA	PHE	B	124	−6.514	25.928	5.009	1.00	30.58		C
ATOM	2609	C	PHE	B	124	−6.854	25.944	3.523	1.00	35.12		C
ATOM	2610	O	PHE	B	124	−7.774	25.250	3.089	1.00	33.03		O
ATOM	2611	CB	PHE	B	124	−5.992	24.540	5.390	1.00	32.40		C
ATOM	2612	CG	PHE	B	124	−5.566	24.410	6.825	1.00	32.10		C
ATOM	2613	CD1	PHE	B	124	−4.314	24.842	7.232	1.00	31.26		C
ATOM	2614	CD2	PHE	B	124	−6.407	23.820	7.759	1.00	31.84		C
ATOM	2615	CE1	PHE	B	124	−3.913	24.711	8.549	1.00	34.33		C
ATOM	2616	CE2	PHE	B	124	−6.015	23.684	9.076	1.00	34.28		C
ATOM	2617	CZ	PHE	B	124	−4.765	24.133	9.474	1.00	35.30		C
ATOM	2618	N	PRO	B	125	−6.107	26.731	2.734	1.00	37.67		N
ATOM	2619	CA	PRO	B	125	−6.296	26.753	1.278	1.00	33.34		C
ATOM	2620	C	PRO	B	125	−5.816	25.454	0.646	1.00	32.58		C
ATOM	2621	O	PRO	B	125	−4.996	24.766	1.247	1.00	29.20		O
ATOM	2622	CB	PRO	B	125	−5.422	27.930	0.816	1.00	33.45		C
ATOM	2623	CG	PRO	B	125	−5.036	28.671	2.074	1.00	39.04		C
ATOM	2624	CD	PRO	B	125	−5.049	27.658	3.171	1.00	32.49		C
ATOM	2625	N	PRO	B	126	−6.307	25.126	−0.557	1.00	31.25		N
ATOM	2626	CA	PRO	B	126	−5.736	23.974	−1.263	1.00	36.87		C
ATOM	2627	C	PRO	B	126	−4.265	24.213	−1.615	1.00	37.25		C
ATOM	2628	O	PRO	B	126	−3.844	25.360	−1.778	1.00	32.38		O
ATOM	2629	CB	PRO	B	126	−6.599	23.868	−2.527	1.00	31.74		C
ATOM	2630	CG	PRO	B	126	−7.137	25.243	−2.728	1.00	32.69		C
ATOM	2631	CD	PRO	B	126	−7.351	25.800	−1.348	1.00	31.78		C
ATOM	2632	N	SER	B	127	−3.491	23.139	−1.709	1.00	33.45		N
ATOM	2633	CA	SER	B	127	−2.082	23.251	−2.055	1.00	37.63		C
ATOM	2634	C	SER	B	127	−1.931	23.368	−3.565	1.00	41.08		C
ATOM	2635	O	SER	B	127	−2.812	22.939	−4.317	1.00	38.62		O
ATOM	2636	CB	SER	B	127	−1.299	22.043	−1.542	1.00	33.64		C
ATOM	2637	OG	SER	B	127	−1.647	20.874	−2.267	1.00	31.28		O
ATOM	2638	N	ASP	B	128	−0.814	23.938	−4.008	1.00	40.33		N
ATOM	2639	CA	ASP	B	128	−0.544	24.044	−5.437	1.00	42.97		C
ATOM	2640	C	ASP	B	128	−0.439	22.664	−6.066	1.00	36.76		C
ATOM	2641	O	ASP	B	128	−0.783	22.481	−7.232	1.00	42.27		O
ATOM	2642	CB	ASP	B	128	0.737	24.841	−5.695	1.00	46.63		C
ATOM	2643	CG	ASP	B	128	0.570	26.322	−5.406	1.00	59.28		C
ATOM	2644	OD1	ASP	B	128	−0.562	26.834	−5.546	1.00	59.20		O
ATOM	2645	OD2	ASP	B	128	1.570	26.974	−5.040	1.00	62.56		O
ATOM	2646	N	GLU	B	129	0.022	21.690	−5.286	1.00	37.90		N
ATOM	2647	CA	GLU	B	129	0.240	20.347	−5.809	1.00	41.75		C
ATOM	2648	C	GLU	B	129	−1.075	19.666	−6.183	1.00	42.49		C
ATOM	2649	O	GLU	B	129	−1.157	18.982	−7.202	1.00	42.15		O
ATOM	2650	CB	GLU	B	129	1.008	19.489	−4.800	1.00	38.29		C
ATOM	2651	CG	GLU	B	129	1.521	18.181	−5.394	1.00	55.48		C
ATOM	2652	CD	GLU	B	129	2.471	17.435	−4.469	1.00	75.53		C
ATOM	2653	OE1	GLU	B	129	3.644	17.234	−4.857	1.00	78.69		O
ATOM	2654	OE2	GLU	B	129	2.044	17.043	−3.360	1.00	72.25		O
ATOM	2655	N	GLN	B	130	−2.104	19.857	−5.365	1.00	37.24		N
ATOM	2656	CA	GLN	B	130	−3.403	19.259	−5.654	1.00	34.81		C
ATOM	2657	C	GLN	B	130	−4.093	19.947	−6.829	1.00	35.05		C
ATOM	2658	O	GLN	B	130	−4.774	19.297	−7.622	1.00	36.82		O
ATOM	2659	CB	GLN	B	130	−4.312	19.312	−4.427	1.00	32.75		C
ATOM	2660	CG	GLN	B	130	−5.631	18.597	−4.645	1.00	30.49		C
ATOM	2661	CD	GLN	B	130	−6.626	18.848	−3.534	1.00	38.30		C
ATOM	2662	NE2	GLN	B	130	−7.643	18.000	−3.456	1.00	35.08		N
ATOM	2663	OE1	GLN	B	130	−6.485	19.793	−2.754	1.00	31.99		O
ATOM	2664	N	LEU	B	131	−3.930	21.265	−6.924	1.00	34.78		N
ATOM	2665	CA	LEU	B	131	−4.512	22.036	−8.019	1.00	46.01		C
ATOM	2666	C	LEU	B	131	−4.044	21.506	−9.369	1.00	40.30		C
ATOM	2667	O	LEU	B	131	−4.800	21.497	−10.337	1.00	49.24		O
ATOM	2668	CB	LEU	B	131	−4.160	23.521	−7.884	1.00	39.51		C
ATOM	2669	CG	LEU	B	131	−4.884	24.279	−6.773	1.00	41.36		C
ATOM	2670	CD1	LEU	B	131	−4.458	25.736	−6.738	1.00	42.24		C
ATOM	2671	CD2	LEU	B	131	−6.385	24.168	−6.956	1.00	37.48		C
ATOM	2672	N	LYS	B	132	−2.798	21.048	−9.414	1.00	43.36		N
ATOM	2673	CA	LYS	B	132	−2.214	20.462	−10.616	1.00	47.83		C
ATOM	2674	C	LYS	B	132	−2.933	19.197	−11.086	1.00	46.86		C
ATOM	2675	O	LYS	B	132	−2.715	18.740	−12.206	1.00	54.52		O
ATOM	2676	CB	LYS	B	132	−0.737	20.146	−10.373	1.00	49.58		C
ATOM	2677	CG	LYS	B	132	0.229	21.216	−10.868	1.00	56.15		C
ATOM	2678	CD	LYS	B	132	1.614	21.060	−10.241	1.00	64.07		C
ATOM	2679	CE	LYS	B	132	2.009	19.593	−10.066	1.00	66.31		C
ATOM	2680	NZ	LYS	B	132	2.086	18.843	−11.352	1.00	66.61		N
ATOM	2681	N	SER	B	133	−3.776	18.626	−10.232	1.00	47.49		N
ATOM	2682	CA	SER	B	133	−4.497	17.403	−10.578	1.00	38.87		C
ATOM	2683	C	SER	B	133	−5.963	17.680	−10.922	1.00	45.85		C
ATOM	2684	O	SER	B	133	−6.718	16.757	−11.226	1.00	45.58		O
ATOM	2685	CB	SER	B	133	−4.415	16.389	−9.433	1.00	48.92		C
ATOM	2686	OG	SER	B	133	−5.127	16.848	−8.293	1.00	52.02		O
ATOM	2687	N	GLY	B	134	−6.365	18.947	−10.858	1.00	39.38		N
ATOM	2688	CA	GLY	B	134	−7.692	19.349	−11.294	1.00	38.72		C
ATOM	2689	C	GLY	B	134	−8.737	19.497	−10.202	1.00	40.64		C
ATOM	2690	O	GLY	B	134	−9.904	19.767	−10.488	1.00	47.67		O
ATOM	2691	N	THR	B	135	−8.320	19.335	−8.951	1.00	44.09		N
ATOM	2692	CA	THR	B	135	−9.239	19.382	−7.816	1.00	41.60		C
ATOM	2693	C	THR	B	135	−8.700	20.294	−6.716	1.00	38.79		C
ATOM	2694	O	THR	B	135	−7.490	20.386	−6.515	1.00	39.11		O
ATOM	2695	CB	THR	B	135	−9.485	17.965	−7.246	1.00	42.58		C
ATOM	2696	CG2	THR	B	135	−10.545	17.982	−6.153	1.00	36.34		C
ATOM	2697	OG1	THR	B	135	−9.910	17.092	−8.300	1.00	49.29		O
ATOM	2698	N	ALA	B	136	−9.599	20.979	−6.016	1.00	39.56		N
ATOM	2699	CA	ALA	B	136	−9.218	21.845	−4.907	1.00	31.14		C
ATOM	2700	C	ALA	B	136	−9.980	21.476	−3.637	1.00	41.19		C
ATOM	2701	O	ALA	B	136	−11.211	21.514	−3.609	1.00	38.90		O
ATOM	2702	CB	ALA	B	136	−9.465	23.300	−5.257	1.00	30.89		C
ATOM	2703	N	SER	B	137	−9.243	21.121	−2.588	1.00	32.83		N
ATOM	2704	CA	SER	B	137	−9.844	20.823	−1.295	1.00	29.16		C
ATOM	2705	C	SER	B	137	−9.551	21.947	−0.312	1.00	31.90		C
ATOM	2706	O	SER	B	137	−8.391	22.273	−0.060	1.00	32.52		O
ATOM	2707	CB	SER	B	137	−9.325	19.493	−0.742	1.00	31.20		C
ATOM	2708	OG	SER	B	137	−9.665	18.411	−1.588	1.00	35.83		O
ATOM	2709	N	VAL	B	138	−10.605	22.549	0.227	1.00	29.38		N
ATOM	2710	CA	VAL	B	138	−10.455	23.578	1.250	1.00	28.61		C
ATOM	2711	C	VAL	B	138	−10.856	22.986	2.596	1.00	28.33		C
ATOM	2712	O	VAL	B	138	−11.896	22.332	2.708	1.00	28.89		O
ATOM	2713	CB	VAL	B	138	−11.304	24.821	0.943	1.00	32.25		C
ATOM	2714	CG1	VAL	B	138	−10.880	25.981	1.825	1.00	32.25		C
ATOM	2715	CG2	VAL	B	138	−11.171	25.197	−0.524	1.00	34.85		C
ATOM	2716	N	VAL	B	139	−10.031	23.208	3.615	1.00	27.05		N
ATOM	2717	CA	VAL	B	139	−10.241	22.558	4.906	1.00	30.66		C
ATOM	2718	C	VAL	B	139	−10.472	23.556	6.033	1.00	28.68		C
ATOM	2719	O	VAL	B	139	−9.741	24.537	6.173	1.00	29.77		O
ATOM	2720	CB	VAL	B	139	−9.042	21.646	5.267	1.00	31.42		C
ATOM	2721	CG1	VAL	B	139	−9.199	21.067	6.665	1.00	30.03		C
ATOM	2722	CG2	VAL	B	139	−8.904	20.529	4.239	1.00	29.56		C
ATOM	2723	N	CYS	B	140	−11.507	23.300	6.826	1.00	31.41		N
ATOM	2724	CA	CYS	B	140	−11.792	24.088	8.015	1.00	30.57		C
ATOM	2725	C	CYS	B	140	−11.634	23.207	9.245	1.00	36.50		C
ATOM	2726	O	CYS	B	140	−12.198	22.113	9.306	1.00	29.35		O
ATOM	2727	CB	CYS	B	140	−13.205	24.672	7.960	1.00	32.78		C
ATOM	2728	SG	CYS	B	140	−13.561	25.937	9.212	1.00	47.42		S
ATOM	2729	N	LEU	B	141	−10.871	23.686	10.222	1.00	34.12		N
ATOM	2730	CA	LEU	B	141	−10.629	22.931	11.444	1.00	30.81		C
ATOM	2731	C	LEU	B	141	−11.230	23.619	12.672	1.00	33.78		C
ATOM	2732	O	LEU	B	141	−11.006	24.809	12.904	1.00	32.21		O
ATOM	2733	CB	LEU	B	141	−9.126	22.721	11.649	1.00	30.25		C
ATOM	2734	CG	LEU	B	141	−8.728	22.199	13.032	1.00	33.72		C
ATOM	2735	CD1	LEU	B	141	−9.143	20.737	13.205	1.00	28.38		C
ATOM	2736	CD2	LEU	B	141	−7.234	22.383	13.280	1.00	35.34		C
ATOM	2737	N	LEU	B	142	−12.006	22.862	13.442	1.00	25.85		N
ATOM	2738	CA	LEU	B	142	−12.538	23.331	14.721	1.00	29.63		C
ATOM	2739	C	LEU	B	142	−11.865	22.526	15.822	1.00	31.52		C
ATOM	2740	O	LEU	B	142	−11.966	21.300	15.848	1.00	32.17		O
ATOM	2741	CB	LEU	B	142	−14.062	23.177	14.796	1.00	28.07		C
ATOM	2742	CG	LEU	B	142	−14.992	24.140	14.044	1.00	29.90		C
ATOM	2743	CD1	LEU	B	142	−14.697	24.189	12.550	1.00	36.79		C
ATOM	2744	CD2	LEU	B	142	−16.440	23.731	14.274	1.00	27.06		C
ATOM	2745	N	ASN	B	143	−11.174	23.209	16.723	1.00	25.29		N
ATOM	2746	CA	ASN	B	143	−10.291	22.521	17.648	1.00	31.88		C
ATOM	2747	C	ASN	B	143	−10.754	22.593	19.100	1.00	34.33		C
ATOM	2748	O	ASN	B	143	−11.042	23.673	19.618	1.00	32.56		O
ATOM	2749	CB	ASN	B	143	−8.876	23.089	17.512	1.00	32.86		C
ATOM	2750	CG	ASN	B	143	−7.813	22.134	18.016	1.00	43.50		C
ATOM	2751	ND2	ASN	B	143	−7.037	22.574	18.997	1.00	47.72		N
ATOM	2752	OD1	ASN	B	143	−7.683	21.018	17.518	1.00	44.96		O
ATOM	2753	N	ASN	B	144	−10.840	21.421	19.733	1.00	33.53		N
ATOM	2754	CA	ASN	B	144	−11.100	21.284	21.171	1.00	31.24		C
ATOM	2755	C	ASN	B	144	−12.330	22.023	21.688	1.00	29.06		C
ATOM	2756	O	ASN	B	144	−12.211	22.953	22.482	1.00	33.00		O
ATOM	2757	CB	ASN	B	144	−9.873	21.743	21.962	1.00	30.14		C
ATOM	2758	CG	ASN	B	144	−8.626	20.965	21.598	1.00	37.05		C
ATOM	2759	ND2	ASN	B	144	−7.468	21.575	21.802	1.00	43.00		N
ATOM	2760	OD1	ASN	B	144	−8.704	19.827	21.134	1.00	38.36		O
ATOM	2761	N	PHE	B	145	−13.513	21.602	21.258	1.00	31.89		N
ATOM	2762	CA	PHE	B	145	−14.732	22.260	21.706	1.00	29.94		C
ATOM	2763	C	PHE	B	145	−15.672	21.295	22.416	1.00	34.88		C
ATOM	2764	O	PHE	B	145	−15.533	20.074	22.317	1.00	26.87		O
ATOM	2765	CB	PHE	B	145	−15.455	22.936	20.529	1.00	26.54		C
ATOM	2766	CG	PHE	B	145	−15.846	21.994	19.418	1.00	27.20		C
ATOM	2767	CD1	PHE	B	145	−14.961	21.705	18.392	1.00	25.82		C
ATOM	2768	CD2	PHE	B	145	−17.102	21.413	19.392	1.00	29.78		C
ATOM	2769	CE1	PHE	B	145	−15.316	20.839	17.368	1.00	27.58		C
ATOM	2770	CE2	PHE	B	145	−17.467	20.551	18.372	1.00	29.41		C
ATOM	2771	CZ	PHE	B	145	−16.569	20.263	17.356	1.00	27.09		C
ATOM	2772	N	TYR	B	146	−16.619	21.871	23.149	1.00	28.10		N
ATOM	2773	CA	TYR	B	146	−17.698	21.125	23.778	1.00	30.54		C
ATOM	2774	C	TYR	B	146	−18.886	22.071	23.962	1.00	29.20		C
ATOM	2775	O	TYR	B	146	−18.702	23.217	24.364	1.00	28.71		O
ATOM	2776	CB	TYR	B	146	−17.262	20.527	25.128	1.00	31.96		C
ATOM	2777	CG	TYR	B	146	−18.319	19.621	25.711	1.00	34.78		C
ATOM	2778	CD2	TYR	B	146	−18.334	18.262	25.418	1.00	31.97		C
ATOM	2779	CD1	TYR	B	146	−19.334	20.131	26.515	1.00	31.84		C
ATOM	2780	CE2	TYR	B	146	−19.319	17.432	25.925	1.00	32.92		C
ATOM	2781	CE1	TYR	B	146	−20.324	19.311	27.022	1.00	32.17		C
ATOM	2782	CZ	TYR	B	146	−20.310	17.965	26.725	1.00	34.30		C
ATOM	2783	OH	TYR	B	146	−21.291	17.149	27.228	1.00	42.60		O
ATOM	2784	N	PRO	B	147	−20.112	21.593	23.695	1.00	25.21		N
ATOM	2785	CA	PRO	B	147	−20.474	20.225	23.311	1.00	31.43		C
ATOM	2786	C	PRO	B	147	−20.233	19.921	21.838	1.00	34.10		C
ATOM	2787	O	PRO	B	147	−19.696	20.751	21.103	1.00	33.70		O
ATOM	2788	CB	PRO	B	147	−21.967	20.159	23.643	1.00	32.07		C
ATOM	2789	CG	PRO	B	147	−22.446	21.552	23.429	1.00	27.75		C
ATOM	2790	CD	PRO	B	147	−21.301	22.453	23.836	1.00	31.95		C
ATOM	2791	N	ARG	B	148	−20.646	18.725	21.434	1.00	34.40		N
ATOM	2792	CA	ARG	B	148	−20.383	18.168	20.110	1.00	32.34		C
ATOM	2793	C	ARG	B	148	−21.069	18.932	18.975	1.00	32.84		C
ATOM	2794	O	ARG	B	148	−20.505	19.087	17.892	1.00	29.63		O
ATOM	2795	CB	ARG	B	148	−20.823	16.700	20.101	1.00	35.79		C
ATOM	2796	CG	ARG	B	148	−20.923	16.051	18.744	1.00	41.03		C
ATOM	2797	CD	ARG	B	148	−19.703	15.208	18.453	1.00	47.90		C
ATOM	2798	NE	ARG	B	148	−20.044	13.980	17.738	1.00	56.46		N
ATOM	2799	CZ	ARG	B	148	−20.405	13.932	16.458	1.00	56.76		C
ATOM	2800	NH1	ARG	B	148	−20.485	15.048	15.740	1.00	54.31		N
ATOM	2801	NH2	ARG	B	148	−20.688	12.767	15.893	1.00	51.59		N
ATOM	2802	N	GLU	B	149	−22.284	19.404	19.230	1.00	36.40		N
ATOM	2803	CA	GLU	B	149	−23.068	20.115	18.224	1.00	39.72		C
ATOM	2804	C	GLU	B	149	−22.387	21.403	17.779	1.00	39.89		C
ATOM	2805	O	GLU	B	149	−22.182	22.319	18.577	1.00	39.53		O
ATOM	2806	CB	GLU	B	149	−24.473	20.431	18.755	1.00	34.93		C
ATOM	2807	CG	GLU	B	149	−25.369	19.209	18.956	1.00	45.72		C
ATOM	2808	CD	GLU	B	149	−24.967	18.363	20.158	1.00	54.80		C
ATOM	2809	OE1	GLU	B	149	−24.402	18.920	21.125	1.00	48.46		O
ATOM	2810	OE2	GLU	B	149	−25.211	17.138	20.130	1.00	62.82		O
ATOM	2811	N	ALA	B	150	−22.042	21.462	16.498	1.00	35.98		N
ATOM	2812	CA	ALA	B	150	−21.432	22.649	15.914	1.00	37.14		C
ATOM	2813	C	ALA	B	150	−21.867	22.779	14.465	1.00	43.97		C
ATOM	2814	O	ALA	B	150	−22.094	21.778	13.786	1.00	46.01		O
ATOM	2815	CB	ALA	B	150	−19.914	22.586	16.014	1.00	32.49		C
ATOM	2816	N	LYS	B	151	−21.987	24.012	13.992	1.00	39.41		N
ATOM	2817	CA	LYS	B	151	−22.417	24.246	12.624	1.00	43.48		C
ATOM	2818	C	LYS	B	151	−21.319	24.913	11.807	1.00	39.53		C
ATOM	2819	O	LYS	B	151	−20.799	25.966	12.179	1.00	36.87		O
ATOM	2820	CB	LYS	B	151	−23.687	25.099	12.596	1.00	43.88		C
ATOM	2821	CG	LYS	B	151	−24.256	25.301	11.196	1.00	55.40		C
ATOM	2822	CD	LYS	B	151	−25.547	26.104	11.223	1.00	53.19		C
ATOM	2823	CE	LYS	B	151	−26.147	26.222	9.830	1.00	70.97		C
ATOM	2824	NZ	LYS	B	151	−27.463	26.923	9.839	1.00	84.38		N
ATOM	2825	N	VAL	B	152	−20.968	24.282	10.694	1.00	36.81		N
ATOM	2826	CA	VAL	B	152	−19.990	24.837	9.774	1.00	37.97		C
ATOM	2827	C	VAL	B	152	−20.652	25.168	8.446	1.00	36.38		C
ATOM	2828	O	VAL	B	152	−21.221	24.292	7.790	1.00	36.25		O
ATOM	2829	CB	VAL	B	152	−18.820	23.867	9.535	1.00	39.90		C
ATOM	2830	CG1	VAL	B	152	−17.884	24.420	8.470	1.00	35.36		C
ATOM	2831	CG2	VAL	B	152	−18.078	23.614	10.834	1.00	39.55		C
ATOM	2832	N	GLN	B	153	−20.590	26.437	8.060	1.00	32.64		N
ATOM	2833	CA	GLN	B	153	−21.118	26.864	6.771	1.00	34.66		C
ATOM	2834	C	GLN	B	153	−19.999	27.378	5.884	1.00	38.08		C
ATOM	2835	O	GLN	B	153	−19.290	28.319	6.244	1.00	38.02		O
ATOM	2836	CB	GLN	B	153	−22.187	27.946	6.946	1.00	37.83		C
ATOM	2837	CG	GLN	B	153	−23.590	27.404	7.164	1.00	60.26		C
ATOM	2838	CD	GLN	B	153	−24.596	28.498	7.470	1.00	67.71		C
ATOM	2839	NE2	GLN	B	153	−25.857	28.257	7.123	1.00	56.86		N
ATOM	2840	OE1	GLN	B	153	−24.244	29.548	8.009	1.00	70.19		O
ATOM	2841	N	TRP	B	154	−19.840	26.747	4.727	1.00	31.58		N
ATOM	2842	CA	TRP	B	154	−18.864	27.189	3.747	1.00	27.44		C
ATOM	2843	C	TRP	B	154	−19.449	28.300	2.884	1.00	33.80		C
ATOM	2844	O	TRP	B	154	−20.592	28.209	2.436	1.00	30.68		O
ATOM	2845	CB	TRP	B	154	−18.415	26.022	2.869	1.00	25.14		C
ATOM	2846	CG	TRP	B	154	−17.449	25.089	3.532	1.00	34.77		C
ATOM	2847	CD1	TRP	B	154	−17.729	23.870	4.080	1.00	29.48		C
ATOM	2848	CD2	TRP	B	154	−16.042	25.295	3.709	1.00	33.52		C
ATOM	2849	CE2	TRP	B	154	−15.534	24.159	4.369	1.00	36.13		C
ATOM	2850	CE3	TRP	B	154	−15.163	26.328	3.370	1.00	28.50		C
ATOM	2851	NE1	TRP	B	154	−16.584	23.304	4.582	1.00	32.42		N
ATOM	2852	CZ2	TRP	B	154	−14.186	24.028	4.697	1.00	35.02		C
ATOM	2853	CZ3	TRP	B	154	−13.827	26.199	3.699	1.00	32.42		C
ATOM	2854	CH2	TRP	B	154	−13.350	25.056	4.355	1.00	33.88		C
ATOM	2855	N	LYS	B	155	−18.661	29.343	2.652	1.00	26.76		N
ATOM	2856	CA	LYS	B	155	−19.089	30.458	1.818	1.00	34.70		C
ATOM	2857	C	LYS	B	155	−18.018	30.803	0.795	1.00	35.14		C
ATOM	2858	O	LYS	B	155	−16.869	31.063	1.149	1.00	34.32		O
ATOM	2859	CB	LYS	B	155	−19.415	31.685	2.671	1.00	31.08		C
ATOM	2860	CG	LYS	B	155	−20.658	31.527	3.525	1.00	39.61		C
ATOM	2861	CD	LYS	B	155	−20.861	32.722	4.439	1.00	45.78		C
ATOM	2862	CE	LYS	B	155	−22.086	32.531	5.322	1.00	52.43		C
ATOM	2863	NZ	LYS	B	155	−22.240	33.644	6.300	1.00	64.93		N
ATOM	2864	N	VAL	B	156	−18.404	30.787	−0.474	1.00	33.51		N
ATOM	2865	CA	VAL	B	156	−17.512	31.163	−1.562	1.00	34.85		C
ATOM	2866	C	VAL	B	156	−18.043	32.430	−2.235	1.00	37.05		C
ATOM	2867	O	VAL	B	156	−19.085	32.398	−2.889	1.00	36.43		O
ATOM	2868	CB	VAL	B	156	−17.378	30.035	−2.590	1.00	37.60		C
ATOM	2869	CG1	VAL	B	156	−16.452	30.450	−3.701	1.00	36.02		C
ATOM	2870	CG2	VAL	B	156	−16.863	28.772	−1.921	1.00	31.56		C
ATOM	2871	N	ASP	B	157	−17.321	33.536	−2.060	1.00	38.87		N
ATOM	2872	CA	ASP	B	157	−17.785	34.866	−2.468	1.00	41.38		C
ATOM	2873	C	ASP	B	157	−19.196	35.139	−1.951	1.00	44.37		C
ATOM	2874	O	ASP	B	157	−20.058	35.627	−2.684	1.00	49.49		O
ATOM	2875	CB	ASP	B	157	−17.733	35.023	−3.991	1.00	42.34		C
ATOM	2876	CG	ASP	B	157	−16.326	35.296	−4.499	1.00	44.58		C
ATOM	2877	OD1	ASP	B	157	−15.517	35.866	−3.734	1.00	49.40		O
ATOM	2878	OD2	ASP	B	157	−16.029	34.942	−5.659	1.00	49.33		O
ATOM	2879	N	ASN	B	158	−19.405	34.809	−0.678	1.00	38.79		N
ATOM	2880	CA	ASN	B	158	−20.688	34.958	0.016	1.00	46.07		C
ATOM	2881	C	ASN	B	158	−21.827	34.101	−0.535	1.00	42.73		C
ATOM	2882	O	ASN	B	158	−22.992	34.335	−0.218	1.00	49.48		O
ATOM	2883	CB	ASN	B	158	−21.115	36.426	0.033	1.00	47.14		C
ATOM	2884	CG	ASN	B	158	−20.716	37.122	1.313	1.00	64.92		C
ATOM	2885	ND2	ASN	B	158	−20.238	38.356	1.196	1.00	70.04		N
ATOM	2886	OD1	ASN	B	158	−20.825	36.549	2.400	1.00	67.22		O
ATOM	2887	N	ALA	B	159	−21.497	33.100	−1.341	1.00	37.66		N
ATOM	2888	CA	ALA	B	159	−22.492	32.110	−1.731	1.00	37.19		C
ATOM	2889	C	ALA	B	159	−22.368	30.887	−0.823	1.00	39.41		C
ATOM	2890	O	ALA	B	159	−21.298	30.285	−0.720	1.00	32.50		O
ATOM	2891	CB	ALA	B	159	−22.330	31.717	−3.191	1.00	30.09		C
ATOM	2892	N	LEU	B	160	−23.464	30.537	−0.159	1.00	34.32		N
ATOM	2893	CA	LEU	B	160	−23.496	29.376	0.720	1.00	29.40		C
ATOM	2894	C	LEU	B	160	−23.360	28.083	−0.073	1.00	33.09		C
ATOM	2895	O	LEU	B	160	−24.083	27.858	−1.044	1.00	36.96		O
ATOM	2896	CB	LEU	B	160	−24.790	29.348	1.540	1.00	37.86		C
ATOM	2897	CG	LEU	B	160	−24.960	30.336	2.701	1.00	54.68		C
ATOM	2898	CD1	LEU	B	160	−25.190	31.767	2.222	1.00	48.85		C
ATOM	2899	CD2	LEU	B	160	−26.100	29.883	3.608	1.00	60.01		C
ATOM	2900	N	GLN	B	161	−22.427	27.238	0.347	1.00	30.58		N
ATOM	2901	CA	GLN	B	161	−22.206	25.943	−0.284	1.00	30.22		C
ATOM	2902	C	GLN	B	161	−22.919	24.850	0.499	1.00	35.29		C
ATOM	2903	O	GLN	B	161	−22.868	24.821	1.727	1.00	38.99		O
ATOM	2904	CB	GLN	B	161	−20.710	25.633	−0.371	1.00	31.23		C
ATOM	2905	CG	GLN	B	161	−19.880	26.761	−0.958	1.00	30.86		C
ATOM	2906	CD	GLN	B	161	−20.221	27.015	−2.407	1.00	32.74		C
ATOM	2907	NE2	GLN	B	161	−20.715	28.210	−2.698	1.00	30.42		N
ATOM	2908	OE1	GLN	B	161	−20.062	26.138	−3.252	1.00	34.09		O
ATOM	2909	N	SER	B	162	−23.588	23.955	−0.215	1.00	27.98		N
ATOM	2910	CA	SER	B	162	−24.234	22.815	0.416	1.00	38.77		C
ATOM	2911	C	SER	B	162	−24.111	21.602	−0.496	1.00	34.56		C
ATOM	2912	O	SER	B	162	−24.271	21.717	−1.713	1.00	33.35		O
ATOM	2913	CB	SER	B	162	−25.703	23.126	0.723	1.00	31.67		C
ATOM	2914	OG	SER	B	162	−26.329	22.040	1.385	1.00	49.66		O
ATOM	2915	N	GLY	B	163	−23.800	20.449	0.090	1.00	33.25		N
ATOM	2916	CA	GLY	B	163	−23.739	19.206	−0.661	1.00	28.14		C
ATOM	2917	C	GLY	B	163	−22.356	18.880	−1.192	1.00	32.51		C
ATOM	2918	O	GLY	B	163	−22.101	17.758	−1.620	1.00	33.73		O
ATOM	2919	N	ASN	B	164	−21.457	19.859	−1.164	1.00	30.22		N
ATOM	2920	CA	ASN	B	164	−20.114	19.664	−1.694	1.00	31.34		C
ATOM	2921	C	ASN	B	164	−19.043	19.693	−0.605	1.00	35.48		C
ATOM	2922	O	ASN	B	164	−17.881	19.990	−0.876	1.00	31.32		O
ATOM	2923	CB	ASN	B	164	−19.809	20.722	−2.767	1.00	30.74		C
ATOM	2924	CG	ASN	B	164	−19.951	22.147	−2.248	1.00	33.60		C
ATOM	2925	ND2	ASN	B	164	−19.572	23.116	−3.073	1.00	33.79		N
ATOM	2926	OD1	ASN	B	164	−20.405	22.374	−1.127	1.00	32.68		O
ATOM	2927	N	SER	B	165	−19.435	19.387	0.628	1.00	35.40		N
ATOM	2928	CA	SER	B	165	−18.470	19.275	1.714	1.00	35.79		C
ATOM	2929	C	SER	B	165	−18.750	18.042	2.561	1.00	32.53		C
ATOM	2930	O	SER	B	165	−19.849	17.490	2.521	1.00	29.82		O
ATOM	2931	CB	SER	B	165	−18.478	20.530	2.593	1.00	32.78		C
ATOM	2932	OG	SER	B	165	−19.639	20.592	3.401	1.00	33.05		O
ATOM	2933	N	GLN	B	166	−17.742	17.606	3.311	1.00	30.86		N
ATOM	2934	CA	GLN	B	166	−17.896	16.486	4.236	1.00	32.40		C
ATOM	2935	C	GLN	B	166	−17.194	16.792	5.553	1.00	32.23		C
ATOM	2936	O	GLN	B	166	−16.181	17.493	5.575	1.00	33.90		O
ATOM	2937	CB	GLN	B	166	−17.346	15.189	3.634	1.00	26.55		C
ATOM	2938	CG	GLN	B	166	−18.110	14.694	2.418	1.00	37.55		C
ATOM	2939	CD	GLN	B	166	−17.656	13.318	1.960	1.00	45.88		C
ATOM	2940	NE2	GLN	B	166	−16.458	13.247	1.393	1.00	37.75		N
ATOM	2941	OE1	GLN	B	166	−18.378	12.332	2.110	1.00	44.50		O
ATOM	2942	N	GLU	B	167	−17.741	16.260	6.642	1.00	26.95		N
ATOM	2943	CA	GLU	B	167	−17.217	16.491	7.985	1.00	34.35		C
ATOM	2944	C	GLU	B	167	−16.789	15.199	8.666	1.00	31.65		C
ATOM	2945	O	GLU	B	167	−17.351	14.136	8.416	1.00	31.31		O
ATOM	2946	CB	GLU	B	167	−18.263	17.166	8.868	1.00	33.65		C
ATOM	2947	CG	GLU	B	167	−18.526	18.617	8.585	1.00	50.67		C
ATOM	2948	CD	GLU	B	167	−19.553	19.191	9.544	1.00	59.29		C
ATOM	2949	OE1	GLU	B	167	−20.018	18.431	10.425	1.00	49.27		O
ATOM	2950	OE2	GLU	B	167	−19.895	20.388	9.418	1.00	59.18		O
ATOM	2951	N	SER	B	168	−15.815	15.317	9.556	1.00	28.62		N
ATOM	2952	CA	SER	B	168	−15.393	14.216	10.407	1.00	32.03		C
ATOM	2953	C	SER	B	168	−15.096	14.753	11.802	1.00	31.07		C
ATOM	2954	O	SER	B	168	−14.499	15.819	11.945	1.00	28.49		O
ATOM	2955	CB	SER	B	168	−14.165	13.522	9.817	1.00	34.82		C
ATOM	2956	OG	SER	B	168	−13.566	12.666	10.762	1.00	40.29		O
ATOM	2957	N	AVAL	B	169	−15.514	14.013	12.828	0.89	30.56		N
ATOM	2958	CA	AVAL	B	169	−15.342	14.433	14.221	0.89	30.43		C
ATOM	2959	C	AVAL	B	169	−14.558	13.389	15.017	0.89	31.75		C
ATOM	2960	O	AVAL	B	169	−14.796	12.193	14.870	0.89	33.51		O
ATOM	2961	CB	AVAL	B	169	−16.708	14.663	14.910	0.89	32.02		C
ATOM	2962	CG1	AVAL	B	169	−16.518	15.215	16.317	0.89	33.65		C
ATOM	2963	CG2	AVAL	B	169	−17.578	15.591	14.079	0.89	31.73		C
ATOM	2964	N	BVAL	B	169	−15.523	14.018	12.822	0.11	30.45		N
ATOM	2965	CA	BVAL	B	169	−15.292	14.424	14.200	0.11	31.12		C
ATOM	2966	C	BVAL	B	169	−14.467	13.380	14.937	0.11	31.77		C
ATOM	2967	O	BVAL	B	169	−14.578	12.184	14.669	0.11	33.10		O
ATOM	2968	CB	BVAL	B	169	−16.616	14.648	14.953	0.11	32.66		C
ATOM	2969	CG1	BVAL	B	169	−17.352	15.847	14.385	0.11	32.73		C
ATOM	2970	CG2	BVAL	B	169	−17.482	13.403	14.878	0.11	33.85		C
ATOM	2971	N	THR	B	170	−13.633	13.837	15.862	1.00	29.38		N
ATOM	2972	CA	THR	B	170	−12.847	12.921	16.682	1.00	36.76		C
ATOM	2973	C	THR	B	170	−13.703	12.346	17.805	1.00	33.01		C
ATOM	2974	O	THR	B	170	−14.762	12.885	18.133	1.00	30.78		O
ATOM	2975	CB	THR	B	170	−11.620	13.605	17.308	1.00	30.27		C
ATOM	2976	CG2	THR	B	170	−10.719	14.211	16.235	1.00	34.58		C
ATOM	2977	OG1	THR	B	170	−12.057	14.633	18.199	1.00	31.73		O
ATOM	2978	N	GLU	B	171	−13.243	11.248	18.390	1.00	34.68		N
ATOM	2979	CA	GLU	B	171	−13.843	10.746	19.618	1.00	35.38		C
ATOM	2980	C	GLU	B	171	−13.613	11.768	20.720	1.00	37.95		C
ATOM	2981	O	GLU	B	171	−12.689	12.584	20.639	1.00	34.11		O
ATOM	2982	CB	GLU	B	171	−13.247	9.391	20.011	1.00	35.96		C
ATOM	2983	CG	GLU	B	171	−13.457	8.290	18.984	1.00	47.50		C
ATOM	2984	CD	GLU	B	171	−14.850	7.683	19.038	1.00	65.62		C
ATOM	2985	OE1	GLU	B	171	−15.595	7.969	20.002	1.00	65.84		O
ATOM	2986	OE2	GLU	B	171	−15.198	6.912	18.116	1.00	70.74		O
ATOM	2987	N	GLN	B	172	−14.456	11.734	21.743	1.00	34.37		N
ATOM	2988	CA	GLN	B	172	−14.272	12.609	22.885	1.00	27.96		C
ATOM	2989	C	GLN	B	172	−12.897	12.347	23.509	1.00	29.48		C
ATOM	2990	O	GLN	B	172	−12.544	11.210	23.785	1.00	33.27		O
ATOM	2991	CB	GLN	B	172	−15.399	12.399	23.899	1.00	31.65		C
ATOM	2992	CG	GLN	B	172	−15.483	13.474	24.959	1.00	34.27		C
ATOM	2993	CD	GLN	B	172	−16.804	13.457	25.706	1.00	37.13		C
ATOM	2994	NE2	GLN	B	172	−17.166	14.594	26.286	1.00	32.91		N
ATOM	2995	OE1	GLN	B	172	−17.496	12.437	25.755	1.00	34.99		O
ATOM	2996	N	ASP	B	173	−12.120	13.408	23.700	1.00	30.64		N
ATOM	2997	CA	ASP	B	173	−10.766	13.296	24.231	1.00	32.58		C
ATOM	2998	C	ASP	B	173	−10.749	12.684	25.636	1.00	36.32		C
ATOM	2999	O	ASP	B	173	−11.537	13.069	26.502	1.00	30.09		O
ATOM	3000	CB	ASP	B	173	−10.097	14.671	24.246	1.00	32.10		C
ATOM	3001	CG	ASP	B	173	−8.613	14.593	24.538	1.00	36.21		C
ATOM	3002	OD2	ASP	B	173	−8.222	14.802	25.708	1.00	36.85		O
ATOM	3003	OD1	ASP	B	173	−7.836	14.324	23.595	1.00	37.22		O
ATOM	3004	N	SER	B	174	−9.844	11.737	25.863	1.00	32.20		N
ATOM	3005	CA	SER	B	174	−9.818	11.015	27.134	1.00	38.98		C
ATOM	3006	C	SER	B	174	−9.243	11.855	28.275	1.00	32.61		C
ATOM	3007	O	SER	B	174	−9.301	11.447	29.432	1.00	42.30		O
ATOM	3008	CB	SER	B	174	−9.017	9.717	26.998	1.00	36.54		C
ATOM	3009	OG	SER	B	174	−7.630	9.986	26.883	1.00	46.81		O
ATOM	3010	N	LYS	B	175	−8.691	13.020	27.954	1.00	35.47		N
ATOM	3011	CA	LYS	B	175	−8.142	13.907	28.981	1.00	33.77		C
ATOM	3012	C	LYS	B	175	−9.040	15.113	29.278	1.00	36.43		C
ATOM	3013	O	LYS	B	175	−9.479	15.287	30.410	1.00	30.79		O
ATOM	3014	CB	LYS	B	175	−6.749	14.404	28.581	1.00	36.54		C
ATOM	3015	CG	LYS	B	175	−5.717	13.303	28.387	1.00	47.29		C
ATOM	3016	CD	LYS	B	175	−4.339	13.895	28.117	1.00	54.56		C
ATOM	3017	CE	LYS	B	175	−3.317	12.811	27.821	1.00	53.35		C
ATOM	3018	NZ	LYS	B	175	−1.931	13.358	27.809	1.00	53.83		N
ATOM	3019	N	ASP	B	176	−9.306	15.950	28.275	1.00	35.92		N
ATOM	3020	CA	ASP	B	176	−10.070	17.176	28.522	1.00	33.42		C
ATOM	3021	C	ASP	B	176	−11.526	17.072	28.069	1.00	33.69		C
ATOM	3022	O	ASP	B	176	−12.293	18.025	28.205	1.00	32.10		O
ATOM	3023	CB	ASP	B	176	−9.391	18.387	27.857	1.00	37.93		C
ATOM	3024	CG	ASP	B	176	−9.374	18.315	26.326	1.00	44.81		C
ATOM	3025	OD1	ASP	B	176	−10.135	17.530	25.718	1.00	39.09		O
ATOM	3026	OD2	ASP	B	176	−8.591	19.081	25.721	1.00	49.31		O
ATOM	3027	N	SER	B	177	−11.879	15.923	27.501	1.00	31.41		N
ATOM	3028	CA	SER	B	177	−13.259	15.601	27.145	1.00	32.38		C
ATOM	3029	C	SER	B	177	−13.869	16.487	26.062	1.00	31.53		C
ATOM	3030	O	SER	B	177	−15.087	16.651	26.017	1.00	29.23		O
ATOM	3031	CB	SER	B	177	−14.142	15.665	28.390	1.00	29.13		C
ATOM	3032	OG	SER	B	177	−13.689	14.767	29.386	1.00	32.14		O
ATOM	3033	N	THR	B	178	−13.031	17.045	25.192	1.00	32.85		N
ATOM	3034	CA	THR	B	178	−13.521	17.873	24.091	1.00	31.34		C
ATOM	3035	C	THR	B	178	−13.603	17.102	22.779	1.00	29.53		C
ATOM	3036	O	THR	B	178	−13.145	15.960	22.680	1.00	31.68		O
ATOM	3037	CB	THR	B	178	−12.627	19.108	23.865	1.00	30.04		C
ATOM	3038	CG2	THR	B	178	−12.576	19.979	25.117	1.00	31.87		C
ATOM	3039	OG1	THR	B	178	−11.302	18.683	23.526	1.00	33.96		O
ATOM	3040	N	TYR	B	179	−14.199	17.738	21.776	1.00	26.97		N
ATOM	3041	CA	TYR	B	179	−14.198	17.225	20.411	1.00	27.62		C
ATOM	3042	C	TYR	B	179	−13.395	18.139	19.503	1.00	28.49		C
ATOM	3043	O	TYR	B	179	−13.193	19.316	19.809	1.00	27.60		O
ATOM	3044	CB	TYR	B	179	−15.620	17.110	19.862	1.00	23.93		C
ATOM	3045	CG	TYR	B	179	−16.540	16.224	20.659	1.00	32.03		C
ATOM	3046	CD2	TYR	B	179	−16.701	14.884	20.326	1.00	29.16		C
ATOM	3047	CD1	TYR	B	179	−17.266	16.729	21.735	1.00	27.55		C
ATOM	3048	CE2	TYR	B	179	−17.549	14.065	21.046	1.00	36.83		C
ATOM	3049	CE1	TYR	B	179	−18.118	15.915	22.467	1.00	35.32		C
ATOM	3050	CZ	TYR	B	179	−18.254	14.584	22.118	1.00	36.45		C
ATOM	3051	OH	TYR	B	179	−19.096	13.768	22.837	1.00	41.00		O
ATOM	3052	N	SER	B	180	−12.945	17.597	18.379	1.00	27.52		N
ATOM	3053	CA	SER	B	180	−12.437	18.418	17.288	1.00	29.79		C
ATOM	3054	C	SER	B	180	−13.143	18.002	16.000	1.00	28.83		C
ATOM	3055	O	SER	B	180	−13.591	16.862	15.875	1.00	26.78		O
ATOM	3056	CB	SER	B	180	−10.921	18.287	17.150	1.00	34.04		C
ATOM	3057	OG	SER	B	180	−10.255	18.889	18.246	1.00	36.05		O
ATOM	3058	N	LEU	B	181	−13.252	18.928	15.053	1.00	27.50		N
ATOM	3059	CA	LEU	B	181	−13.984	18.670	13.819	1.00	29.24		C
ATOM	3060	C	LEU	B	181	−13.206	19.150	12.595	1.00	34.49		C
ATOM	3061	O	LEU	B	181	−12.583	20.214	12.610	1.00	29.64		O
ATOM	3062	CB	LEU	B	181	−15.367	19.337	13.866	1.00	31.76		C
ATOM	3063	CG	LEU	B	181	−16.315	19.197	12.662	1.00	33.92		C
ATOM	3064	CD1	LEU	B	181	−17.770	19.237	13.115	1.00	33.67		C
ATOM	3065	CD2	LEU	B	181	−16.071	20.275	11.620	1.00	27.36		C
ATOM	3066	N	SER	B	182	−13.266	18.355	11.534	1.00	30.45		N
ATOM	3067	CA	SER	B	182	−12.622	18.683	10.273	1.00	32.39		C
ATOM	3068	C	SER	B	182	−13.653	18.706	9.157	1.00	34.50		C
ATOM	3069	O	SER	B	182	−14.346	17.715	8.935	1.00	32.11		O
ATOM	3070	CB	SER	B	182	−11.521	17.671	9.953	1.00	35.13		C
ATOM	3071	OG	SER	B	182	−10.952	17.929	8.684	1.00	35.29		O
ATOM	3072	N	SER	B	183	−13.769	19.841	8.473	1.00	32.48		N
ATOM	3073	CA	SER	B	183	−14.666	19.946	7.327	1.00	31.00		C
ATOM	3074	C	SER	B	183	−13.877	20.240	6.058	1.00	37.54		C
ATOM	3075	O	SER	B	183	−13.014	21.119	6.041	1.00	34.24		O
ATOM	3076	CB	SER	B	183	−15.720	21.028	7.548	1.00	28.88		C
ATOM	3077	OG	SER	B	183	−16.568	21.127	6.415	1.00	34.00		O
ATOM	3078	N	THR	B	184	−14.185	19.495	5.002	1.00	29.33		N
ATOM	3079	CA	THR	B	184	−13.490	19.618	3.733	1.00	32.43		C
ATOM	3080	C	THR	B	184	−14.449	20.002	2.609	1.00	33.53		C
ATOM	3081	O	THR	B	184	−15.375	19.258	2.296	1.00	30.24		O
ATOM	3082	CB	THR	B	184	−12.778	18.303	3.347	1.00	30.27		C
ATOM	3083	CG2	THR	B	184	−12.075	18.448	1.993	1.00	34.53		C
ATOM	3084	OG1	THR	B	184	−11.813	17.966	4.348	1.00	43.02		O
ATOM	3085	N	LEU	B	185	−14.212	21.164	2.013	1.00	29.43		N
ATOM	3086	CA	LEU	B	185	−14.950	21.610	0.838	1.00	26.42		C
ATOM	3087	C	LEU	B	185	−14.195	21.216	−0.428	1.00	31.67		C
ATOM	3088	O	LEU	B	185	−13.021	21.549	−0.587	1.00	32.58		O
ATOM	3089	CB	LEU	B	185	−15.162	23.123	0.882	1.00	26.19		C
ATOM	3090	CG	LEU	B	185	−15.801	23.777	−0.346	1.00	33.72		C
ATOM	3091	CD1	LEU	B	185	−17.290	23.451	−0.426	1.00	29.32		C
ATOM	3092	CD2	LEU	B	185	−15.570	25.285	−0.336	1.00	29.64		C
ATOM	3093	N	THR	B	186	−14.862	20.503	−1.330	1.00	27.07		N
ATOM	3094	CA	THR	B	186	−14.200	20.043	−2.544	1.00	32.13		C
ATOM	3095	C	THR	B	186	−14.797	20.676	−3.794	1.00	34.19		C
ATOM	3096	O	THR	B	186	−15.999	20.569	−4.046	1.00	32.51		O
ATOM	3097	CB	THR	B	186	−14.265	18.512	−2.672	1.00	35.70		C
ATOM	3098	CG2	THR	B	186	−13.532	18.054	−3.919	1.00	33.31		C
ATOM	3099	OG1	THR	B	186	−13.652	17.913	−1.522	1.00	40.62		O
ATOM	3100	N	LEU	B	187	−13.941	21.346	−4.562	1.00	35.11		N
ATOM	3101	CA	LEU	B	187	−14.315	21.945	−5.843	1.00	35.77		C
ATOM	3102	C	LEU	B	187	−13.339	21.525	−6.932	1.00	37.88		C
ATOM	3103	O	LEU	B	187	−12.206	21.145	−6.642	1.00	36.56		O
ATOM	3104	CB	LEU	B	187	−14.333	23.471	−5.755	1.00	30.60		C
ATOM	3105	CG	LEU	B	187	−15.286	24.143	−4.775	1.00	36.33		C
ATOM	3106	CD1	LEU	B	187	−15.031	25.641	−4.767	1.00	43.76		C
ATOM	3107	CD2	LEU	B	187	−16.729	23.835	−5.147	1.00	50.34		C
ATOM	3108	N	SER	B	188	−13.767	21.609	−8.187	1.00	38.12		N
ATOM	3109	CA	SER	B	188	−12.839	21.434	−9.297	1.00	37.37		C
ATOM	3110	C	SER	B	188	−11.888	22.627	−9.343	1.00	37.79		C
ATOM	3111	O	SER	B	188	−12.169	23.681	−8.761	1.00	33.69		O
ATOM	3112	CB	SER	B	188	−13.584	21.297	−10.625	1.00	36.22		C
ATOM	3113	OG	SER	B	188	−14.208	22.519	−10.973	1.00	39.78		O
ATOM	3114	N	LYS	B	189	−10.765	22.460	−10.031	1.00	38.51		N
ATOM	3115	CA	LYS	B	189	−9.809	23.546	−10.193	1.00	37.38		C
ATOM	3116	C	LYS	B	189	−10.460	24.721	−10.915	1.00	37.61		C
ATOM	3117	O	LYS	B	189	−10.331	25.869	−10.491	1.00	42.81		O
ATOM	3118	CB	LYS	B	189	−8.576	23.064	−10.959	1.00	43.42		C
ATOM	3119	CG	LYS	B	189	−7.574	24.158	−11.293	1.00	46.58		C
ATOM	3120	CD	LYS	B	189	−6.453	23.615	−12.166	1.00	47.94		C
ATOM	3121	CE	LYS	B	189	−5.477	24.704	−12.561	1.00	50.50		C
ATOM	3122	NZ	LYS	B	189	−4.369	24.160	−13.395	1.00	67.88		N
ATOM	3123	N	ALA	B	190	−11.175	24.415	−11.995	1.00	37.86		N
ATOM	3124	CA	ALA	B	190	−11.862	25.429	−12.791	1.00	38.31		C
ATOM	3125	C	ALA	B	190	−12.825	26.252	−11.947	1.00	41.13		C
ATOM	3126	O	ALA	B	190	−12.859	27.477	−12.057	1.00	45.90		O
ATOM	3127	CB	ALA	B	190	−12.602	24.777	−13.953	1.00	30.47		C
ATOM	3128	N	ASP	B	191	−13.602	25.582	−11.100	1.00	38.92		N
ATOM	3129	CA	ASP	B	191	−14.536	26.287	−10.226	1.00	37.31		C
ATOM	3130	C	ASP	B	191	−13.796	27.103	−9.175	1.00	35.97		C
ATOM	3131	O	ASP	B	191	−14.211	28.214	−8.831	1.00	35.16		O
ATOM	3132	CB	ASP	B	191	−15.497	25.308	−9.542	1.00	40.65		C
ATOM	3133	CG	ASP	B	191	−16.675	24.932	−10.425	1.00	54.48		C
ATOM	3134	OD1	ASP	B	191	−16.840	25.554	−11.498	1.00	48.85		O
ATOM	3135	OD2	ASP	B	191	−17.445	24.024	−10.039	1.00	50.23		O
ATOM	3136	N	TYR	B	192	−12.700	26.549	−8.667	1.00	35.50		N
ATOM	3137	CA	TYR	B	192	−11.948	27.193	−7.595	1.00	34.33		C
ATOM	3138	C	TYR	B	192	−11.381	28.543	−8.022	1.00	37.59		C
ATOM	3139	O	TYR	B	192	−11.395	29.505	−7.256	1.00	35.83		O
ATOM	3140	CB	TYR	B	192	−10.814	26.288	−7.115	1.00	34.12		C
ATOM	3141	CG	TYR	B	192	−9.932	26.940	−6.076	1.00	36.45		C
ATOM	3142	CD1	TYR	B	192	−10.429	27.251	−4.815	1.00	34.80		C
ATOM	3143	CD2	TYR	B	192	−8.606	27.243	−6.350	1.00	32.17		C
ATOM	3144	CE1	TYR	B	192	−9.632	27.849	−3.857	1.00	32.72		C
ATOM	3145	CE2	TYR	B	192	−7.797	27.838	−5.394	1.00	34.13		C
ATOM	3146	CZ	TYR	B	192	−8.319	28.142	−4.152	1.00	31.36		C
ATOM	3147	OH	TYR	B	192	−7.526	28.732	−3.197	1.00	35.96		O
ATOM	3148	N	GLU	B	193	−10.895	28.609	−9.255	1.00	39.80		N
ATOM	3149	CA	GLU	B	193	−10.237	29.811	−9.763	1.00	43.18		C
ATOM	3150	C	GLU	B	193	−11.213	30.900	−10.210	1.00	39.55		C
ATOM	3151	O	GLU	B	193	−10.799	32.022	−10.496	1.00	44.13		O
ATOM	3152	CB	GLU	B	193	−9.311	29.440	−10.921	1.00	44.18		C
ATOM	3153	CG	GLU	B	193	−8.172	28.528	−10.515	1.00	46.87		C
ATOM	3154	CD	GLU	B	193	−7.393	28.010	−11.704	1.00	66.53		C
ATOM	3155	OE1	GLU	B	193	−7.965	27.968	−12.815	1.00	70.34		O
ATOM	3156	OE2	GLU	B	193	−6.210	27.648	−11.529	1.00	73.19		O
ATOM	3157	N	LYS	B	194	−12.502	30.575	−10.261	1.00	41.15		N
ATOM	3158	CA	LYS	B	194	−13.522	31.554	−10.634	1.00	39.86		C
ATOM	3159	C	LYS	B	194	−13.955	32.429	−9.461	1.00	44.25		C
ATOM	3160	O	LYS	B	194	−14.816	33.295	−9.615	1.00	42.88		O
ATOM	3161	CB	LYS	B	194	−14.754	30.855	−11.214	1.00	43.14		C
ATOM	3162	CG	LYS	B	194	−14.506	30.110	−12.507	1.00	50.46		C
ATOM	3163	CD	LYS	B	194	−15.768	29.418	−12.991	1.00	54.94		C
ATOM	3164	CE	LYS	B	194	−15.503	28.612	−14.255	1.00	65.50		C
ATOM	3165	NZ	LYS	B	194	−14.922	29.454	−15.339	1.00	69.52		N
ATOM	3166	N	HIS	B	195	−13.373	32.204	−8.288	1.00	42.19		N
ATOM	3167	CA	HIS	B	195	−13.799	32.939	−7.099	1.00	42.19		C
ATOM	3168	C	HIS	B	195	−12.625	33.455	−6.285	1.00	36.87		C
ATOM	3169	O	HIS	B	195	−11.498	32.976	−6.423	1.00	37.36		O
ATOM	3170	CB	HIS	B	195	−14.687	32.061	−6.214	1.00	38.63		C
ATOM	3171	CG	HIS	B	195	−15.894	31.518	−6.914	1.00	41.06		C
ATOM	3172	CD2	HIS	B	195	−16.180	30.270	−7.356	1.00	44.21		C
ATOM	3173	ND1	HIS	B	195	−16.987	32.296	−7.224	1.00	43.75		N
ATOM	3174	CE1	HIS	B	195	−17.894	31.554	−7.834	1.00	44.35		C
ATOM	3175	NE2	HIS	B	195	−17.430	30.321	−7.926	1.00	44.01		N
ATOM	3176	N	LYS	B	196	−12.908	34.424	−5.420	1.00	38.25		N
ATOM	3177	CA	LYS	B	196	−11.876	35.084	−4.639	1.00	35.29		C
ATOM	3178	C	LYS	B	196	−11.915	34.716	−3.152	1.00	39.07		C
ATOM	3179	O	LYS	B	196	−10.942	34.190	−2.615	1.00	39.45		O
ATOM	3180	CB	LYS	B	196	−11.998	36.602	−4.793	1.00	41.25		C
ATOM	3181	CG	LYS	B	196	−10.931	37.391	−4.047	1.00	43.11		C
ATOM	3182	CD	LYS	B	196	−11.215	38.884	−4.099	1.00	57.11		C
ATOM	3183	CE	LYS	B	196	−10.103	39.686	−3.447	1.00	60.58		C
ATOM	3184	NZ	LYS	B	196	−10.341	41.150	−3.566	1.00	75.28		N
ATOM	3185	N	VAL	B	197	−13.032	35.002	−2.488	1.00	33.64		N
ATOM	3186	CA	VAL	B	197	−13.108	34.851	−1.037	1.00	41.13		C
ATOM	3187	C	VAL	B	197	−13.640	33.478	−0.620	1.00	39.79		C
ATOM	3188	O	VAL	B	197	−14.758	33.098	−0.973	1.00	35.93		O
ATOM	3189	CB	VAL	B	197	−13.993	35.943	−0.400	1.00	39.79		C
ATOM	3190	CG1	VAL	B	197	−13.964	35.829	1.117	1.00	33.80		C
ATOM	3191	CG2	VAL	B	197	−13.532	37.330	−0.834	1.00	36.75		C
ATOM	3192	N	TYR	B	198	−12.827	32.743	0.134	1.00	36.80		N
ATOM	3193	CA	TYR	B	198	−13.223	31.442	0.662	1.00	31.41		C
ATOM	3194	C	TYR	B	198	−13.289	31.518	2.173	1.00	34.47		C
ATOM	3195	O	TYR	B	198	−12.324	31.909	2.821	1.00	35.65		O
ATOM	3196	CB	TYR	B	198	−12.252	30.347	0.210	1.00	29.88		C
ATOM	3197	CG	TYR	B	198	−12.394	30.041	−1.259	1.00	32.49		C
ATOM	3198	CD1	TYR	B	198	−11.774	30.838	−2.219	1.00	31.45		C
ATOM	3199	CD2	TYR	B	198	−13.179	28.978	−1.694	1.00	30.07		C
ATOM	3200	CE1	TYR	B	198	−11.919	30.573	−3.572	1.00	35.86		C
ATOM	3201	CE2	TYR	B	198	−13.327	28.706	−3.043	1.00	31.84		C
ATOM	3202	CZ	TYR	B	198	−12.695	29.509	−3.975	1.00	31.78		C
ATOM	3203	OH	TYR	B	198	−12.842	29.245	−5.313	1.00	37.12		O
ATOM	3204	N	ALA	B	199	−14.435	31.148	2.731	1.00	31.33		N
ATOM	3205	CA	ALA	B	199	−14.672	31.330	4.155	1.00	35.87		C
ATOM	3206	C	ALA	B	199	−15.414	30.150	4.755	1.00	37.75		C
ATOM	3207	O	ALA	B	199	−16.236	29.517	4.090	1.00	29.26		O
ATOM	3208	CB	ALA	B	199	−15.454	32.614	4.394	1.00	28.89		C
ATOM	3209	N	CYS	B	200	−15.114	29.844	6.012	1.00	29.79		N
ATOM	3210	CA	CYS	B	200	−15.967	28.940	6.764	1.00	30.62		C
ATOM	3211	C	CYS	B	200	−16.481	29.695	7.980	1.00	34.82		C
ATOM	3212	O	CYS	B	200	−15.727	30.376	8.673	1.00	35.07		O
ATOM	3213	CB	CYS	B	200	−15.232	27.651	7.157	1.00	39.10		C
ATOM	3214	SG	CYS	B	200	−13.954	27.783	8.432	1.00	54.20		S
ATOM	3215	N	GLU	B	201	−17.785	29.598	8.205	1.00	34.80		N
ATOM	3216	CA	GLU	B	201	−18.438	30.312	9.289	1.00	35.26		C
ATOM	3217	C	GLU	B	201	−18.905	29.313	10.338	1.00	33.11		C
ATOM	3218	O	GLU	B	201	−19.670	28.395	10.036	1.00	30.25		O
ATOM	3219	CB	GLU	B	201	−19.619	31.134	8.764	1.00	31.34		C
ATOM	3220	CG	GLU	B	201	−20.333	31.938	9.838	1.00	46.76		C
ATOM	3221	CD	GLU	B	201	−21.725	32.382	9.423	1.00	57.59		C
ATOM	3222	OE1	GLU	B	201	−22.650	31.538	9.431	1.00	59.83		O
ATOM	3223	OE2	GLU	B	201	−21.893	33.575	9.093	1.00	62.46		O
ATOM	3224	N	VAL	B	202	−18.450	29.490	11.572	1.00	33.14		N
ATOM	3225	CA	VAL	B	202	−18.715	28.498	12.604	1.00	34.14		C
ATOM	3226	C	VAL	B	202	−19.683	28.996	13.674	1.00	34.64		C
ATOM	3227	O	VAL	B	202	−19.512	30.079	14.236	1.00	32.69		O
ATOM	3228	CB	VAL	B	202	−17.408	28.046	13.276	1.00	32.83		C
ATOM	3229	CG1	VAL	B	202	−17.699	27.136	14.458	1.00	27.65		C
ATOM	3230	CG2	VAL	B	202	−16.513	27.355	12.258	1.00	31.56		C
ATOM	3231	N	THR	B	203	−20.702	28.185	13.942	1.00	30.80		N
ATOM	3232	CA	THR	B	203	−21.670	28.455	14.997	1.00	34.07		C
ATOM	3233	C	THR	B	203	−21.556	27.394	16.091	1.00	36.01		C
ATOM	3234	O	THR	B	203	−21.518	26.196	15.802	1.00	34.64		O
ATOM	3235	CB	THR	B	203	−23.111	28.477	14.444	1.00	36.63		C
ATOM	3236	CG2	THR	B	203	−24.102	28.883	15.526	1.00	36.15		C
ATOM	3237	OG1	THR	B	203	−23.190	29.403	13.356	1.00	45.86		O
ATOM	3238	N	HIS	B	204	−21.499	27.841	17.343	1.00	32.76		N
ATOM	3239	CA	HIS	B	204	−21.356	26.946	18.487	1.00	34.42		C
ATOM	3240	C	HIS	B	204	−21.850	27.620	19.764	1.00	33.50		C
ATOM	3241	O	HIS	B	204	−21.750	28.837	19.909	1.00	34.28		O
ATOM	3242	CB	HIS	B	204	−19.895	26.510	18.656	1.00	29.00		C
ATOM	3243	CG	HIS	B	204	−19.689	25.483	19.728	1.00	38.33		C
ATOM	3244	CD2	HIS	B	204	−19.847	24.138	19.717	1.00	32.84		C
ATOM	3245	ND1	HIS	B	204	−19.266	25.810	20.999	1.00	29.49		N
ATOM	3246	CE1	HIS	B	204	−19.177	24.710	21.726	1.00	34.17		C
ATOM	3247	NE2	HIS	B	204	−19.522	23.681	20.973	1.00	33.34		N
ATOM	3248	N	GLN	B	205	−22.367	26.816	20.687	1.00	33.90		N
ATOM	3249	CA	GLN	B	205	−22.892	27.307	21.961	1.00	33.84		C
ATOM	3250	C	GLN	B	205	−21.905	28.198	22.725	1.00	36.35		C
ATOM	3251	O	GLN	B	205	−22.313	29.126	23.425	1.00	40.21		O
ATOM	3252	CB	GLN	B	205	−23.309	26.121	22.835	1.00	33.40		C
ATOM	3253	CG	GLN	B	205	−23.981	26.507	24.136	1.00	49.24		C
ATOM	3254	CD	GLN	B	205	−24.475	25.304	24.914	1.00	50.37		C
ATOM	3255	NE2	GLN	B	205	−24.852	25.527	26.168	1.00	57.58		N
ATOM	3256	OE1	GLN	B	205	−24.518	24.186	24.396	1.00	53.77		O
ATOM	3257	N	GLY	B	206	−20.610	27.931	22.578	1.00	30.24		N
ATOM	3258	CA	GLY	B	206	−19.587	28.728	23.237	1.00	32.96		C
ATOM	3259	C	GLY	B	206	−19.239	30.036	22.542	1.00	34.80		C
ATOM	3260	O	GLY	B	206	−18.466	30.834	23.064	1.00	30.49		O
ATOM	3261	N	LEU	B	207	−19.806	30.260	21.363	1.00	38.67		N
ATOM	3262	CA	LEU	B	207	−19.553	31.492	20.619	1.00	41.75		C
ATOM	3263	C	LEU	B	207	−20.765	32.412	20.674	1.00	40.10		C
ATOM	3264	O	LEU	B	207	−21.848	32.050	20.210	1.00	42.41		O
ATOM	3265	CB	LEU	B	207	−19.204	31.180	19.165	1.00	34.75		C
ATOM	3266	CG	LEU	B	207	−17.957	30.336	18.917	1.00	35.04		C
ATOM	3267	CD1	LEU	B	207	−17.871	29.946	17.444	1.00	32.97		C
ATOM	3268	CD2	LEU	B	207	−16.709	31.087	19.362	1.00	34.44		C
ATOM	3269	N	SER	B	208	−20.582	33.600	21.239	1.00	41.65		N
ATOM	3270	CA	SER	B	208	−21.685	34.551	21.366	1.00	50.19		C
ATOM	3271	C	SER	B	208	−22.189	34.991	19.989	1.00	43.51		C
ATOM	3272	O	SER	B	208	−23.367	35.307	19.824	1.00	51.88		O
ATOM	3273	CB	SER	B	208	−21.260	35.758	22.207	1.00	41.21		C
ATOM	3274	OG	SER	B	208	−19.985	36.239	21.815	1.00	63.38		O
ATOM	3275	N	SER	B	209	−21.296	34.995	19.002	1.00	40.06		N
ATOM	3276	CA	SER	B	209	−21.682	35.228	17.613	1.00	44.47		C
ATOM	3277	C	SER	B	209	−20.812	34.364	16.695	1.00	38.33		C
ATOM	3278	O	SER	B	209	−19.696	34.005	17.067	1.00	43.33		O
ATOM	3279	CB	SER	B	209	−21.557	36.715	17.253	1.00	45.07		C
ATOM	3280	OG	SER	B	209	−20.203	37.102	17.120	1.00	49.50		O
ATOM	3281	N	PRO	B	210	−21.323	34.017	15.499	1.00	44.65		N
ATOM	3282	CA	PRO	B	210	−20.580	33.149	14.574	1.00	38.77		C
ATOM	3283	C	PRO	B	210	−19.176	33.661	14.264	1.00	41.23		C
ATOM	3284	O	PRO	B	210	−18.966	34.867	14.141	1.00	45.61		O
ATOM	3285	CB	PRO	B	210	−21.450	33.156	13.315	1.00	39.30		C
ATOM	3286	CG	PRO	B	210	−22.826	33.399	13.826	1.00	43.89		C
ATOM	3287	CD	PRO	B	210	−22.658	34.357	14.974	1.00	40.75		C
ATOM	3288	N	VAL	B	211	−18.224	32.741	14.155	1.00	39.40		N
ATOM	3289	CA	VAL	B	211	−16.834	33.090	13.883	1.00	39.75		C
ATOM	3290	C	VAL	B	211	−16.475	32.703	12.452	1.00	40.69		C
ATOM	3291	O	VAL	B	211	−16.747	31.582	12.020	1.00	36.87		O
ATOM	3292	CB	VAL	B	211	−15.877	32.398	14.880	1.00	38.99		C
ATOM	3293	CG1	VAL	B	211	−14.429	32.537	14.436	1.00	34.79		C
ATOM	3294	CG2	VAL	B	211	−16.071	32.973	16.272	1.00	40.49		C
ATOM	3295	N	THR	B	212	−15.880	33.639	11.716	1.00	35.72		N
ATOM	3296	CA	THR	B	212	−15.550	33.409	10.314	1.00	39.63		C
ATOM	3297	C	THR	B	212	−14.055	33.500	10.046	1.00	35.76		C
ATOM	3298	O	THR	B	212	−13.424	34.518	10.323	1.00	42.94		O
ATOM	3299	CB	THR	B	212	−16.272	34.414	9.391	1.00	38.85		C
ATOM	3300	CG2	THR	B	212	−15.814	34.238	7.953	1.00	37.83		C
ATOM	3301	OG1	THR	B	212	−17.687	34.196	9.461	1.00	46.70		O
ATOM	3302	N	LYS	B	213	−13.491	32.424	9.513	1.00	33.60		N
ATOM	3303	CA	LYS	B	213	−12.120	32.451	9.029	1.00	36.19		C
ATOM	3304	C	LYS	B	213	−12.155	32.386	7.514	1.00	38.31		C
ATOM	3305	O	LYS	B	213	−12.964	31.659	6.938	1.00	40.76		O
ATOM	3306	CB	LYS	B	213	−11.298	31.295	9.602	1.00	35.13		C
ATOM	3307	CG	LYS	B	213	−11.186	31.301	11.120	1.00	41.13		C
ATOM	3308	CD	LYS	B	213	−10.462	32.537	11.635	1.00	36.48		C
ATOM	3309	CE	LYS	B	213	−10.432	32.550	13.161	1.00	36.86		C
ATOM	3310	NZ	LYS	B	213	−9.699	33.727	13.703	1.00	51.87		N
ATOM	3311	N	SER	B	214	−11.283	33.149	6.869	1.00	36.97		N
ATOM	3312	CA	SER	B	214	−11.301	33.233	5.420	1.00	35.10		C
ATOM	3313	C	SER	B	214	−9.934	33.547	4.827	1.00	37.64		C
ATOM	3314	O	SER	B	214	−9.021	33.986	5.524	1.00	41.48		O
ATOM	3315	CB	SER	B	214	−12.307	34.291	4.971	1.00	35.76		C
ATOM	3316	OG	SER	B	214	−11.918	35.574	5.422	1.00	40.23		O
ATOM	3317	N	PHE	B	215	−9.804	33.297	3.530	1.00	36.45		N
ATOM	3318	CA	PHE	B	215	−8.651	33.746	2.767	1.00	39.24		C
ATOM	3319	C	PHE	B	215	−9.114	34.202	1.388	1.00	45.83		C
ATOM	3320	O	PHE	B	215	−10.185	33.804	0.916	1.00	37.02		O
ATOM	3321	CB	PHE	B	215	−7.598	32.640	2.645	1.00	32.01		C
ATOM	3322	CG	PHE	B	215	−8.066	31.428	1.878	1.00	38.83		C
ATOM	3323	CD1	PHE	B	215	−8.729	30.397	2.524	1.00	31.21		C
ATOM	3324	CD2	PHE	B	215	−7.830	31.315	0.516	1.00	35.76		C
ATOM	3325	CE1	PHE	B	215	−9.156	29.279	1.825	1.00	33.60		C
ATOM	3326	CE2	PHE	B	215	−8.251	30.201	−0.190	1.00	35.19		C
ATOM	3327	CZ	PHE	B	215	−8.915	29.180	0.466	1.00	34.00		C
ATOM	3328	N	ASN	B	216	−8.316	35.057	0.761	1.00	45.06		N
ATOM	3329	CA	ASN	B	216	−8.533	35.429	−0.629	1.00	42.67		C
ATOM	3330	C	ASN	B	216	−7.591	34.626	−1.499	1.00	39.47		C
ATOM	3331	O	ASN	B	216	−6.388	34.607	−1.255	1.00	45.25		O
ATOM	3332	CB	ASN	B	216	−8.310	36.926	−0.843	1.00	45.51		C
ATOM	3333	CG	ASN	B	216	−9.256	37.778	−0.024	1.00	49.43		C
ATOM	3334	ND2	ASN	B	216	−8.785	38.943	0.402	1.00	55.43		N
ATOM	3335	OD1	ASN	B	216	−10.396	37.393	0.227	1.00	51.90		O
ATOM	3336	N	ARG	B	217	−8.138	33.946	−2.499	1.00	39.98		N
ATOM	3337	CA	ARG	B	217	−7.327	33.135	−3.396	1.00	43.37		C
ATOM	3338	C	ARG	B	217	−6.257	33.985	−4.069	1.00	49.33		C
ATOM	3339	O	ARG	B	217	−6.559	35.019	−4.665	1.00	52.85		O
ATOM	3340	CB	ARG	B	217	−8.207	32.457	−4.449	1.00	42.40		C
ATOM	3341	CG	ARG	B	217	−7.441	31.578	−5.420	1.00	38.23		C
ATOM	3342	CD	ARG	B	217	−8.358	31.012	−6.485	1.00	38.31		C
ATOM	3343	NE	ARG	B	217	−9.059	32.068	−7.204	1.00	42.76		N
ATOM	3344	CZ	ARG	B	217	−8.588	32.665	−8.292	1.00	51.33		C
ATOM	3345	NH1	ARG	B	217	−7.414	32.303	−8.793	1.00	42.73		N
ATOM	3346	NH2	ARG	B	217	−9.294	33.622	−8.883	1.00	48.38		N
ATOM	3347	N	GLY	B	218	−5.004	33.555	−3.952	1.00	53.01		N
ATOM	3348	CA	GLY	B	218	−3.897	34.253	−4.582	1.00	57.34		C
ATOM	3349	C	GLY	B	218	−3.338	35.410	−3.771	1.00	63.03		C
ATOM	3350	O	GLY	B	218	−2.818	36.373	−4.334	1.00	67.80		O
ATOM	3351	N	GLU	B	219	−3.443	35.321	−2.449	1.00	60.01		N
ATOM	3352	CA	GLU	B	219	−2.900	36.353	−1.571	1.00	61.79		C
ATOM	3353	C	GLU	B	219	−2.130	35.742	−0.405	1.00	61.79		C
ATOM	3354	O	GLU	B	219	−1.976	34.525	−0.321	1.00	69.81		O
ATOM	3355	CB	GLU	B	219	−4.015	37.259	−1.042	1.00	62.53		C
ATOM	3356	CG	GLU	B	219	−4.663	38.151	−2.096	1.00	56.22		C
ATOM	3357	CD	GLU	B	219	−5.625	39.161	−1.489	1.00	74.19		C
ATOM	3358	OE1	GLU	B	219	−5.593	39.345	−0.252	1.00	78.86		O
ATOM	3359	OE2	GLU	B	219	−6.413	39.770	−2.247	1.00	64.28		O
TER
ATOM	3360	N	THR	C	152	−29.241	−45.858	26.627	1.00	80.47	D000	N
ATOM	3361	CA	THR	C	152	−29.487	−45.616	28.045	1.00	91.58	D000	C
ATOM	3362	C	THR	C	152	−29.269	−44.146	28.405	1.00	88.87	D000	C
ATOM	3363	O	THR	C	152	−28.934	−43.329	27.545	1.00	88.60	D000	O
ATOM	3364	CB	THR	C	152	−28.582	−46.499	28.936	1.00	90.05	D000	C
ATOM	3365	CG2	THR	C	152	−29.009	−47.960	28.857	1.00	70.32	D000	C
ATOM	3366	OG1	THR	C	152	−27.220	−46.382	28.506	1.00	79.38	D000	O
ATOM	3367	N	CYS	C	153	−29.465	−43.813	29.677	1.00	83.40	D000	N
ATOM	3368	CA	CYS	C	153	−29.261	−42.446	30.143	1.00	72.69	D000	C
ATOM	3369	C	CYS	C	153	−28.836	−42.415	31.611	1.00	63.73	D000	C
ATOM	3370	O	CYS	C	153	−28.923	−43.419	32.318	1.00	52.26	D000	O
ATOM	3371	CB	CYS	C	153	−30.532	−41.616	29.941	1.00	73.56	D000	C
ATOM	3372	SG	CYS	C	153	−30.281	−39.826	30.081	1.00	98.30	D000	S
ATOM	3373	N	CYS	C	154	−28.370	−41.254	32.059	1.00	61.15	D000	N
ATOM	3374	CA	CYS	C	154	−27.916	−41.085	33.434	1.00	58.46	D000	C
ATOM	3375	C	CYS	C	154	−29.071	−41.141	34.432	1.00	51.28	D000	C
ATOM	3376	O	CYS	C	154	−30.208	−40.827	34.086	1.00	47.54	D000	O
ATOM	3377	CB	CYS	C	154	−27.160	−39.758	33.580	1.00	53.06	D000	C
ATOM	3378	SG	CYS	C	154	−25.446	−39.818	33.000	1.00	71.64	D000	S
ATOM	3379	N	PRO	C	155	−28.781	−41.556	35.674	1.00	43.23	D000	N
ATOM	3380	CA	PRO	C	155	−29.767	−41.494	36.757	1.00	48.50	D000	C
ATOM	3381	C	PRO	C	155	−30.193	−40.062	37.062	1.00	49.23	D000	C
ATOM	3382	O	PRO	C	155	−29.481	−39.117	36.708	1.00	42.32	D000	O
ATOM	3383	CB	PRO	C	155	−29.020	−42.104	37.953	1.00	42.80	D000	C
ATOM	3384	CG	PRO	C	155	−27.576	−41.991	37.609	1.00	50.48	D000	C
ATOM	3385	CD	PRO	C	155	−27.514	−42.158	36.122	1.00	50.94	D000	C
ATOM	3386	N	VAL	C	156	−31.343	−39.913	37.713	1.00	40.74	D000	N
ATOM	3387	CA	VAL	C	156	−31.863	−38.598	38.077	1.00	48.19	D000	C
ATOM	3388	C	VAL	C	156	−30.837	−37.822	38.897	1.00	42.17	D000	C
ATOM	3389	O	VAL	C	156	−30.149	−38.403	39.739	1.00	40.87	D000	O
ATOM	3390	CB	VAL	C	156	−33.183	−38.717	38.875	1.00	54.12	D000	C
ATOM	3391	CG1	VAL	C	156	−33.775	−37.341	39.149	1.00	44.84	D000	C
ATOM	3392	CG2	VAL	C	156	−34.181	−39.590	38.122	1.00	50.34	D000	C
ATOM	3393	N	ASN	C	157	−30.727	−36.522	38.610	1.00	41.21	D000	N
ATOM	3394	CA	ASN	C	157	−29.820	−35.593	39.292	1.00	41.02	D000	C
ATOM	3395	C	ASN	C	157	−28.353	−35.786	38.927	1.00	39.65	D000	C
ATOM	3396	O	ASN	C	157	−27.481	−35.121	39.485	1.00	47.91	D000	O
ATOM	3397	CB	ASN	C	157	−29.979	−35.689	40.812	1.00	45.93	D000	C
ATOM	3398	CG	ASN	C	157	−31.360	−35.289	41.276	1.00	51.89	D000	C
ATOM	3399	ND2	ASN	C	157	−31.885	−36.011	42.260	1.00	51.21	D000	N
ATOM	3400	OD1	ASN	C	157	−31.953	−34.347	40.752	1.00	55.30	D000	O
ATOM	3401	N	TRP	C	158	−28.081	−36.696	37.997	1.00	38.04	D000	N
ATOM	3402	CA	TRP	C	158	−26.737	−36.841	37.449	1.00	35.52	D000	C
ATOM	3403	C	TRP	C	158	−26.694	−36.212	36.061	1.00	41.15	D000	C
ATOM	3404	O	TRP	C	158	−27.720	−36.118	35.387	1.00	32.47	D000	O
ATOM	3405	CB	TRP	C	158	−26.323	−38.313	37.394	1.00	35.29	D000	C
ATOM	3406	CG	TRP	C	158	−26.115	−38.930	38.751	1.00	40.11	D000	C
ATOM	3407	CD1	TRP	C	158	−27.045	−39.064	39.741	1.00	38.54	D000	C
ATOM	3408	CD2	TRP	C	158	−24.903	−39.505	39.262	1.00	36.91	D000	C
ATOM	3409	CE2	TRP	C	158	−25.175	−39.961	40.568	1.00	38.54	D000	C
ATOM	3410	CE3	TRP	C	158	−23.615	−39.676	38.743	1.00	32.86	D000	C
ATOM	3411	NE1	TRP	C	158	−26.488	−39.677	40.837	1.00	42.00	D000	N
ATOM	3412	CZ2	TRP	C	158	−24.209	−40.576	41.362	1.00	34.01	D000	C
ATOM	3413	CZ3	TRP	C	158	−22.657	−40.286	39.533	1.00	31.10	D000	C
ATOM	3414	CH2	TRP	C	158	−22.958	−40.728	40.827	1.00	31.72	D000	C
ATOM	3415	N	VAL	C	159	−25.511	−35.775	35.640	1.00	37.12	D000	N
ATOM	3416	CA	VAL	C	159	−25.359	−35.091	34.360	1.00	35.19	D000	C
ATOM	3417	C	VAL	C	159	−24.434	−35.876	33.422	1.00	42.52	D000	C
ATOM	3418	O	VAL	C	159	−23.383	−36.372	33.837	1.00	37.10	D000	O
ATOM	3419	CB	VAL	C	159	−24.811	−33.660	34.557	1.00	36.85	D000	C
ATOM	3420	CG1	VAL	C	159	−24.794	−32.907	33.240	1.00	35.63	D000	C
ATOM	3421	CG2	VAL	C	159	−25.650	−32.909	35.583	1.00	36.56	D000	C
ATOM	3422	N	GLU	C	160	−24.827	−35.987	32.157	1.00	36.06	D000	N
ATOM	3423	CA	GLU	C	160	−24.070	−36.784	31.197	1.00	43.73	D000	C
ATOM	3424	C	GLU	C	160	−23.047	−35.975	30.405	1.00	36.77	D000	C
ATOM	3425	O	GLU	C	160	−23.328	−34.874	29.939	1.00	41.07	D000	O
ATOM	3426	CB	GLU	C	160	−25.018	−37.481	30.221	1.00	43.94	D000	C
ATOM	3427	CG	GLU	C	160	−24.301	−38.291	29.158	1.00	50.04	D000	C
ATOM	3428	CD	GLU	C	160	−25.222	−38.743	28.045	1.00	67.78	D000	C
ATOM	3429	OE1	GLU	C	160	−26.430	−38.930	28.308	1.00	69.69	D000	O
ATOM	3430	OE2	GLU	C	160	−24.735	−38.904	26.905	1.00	67.23	D000	O
ATOM	3431	N	HIS	C	161	−21.856	−36.541	30.261	1.00	37.45	D000	N
ATOM	3432	CA	HIS	C	161	−20.829	−35.993	29.388	1.00	38.41	D000	C
ATOM	3433	C	HIS	C	161	−19.987	−37.135	28.842	1.00	40.31	D000	C
ATOM	3434	O	HIS	C	161	−19.301	−37.816	29.604	1.00	36.78	D000	O
ATOM	3435	CB	HIS	C	161	−19.951	−34.987	30.134	1.00	35.44	D000	C
ATOM	3436	CG	HIS	C	161	−18.785	−34.487	29.334	1.00	39.39	D000	C
ATOM	3437	CD2	HIS	C	161	−17.492	−34.888	29.300	1.00	37.49	D000	C
ATOM	3438	ND1	HIS	C	161	−18.888	−33.445	28.439	1.00	37.81	D000	N
ATOM	3439	CE1	HIS	C	161	−17.707	−33.223	27.887	1.00	36.44	D000	C
ATOM	3440	NE2	HIS	C	161	−16.844	−34.085	28.390	1.00	39.12	D000	N
ATOM	3441	N	GLU	C	162	−20.066	−37.349	27.529	1.00	45.55	D000	N
ATOM	3442	CA	GLU	C	162	−19.271	−38.365	26.834	1.00	40.64	D000	C
ATOM	3443	C	GLU	C	162	−19.341	−39.749	27.484	1.00	41.12	D000	C
ATOM	3444	O	GLU	C	162	−18.318	−40.305	27.887	1.00	42.56	D000	O
ATOM	3445	CB	GLU	C	162	−17.806	−37.919	26.744	1.00	41.10	D000	C
ATOM	3446	CG	GLU	C	162	−17.596	−36.576	26.052	1.00	49.56	D000	C
ATOM	3447	CD	GLU	C	162	−18.120	−36.554	24.622	1.00	68.97	D000	C
ATOM	3448	OE1	GLU	C	162	−18.103	−37.612	23.955	1.00	61.44	D000	O
ATOM	3449	OE2	GLU	C	162	−18.551	−35.472	24.163	1.00	82.19	D000	O
ATOM	3450	N	ARG	C	163	−20.550	−40.289	27.586	1.00	39.55	D000	N
ATOM	3451	CA	ARG	C	163	−20.790	−41.614	28.175	1.00	50.72	D000	C
ATOM	3452	C	ARG	C	163	−20.305	−41.757	29.628	1.00	46.47	D000	C
ATOM	3453	O	ARG	C	163	−20.132	−42.870	30.127	1.00	44.94	D000	O
ATOM	3454	CB	ARG	C	163	−20.156	−42.710	27.306	1.00	49.40	D000	C
ATOM	3455	CG	ARG	C	163	−20.768	−42.827	25.907	1.00	51.79	D000	C
ATOM	3456	CD	ARG	C	163	−20.685	−44.252	25.348	1.00	44.72	D000	C
ATOM	3457	NE	ARG	C	163	−21.723	−45.140	25.879	1.00	51.93	D000	N
ATOM	3458	CZ	ARG	C	163	−21.483	−46.234	26.606	1.00	59.01	D000	C
ATOM	3459	NH1	ARG	C	163	−22.492	−46.980	27.044	1.00	45.88	D000	N
ATOM	3460	NH2	ARG	C	163	−20.236	−46.586	26.897	1.00	49.85	D000	N
ATOM	3461	N	SER	C	164	−20.099	−40.633	30.306	1.00	43.03	D000	N
ATOM	3462	CA	SER	C	164	−19.865	−40.646	31.746	1.00	37.64	D000	C
ATOM	3463	C	SER	C	164	−20.969	−39.876	32.459	1.00	37.23	D000	C
ATOM	3464	O	SER	C	164	−21.536	−38.933	31.903	1.00	37.58	D000	O
ATOM	3465	CB	SER	C	164	−18.498	−40.052	32.092	1.00	37.20	D000	C
ATOM	3466	OG	SER	C	164	−17.509	−41.061	32.172	1.00	40.60	D000	O
ATOM	3467	N	CYS	C	165	−21.272	−40.283	33.687	1.00	36.28	D000	N
ATOM	3468	CA	CYS	C	165	−22.296	−39.624	34.493	1.00	35.32	D000	C
ATOM	3469	C	CYS	C	165	−21.666	−38.921	35.688	1.00	39.53	D000	C
ATOM	3470	O	CYS	C	165	−20.843	−39.504	36.398	1.00	33.29	D000	O
ATOM	3471	CB	CYS	C	165	−23.344	−40.632	34.974	1.00	42.45	D000	C
ATOM	3472	SG	CYS	C	165	−24.315	−41.382	33.657	1.00	55.85	D000	S
ATOM	3473	N	TYR	C	166	−22.065	−37.674	35.915	1.00	29.38	D000	N
ATOM	3474	CA	TYR	C	166	−21.475	−36.870	36.976	1.00	33.48	D000	C
ATOM	3475	C	TYR	C	166	−22.532	−36.391	37.963	1.00	33.01	D000	C
ATOM	3476	O	TYR	C	166	−23.665	−36.110	37.589	1.00	33.24	D000	O
ATOM	3477	CB	TYR	C	166	−20.730	−35.667	36.388	1.00	32.05	D000	C
ATOM	3478	CG	TYR	C	166	−19.658	−36.030	35.383	1.00	31.06	D000	C
ATOM	3479	CD1	TYR	C	166	−19.990	−36.385	34.080	1.00	30.70	D000	C
ATOM	3480	CD2	TYR	C	166	−18.313	−36.003	35.732	1.00	30.70	D000	C
ATOM	3481	CE1	TYR	C	166	−19.017	−36.713	33.153	1.00	33.69	D000	C
ATOM	3482	CE2	TYR	C	166	−17.329	−36.329	34.807	1.00	32.22	D000	C
ATOM	3483	CZ	TYR	C	166	−17.690	−36.682	33.519	1.00	32.45	D000	C
ATOM	3484	OH	TYR	C	166	−16.723	−37.007	32.593	1.00	35.47	D000	O
ATOM	3485	N	TRP	C	167	−22.156	−36.309	39.231	1.00	33.71	D000	N
ATOM	3486	CA	TRP	C	167	−23.032	−35.743	40.246	1.00	35.55	D000	C
ATOM	3487	C	TRP	C	167	−22.262	−34.685	41.017	1.00	32.66	D000	C
ATOM	3488	O	TRP	C	167	−21.140	−34.931	41.470	1.00	31.46	D000	O
ATOM	3489	CB	TRP	C	167	−23.559	−36.827	41.186	1.00	35.80	D000	C
ATOM	3490	CG	TRP	C	167	−24.458	−36.290	42.265	1.00	43.58	D000	C
ATOM	3491	CD1	TRP	C	167	−25.805	−36.079	42.183	1.00	38.70	D000	C
ATOM	3492	CD2	TRP	C	167	−24.070	−35.896	43.587	1.00	35.59	D000	C
ATOM	3493	CE2	TRP	C	167	−25.235	−35.456	44.251	1.00	41.09	D000	C
ATOM	3494	CE3	TRP	C	167	−22.852	−35.869	44.271	1.00	35.37	D000	C
ATOM	3495	NE1	TRP	C	167	−26.280	−35.577	43.373	1.00	39.42	D000	N
ATOM	3496	CZ2	TRP	C	167	−25.215	−34.997	45.567	1.00	38.44	D000	C
ATOM	3497	CZ3	TRP	C	167	−22.835	−35.415	45.579	1.00	37.33	D000	C
ATOM	3498	CH2	TRP	C	167	−24.008	−34.985	46.213	1.00	36.75	D000	C
ATOM	3499	N	PHE	C	168	−22.858	−33.505	41.155	1.00	33.58	D000	N
ATOM	3500	CA	PHE	C	168	−22.172	−32.374	41.778	1.00	33.25	D000	C
ATOM	3501	C	PHE	C	168	−22.773	−32.041	43.134	1.00	31.97	D000	C
ATOM	3502	O	PHE	C	168	−23.953	−31.721	43.227	1.00	34.21	D000	O
ATOM	3503	CB	PHE	C	168	−22.229	−31.148	40.861	1.00	28.44	D000	C
ATOM	3504	CG	PHE	C	168	−21.573	−31.363	39.526	1.00	30.16	D000	C
ATOM	3505	CD1	PHE	C	168	−22.287	−31.896	38.463	1.00	31.96	D000	C
ATOM	3506	CD2	PHE	C	168	−20.239	−31.038	39.337	1.00	29.17	D000	C
ATOM	3507	CE1	PHE	C	168	−21.682	−32.099	37.229	1.00	29.38	D000	C
ATOM	3508	CE2	PHE	C	168	−19.625	−31.242	38.114	1.00	28.14	D000	C
ATOM	3509	CZ	PHE	C	168	−20.348	−31.776	37.057	1.00	28.28	D000	C
ATOM	3510	N	SER	C	169	−21.961	−32.110	44.186	1.00	30.11	D000	N
ATOM	3511	CA	SER	C	169	−22.462	−31.851	45.528	1.00	31.18	D000	C
ATOM	3512	C	SER	C	169	−22.693	−30.360	45.740	1.00	37.87	D000	C
ATOM	3513	O	SER	C	169	−22.121	−29.522	45.038	1.00	34.20	D000	O
ATOM	3514	CB	SER	C	169	−21.494	−32.389	46.583	1.00	30.35	D000	C
ATOM	3515	OG	SER	C	169	−20.471	−31.453	46.859	1.00	30.05	D000	O
ATOM	3516	N	ARG	C	170	−23.536	−30.027	46.708	1.00	37.76	D000	N
ATOM	3517	CA	ARG	C	170	−23.767	−28.628	47.046	1.00	42.71	D000	C
ATOM	3518	C	ARG	C	170	−23.330	−28.383	48.488	1.00	43.83	D000	C
ATOM	3519	O	ARG	C	170	−23.437	−27.274	49.010	1.00	47.78	D000	O
ATOM	3520	CB	ARG	C	170	−25.237	−28.254	46.829	1.00	44.70	D000	C
ATOM	3521	CG	ARG	C	170	−25.717	−28.513	45.395	1.00	57.03	D000	C
ATOM	3522	CD	ARG	C	170	−27.063	−27.862	45.082	1.00	63.29	D000	C
ATOM	3523	NE	ARG	C	170	−28.144	−28.365	45.925	1.00	84.25	D000	N
ATOM	3524	CZ	ARG	C	170	−28.822	−29.485	45.688	1.00	84.39	D000	C
ATOM	3525	NH1	ARG	C	170	−29.792	−29.862	46.511	1.00	72.14	D000	N
ATOM	3526	NH2	ARG	C	170	−28.528	−30.230	44.631	1.00	91.59	D000	N
ATOM	3527	N	SER	C	171	−22.817	−29.439	49.112	1.00	39.23	D000	N
ATOM	3528	CA	SER	C	171	−22.298	−29.372	50.470	1.00	41.01	D000	C
ATOM	3529	C	SER	C	171	−20.827	−29.773	50.489	1.00	37.33	D000	C
ATOM	3530	O	SER	C	171	−20.305	−30.281	49.499	1.00	31.87	D000	O
ATOM	3531	CB	SER	C	171	−23.106	−30.277	51.401	1.00	36.62	D000	C
ATOM	3532	OG	SER	C	171	−23.000	−31.633	51.004	1.00	43.48	D000	O
ATOM	3533	N	GLY	C	172	−20.166	−29.549	51.620	1.00	31.79	D000	N
ATOM	3534	CA	GLY	C	172	−18.749	−29.840	51.743	1.00	31.58	D000	C
ATOM	3535	C	GLY	C	172	−18.428	−31.069	52.573	1.00	37.61	D000	C
ATOM	3536	O	GLY	C	172	−19.161	−31.427	53.495	1.00	34.62	D000	O
ATOM	3537	N	LYS	C	173	−17.317	−31.714	52.231	1.00	32.21	D000	N
ATOM	3538	CA	LYS	C	173	−16.818	−32.878	52.954	1.00	30.84	D000	C
ATOM	3539	C	LYS	C	173	−15.300	−32.903	52.885	1.00	36.15	D000	C
ATOM	3540	O	LYS	C	173	−14.715	−32.463	51.894	1.00	35.63	D000	O
ATOM	3541	CB	LYS	C	173	−17.365	−34.184	52.367	1.00	35.20	D000	C
ATOM	3542	CG	LYS	C	173	−18.746	−34.590	52.824	1.00	33.26	D000	C
ATOM	3543	CD	LYS	C	173	−19.092	−35.966	52.277	1.00	36.71	D000	C
ATOM	3544	CE	LYS	C	173	−20.518	−36.364	52.617	1.00	39.30	D000	C
ATOM	3545	NZ	LYS	C	173	−20.706	−36.532	54.082	1.00	42.46	D000	N
ATOM	3546	N	ALA	C	174	−14.665	−33.423	53.930	1.00	34.50	D000	N
ATOM	3547	CA	ALA	C	174	−13.244	−33.733	53.871	1.00	32.78	D000	C
ATOM	3548	C	ALA	C	174	−13.011	−34.731	52.737	1.00	30.79	D000	C
ATOM	3549	O	ALA	C	174	−13.918	−35.486	52.375	1.00	27.51	D000	O
ATOM	3550	CB	ALA	C	174	−12.756	−34.296	55.201	1.00	32.37	D000	C
ATOM	3551	N	TRP	C	175	−11.802	−34.736	52.182	1.00	28.74	D000	N
ATOM	3552	CA	TRP	C	175	−11.510	−35.556	51.011	1.00	34.63	D000	C
ATOM	3553	C	TRP	C	175	−11.853	−37.026	51.230	1.00	31.83	D000	C
ATOM	3554	O	TRP	C	175	−12.520	−37.640	50.398	1.00	31.59	D000	O
ATOM	3555	CB	TRP	C	175	−10.041	−35.430	50.606	1.00	31.97	D000	C
ATOM	3556	CG	TRP	C	175	−9.771	−36.017	49.251	1.00	27.08	D000	C
ATOM	3557	CD1	TRP	C	175	−9.812	−35.364	48.051	1.00	33.57	D000	C
ATOM	3558	CD2	TRP	C	175	−9.442	−37.378	48.955	1.00	30.56	D000	C
ATOM	3559	CE2	TRP	C	175	−9.285	−37.476	47.558	1.00	29.73	D000	C
ATOM	3560	CE3	TRP	C	175	−9.257	−38.524	49.737	1.00	31.43	D000	C
ATOM	3561	NE1	TRP	C	175	−9.518	−36.234	47.029	1.00	30.16	D000	N
ATOM	3562	CZ2	TRP	C	175	−8.958	−38.674	46.926	1.00	31.89	D000	C
ATOM	3563	CZ3	TRP	C	175	−8.934	−39.711	49.107	1.00	33.11	D000	C
ATOM	3564	CH2	TRP	C	175	−8.787	−39.777	47.715	1.00	31.57	D000	C
ATOM	3565	N	ALA	C	176	−11.402	−37.585	52.349	1.00	36.55	D000	N
ATOM	3566	CA	ALA	C	176	−11.654	−38.992	52.642	1.00	34.85	D000	C
ATOM	3567	C	ALA	C	176	−13.153	−39.287	52.720	1.00	31.81	D000	C
ATOM	3568	O	ALA	C	176	−13.611	−40.335	52.264	1.00	32.34	D000	O
ATOM	3569	CB	ALA	C	176	−10.961	−39.397	53.940	1.00	39.21	D000	C
ATOM	3570	N	ASP	C	177	−13.921	−38.362	53.286	1.00	29.24	D000	N
ATOM	3571	CA	ASP	C	177	−15.363	−38.562	53.387	1.00	30.70	D000	C
ATOM	3572	C	ASP	C	177	−16.048	−38.465	52.021	1.00	34.41	D000	C
ATOM	3573	O	ASP	C	177	−17.005	−39.186	51.749	1.00	30.91	D000	O
ATOM	3574	CB	ASP	C	177	−15.976	−37.560	54.363	1.00	36.68	D000	C
ATOM	3575	CG	ASP	C	177	−15.641	−37.883	55.810	1.00	47.91	D000	C
ATOM	3576	OD1	ASP	C	177	−15.459	−39.080	56.124	1.00	48.52	D000	O
ATOM	3577	OD2	ASP	C	177	−15.561	−36.943	56.631	1.00	44.32	D000	O
ATOM	3578	N	ALA	C	178	−15.558	−37.575	51.164	1.00	33.94	D000	N
ATOM	3579	CA	ALA	C	178	−16.104	−37.450	49.814	1.00	37.48	D000	C
ATOM	3580	C	ALA	C	178	−15.776	−38.696	48.994	1.00	30.71	D000	C
ATOM	3581	O	ALA	C	178	−16.620	−39.219	48.265	1.00	33.32	D000	O
ATOM	3582	CB	ALA	C	178	−15.568	−36.197	49.130	1.00	29.20	D000	C
ATOM	3583	N	ASP	C	179	−14.540	−39.161	49.134	1.00	30.70	D000	N
ATOM	3584	CA	ASP	C	179	−14.078	−40.389	48.501	1.00	27.81	D000	C
ATOM	3585	C	ASP	C	179	−14.986	−41.564	48.868	1.00	36.66	D000	C
ATOM	3586	O	ASP	C	179	−15.411	−42.333	48.005	1.00	36.40	D000	O
ATOM	3587	CB	ASP	C	179	−12.630	−40.671	48.918	1.00	31.15	D000	C
ATOM	3588	CG	ASP	C	179	−12.068	−41.935	48.289	1.00	39.74	D000	C
ATOM	3589	OD1	ASP	C	179	−12.435	−42.255	47.139	1.00	49.64	D000	O
ATOM	3590	OD2	ASP	C	179	−11.247	−42.607	48.947	1.00	47.11	D000	O
ATOM	3591	N	ASN	C	180	−15.299	−41.680	50.153	1.00	32.38	D000	N
ATOM	3592	CA	ASN	C	180	−16.155	−42.751	50.642	1.00	33.10	D000	C
ATOM	3593	C	ASN	C	180	−17.598	−42.602	50.155	1.00	32.93	D000	C
ATOM	3594	O	ASN	C	180	−18.224	−43.582	49.755	1.00	36.93	D000	O
ATOM	3595	CB	ASN	C	180	−16.108	−42.799	52.171	1.00	39.79	D000	C
ATOM	3596	CG	ASN	C	180	−16.936	−43.931	52.745	1.00	50.05	D000	C
ATOM	3597	ND2	ASN	C	180	−16.557	−45.165	52.427	1.00	44.28	D000	N
ATOM	3598	OD1	ASN	C	180	−17.911	−43.699	53.461	1.00	53.44	D000	O
ATOM	3599	N	TYR	C	181	−18.120	−41.378	50.182	1.00	33.15	D000	N
ATOM	3600	CA	TYR	C	181	−19.460	−41.105	49.659	1.00	36.25	D000	C
ATOM	3601	C	TYR	C	181	−19.609	−41.606	48.218	1.00	38.76	D000	C
ATOM	3602	O	TYR	C	181	−20.608	−42.238	47.875	1.00	36.89	D000	O
ATOM	3603	CB	TYR	C	181	−19.775	−39.605	49.728	1.00	29.33	D000	C
ATOM	3604	CG	TYR	C	181	−21.139	−39.226	49.184	1.00	38.78	D000	C
ATOM	3605	CD1	TYR	C	181	−21.333	−39.016	47.820	1.00	39.24	D000	C
ATOM	3606	CD2	TYR	C	181	−22.232	−39.065	50.032	1.00	37.86	D000	C
ATOM	3607	CE1	TYR	C	181	−22.574	−38.670	47.316	1.00	41.79	D000	C
ATOM	3608	CE2	TYR	C	181	−23.484	−38.716	49.534	1.00	30.18	D000	C
ATOM	3609	CZ	TYR	C	181	−23.643	−38.520	48.173	1.00	43.34	D000	C
ATOM	3610	OH	TYR	C	181	−24.868	−38.175	47.654	1.00	43.72	D000	O
ATOM	3611	N	CYS	C	182	−18.617	−41.321	47.379	1.00	32.27	D000	N
ATOM	3612	CA	CYS	C	182	−18.688	−41.720	45.977	1.00	33.21	D000	C
ATOM	3613	C	CYS	C	182	−18.666	−43.240	45.819	1.00	36.35	D000	C
ATOM	3614	O	CYS	C	182	−19.433	−43.793	45.032	1.00	28.20	D000	O
ATOM	3615	CB	CYS	C	182	−17.550	−41.079	45.177	1.00	33.72	D000	C
ATOM	3616	SG	CYS	C	182	−17.775	−39.294	44.910	1.00	35.82	D000	S
ATOM	3617	N	ARG	C	183	−17.798	−43.911	46.573	1.00	38.71	D000	N
ATOM	3618	CA	ARG	C	183	−17.731	−45.373	46.546	1.00	38.40	D000	C
ATOM	3619	C	ARG	C	183	−19.071	−45.997	46.942	1.00	41.03	D000	C
ATOM	3620	O	ARG	C	183	−19.466	−47.030	46.409	1.00	42.99	D000	O
ATOM	3621	CB	ARG	C	183	−16.621	−45.880	47.473	1.00	39.02	D000	C
ATOM	3622	CG	ARG	C	183	−15.217	−45.538	47.002	1.00	46.96	D000	C
ATOM	3623	CD	ARG	C	183	−14.169	−45.992	48.007	1.00	60.57	D000	C
ATOM	3624	NE	ARG	C	183	−12.816	−45.655	47.570	1.00	80.77	D000	N
ATOM	3625	CZ	ARG	C	183	−11.722	−45.845	48.301	1.00	85.00	D000	C
ATOM	3626	NH1	ARG	C	183	−11.814	−46.372	49.516	1.00	72.80	D000	N
ATOM	3627	NH2	ARG	C	183	−10.532	−45.505	47.818	1.00	88.26	D000	N
ATOM	3628	N	LEU	C	184	−19.769	−45.348	47.869	1.00	38.52	D000	N
ATOM	3629	CA	LEU	C	184	−21.063	−45.822	48.348	1.00	45.53	D000	C
ATOM	3630	C	LEU	C	184	−22.165	−45.627	47.305	1.00	44.46	D000	C
ATOM	3631	O	LEU	C	184	−23.192	−46.300	47.344	1.00	49.42	D000	O
ATOM	3632	CB	LEU	C	184	−21.436	−45.110	49.656	1.00	38.94	D000	C
ATOM	3633	CG	LEU	C	184	−21.111	−45.837	50.967	1.00	47.53	D000	C
ATOM	3634	CD1	LEU	C	184	−19.766	−46.545	50.898	1.00	51.14	D000	C
ATOM	3635	CD2	LEU	C	184	−21.138	−44.869	52.138	1.00	42.20	D000	C
ATOM	3636	N	GLU	C	185	−21.953	−44.701	46.376	1.00	42.20	D000	N
ATOM	3637	CA	GLU	C	185	−22.903	−44.483	45.288	1.00	39.20	D000	C
ATOM	3638	C	GLU	C	185	−22.504	−45.293	44.056	1.00	40.02	D000	C
ATOM	3639	O	GLU	C	185	−22.992	−45.040	42.954	1.00	41.00	D000	O
ATOM	3640	CB	GLU	C	185	−22.991	−42.997	44.936	1.00	43.28	D000	C
ATOM	3641	CG	GLU	C	185	−23.645	−42.139	46.005	1.00	50.04	D000	C
ATOM	3642	CD	GLU	C	185	−25.132	−42.410	46.144	1.00	63.83	D000	C
ATOM	3643	OE1	GLU	C	185	−25.853	−42.327	45.125	1.00	64.40	D000	O
ATOM	3644	OE2	GLU	C	185	−25.578	−42.711	47.274	1.00	66.65	D000	O
ATOM	3645	N	ASP	C	186	−21.618	−46.266	44.266	1.00	39.71	D000	N
ATOM	3646	CA	ASP	C	186	−21.073	−47.104	43.197	1.00	46.14	D000	C
ATOM	3647	C	ASP	C	186	−20.374	−46.235	42.149	1.00	46.36	D000	C
ATOM	3648	O	ASP	C	186	−20.472	−46.469	40.940	1.00	37.33	D000	O
ATOM	3649	CB	ASP	C	186	−22.172	−47.957	42.555	1.00	48.03	D000	C
ATOM	3650	CG	ASP	C	186	−21.616	−49.072	41.689	1.00	57.58	D000	C
ATOM	3651	OD1	ASP	C	186	−20.621	−49.705	42.104	1.00	69.48	D000	O
ATOM	3652	OD2	ASP	C	186	−22.167	−49.306	40.592	1.00	63.55	D000	O
ATOM	3653	N	ALA	C	187	−19.667	−45.222	42.634	1.00	37.49	D000	N
ATOM	3654	CA	ALA	C	187	−18.974	−44.291	41.763	1.00	36.04	D000	C
ATOM	3655	C	ALA	C	187	−17.592	−43.992	42.322	1.00	37.13	D000	C
ATOM	3656	O	ALA	C	187	−17.086	−44.715	43.183	1.00	35.71	D000	O
ATOM	3657	CB	ALA	C	187	−19.784	−43.005	41.603	1.00	29.96	D000	C
ATOM	3658	N	HIS	C	188	−16.981	−42.924	41.826	1.00	31.72	D000	N
ATOM	3659	CA	HIS	C	188	−15.693	−42.486	42.332	1.00	29.40	D000	C
ATOM	3660	C	HIS	C	188	−15.569	−40.982	42.157	1.00	28.01	D000	C
ATOM	3661	O	HIS	C	188	−16.263	−40.391	41.329	1.00	26.39	D000	O
ATOM	3662	CB	HIS	C	188	−14.556	−43.211	41.618	1.00	23.87	D000	C
ATOM	3663	CG	HIS	C	188	−14.541	−43.002	40.137	1.00	35.80	D000	C
ATOM	3664	CD2	HIS	C	188	−14.996	−43.776	39.123	1.00	32.29	D000	C
ATOM	3665	ND1	HIS	C	188	−14.009	−41.874	39.548	1.00	32.82	D000	N
ATOM	3666	CE1	HIS	C	188	−14.134	−41.964	38.236	1.00	33.00	D000	C
ATOM	3667	NE2	HIS	C	188	−14.729	−43.109	37.951	1.00	33.93	D000	N
ATOM	3668	N	LEU	C	189	−14.708	−40.364	42.958	1.00	26.16	D000	N
ATOM	3669	CA	LEU	C	189	−14.400	−38.950	42.784	1.00	28.90	D000	C
ATOM	3670	C	LEU	C	189	−13.909	−38.716	41.362	1.00	29.00	D000	C
ATOM	3671	O	LEU	C	189	−13.176	−39.541	40.805	1.00	27.16	D000	O
ATOM	3672	CB	LEU	C	189	−13.356	−38.488	43.796	1.00	26.67	D000	C
ATOM	3673	CG	LEU	C	189	−13.882	−38.242	45.208	1.00	33.12	D000	C
ATOM	3674	CD1	LEU	C	189	−12.735	−37.973	46.169	1.00	33.71	D000	C
ATOM	3675	CD2	LEU	C	189	−14.857	−37.076	45.186	1.00	27.90	D000	C
ATOM	3676	N	VAL	C	190	−14.320	−37.592	40.786	1.00	27.74	D000	N
ATOM	3677	CA	VAL	C	190	−14.117	−37.333	39.365	1.00	27.15	D000	C
ATOM	3678	C	VAL	C	190	−12.644	−37.428	38.968	1.00	29.08	D000	C
ATOM	3679	O	VAL	C	190	−11.743	−36.982	39.690	1.00	26.29	D000	O
ATOM	3680	CB	VAL	C	190	−14.699	−35.946	38.957	1.00	29.42	D000	C
ATOM	3681	CG1	VAL	C	190	−13.956	−34.796	39.654	1.00	25.30	D000	C
ATOM	3682	CG2	VAL	C	190	−14.705	−35.779	37.434	1.00	23.06	D000	C
ATOM	3683	N	VAL	C	191	−12.420	−38.079	37.834	1.00	26.83	D000	N
ATOM	3684	CA	VAL	C	191	−11.106	−38.192	37.221	1.00	30.57	D000	C
ATOM	3685	C	VAL	C	191	−11.136	−37.388	35.927	1.00	28.23	D000	C
ATOM	3686	O	VAL	C	191	−12.017	−37.590	35.096	1.00	26.03	D000	O
ATOM	3687	CB	VAL	C	191	−10.739	−39.664	36.942	1.00	28.44	D000	C
ATOM	3688	CG1	VAL	C	191	−9.433	−39.763	36.170	1.00	25.60	D000	C
ATOM	3689	CG2	VAL	C	191	−10.663	−40.445	38.256	1.00	26.79	D000	C
ATOM	3690	N	VAL	C	192	−10.200	−36.457	35.770	1.00	28.93	D000	N
ATOM	3691	CA	VAL	C	192	−10.224	−35.550	34.629	1.00	27.42	D000	C
ATOM	3692	C	VAL	C	192	−9.181	−35.963	33.602	1.00	31.88	D000	C
ATOM	3693	O	VAL	C	192	−7.984	−35.957	33.888	1.00	27.55	D000	O
ATOM	3694	CB	VAL	C	192	−9.979	−34.094	35.061	1.00	23.02	D000	C
ATOM	3695	CG1	VAL	C	192	−10.008	−33.170	33.851	1.00	23.08	D000	C
ATOM	3696	CG2	VAL	C	192	−11.017	−33.670	36.085	1.00	21.27	D000	C
ATOM	3697	N	THR	C	193	−9.637	−36.314	32.403	1.00	25.64	D000	N
ATOM	3698	CA	THR	C	193	−8.751	−36.918	31.415	1.00	32.64	D000	C
ATOM	3699	C	THR	C	193	−8.608	−36.120	30.125	1.00	31.08	D000	C
ATOM	3700	O	THR	C	193	−7.920	−36.558	29.206	1.00	30.10	D000	O
ATOM	3701	CB	THR	C	193	−9.223	−38.333	31.040	1.00	33.34	D000	C
ATOM	3702	CG2	THR	C	193	−9.327	−39.208	32.285	1.00	32.24	D000	C
ATOM	3703	OG1	THR	C	193	−10.501	−38.252	30.398	1.00	34.27	D000	O
ATOM	3704	N	SER	C	194	−9.247	−34.958	30.049	1.00	29.11	D000	N
ATOM	3705	CA	SER	C	194	−9.115	−34.111	28.866	1.00	29.77	D000	C
ATOM	3706	C	SER	C	194	−9.525	−32.671	29.159	1.00	29.25	D000	C
ATOM	3707	O	SER	C	194	−10.227	−32.400	30.137	1.00	23.94	D000	O
ATOM	3708	CB	SER	C	194	−9.956	−34.663	27.708	1.00	25.83	D000	C
ATOM	3709	OG	SER	C	194	−11.335	−34.423	27.935	1.00	28.83	D000	O
ATOM	3710	N	TRP	C	195	−9.080	−31.753	28.305	1.00	28.44	D000	N
ATOM	3711	CA	TRP	C	195	−9.456	−30.343	28.409	1.00	29.60	D000	C
ATOM	3712	C	TRP	C	195	−10.972	−30.177	28.304	1.00	25.02	D000	C
ATOM	3713	O	TRP	C	195	−11.553	−29.331	28.974	1.00	29.97	D000	O
ATOM	3714	CB	TRP	C	195	−8.737	−29.531	27.323	1.00	26.47	D000	C
ATOM	3715	CG	TRP	C	195	−9.010	−28.039	27.283	1.00	32.42	D000	C
ATOM	3716	CD1	TRP	C	195	−9.356	−27.306	26.181	1.00	34.68	D000	C
ATOM	3717	CD2	TRP	C	195	−8.932	−27.101	28.375	1.00	30.83	D000	C
ATOM	3718	CE2	TRP	C	195	−9.245	−25.827	27.853	1.00	34.03	D000	C
ATOM	3719	CE3	TRP	C	195	−8.631	−27.215	29.736	1.00	30.71	D000	C
ATOM	3720	NE1	TRP	C	195	−9.498	−25.981	26.515	1.00	32.39	D000	N
ATOM	3721	CZ2	TRP	C	195	−9.271	−24.678	28.645	1.00	31.06	D000	C
ATOM	3722	CZ3	TRP	C	195	−8.655	−26.071	30.523	1.00	32.95	D000	C
ATOM	3723	CH2	TRP	C	195	−8.969	−24.820	29.974	1.00	30.07	D000	C
ATOM	3724	N	GLU	C	196	−11.607	−30.999	27.471	1.00	26.97	D000	N
ATOM	3725	CA	GLU	C	196	−13.060	−30.960	27.306	1.00	30.42	D000	C
ATOM	3726	C	GLU	C	196	−13.794	−31.365	28.580	1.00	34.02	D000	C
ATOM	3727	O	GLU	C	196	−14.802	−30.757	28.943	1.00	28.31	D000	O
ATOM	3728	CB	GLU	C	196	−13.505	−31.871	26.158	1.00	30.46	D000	C
ATOM	3729	CG	GLU	C	196	−13.221	−31.329	24.769	1.00	41.10	D000	C
ATOM	3730	CD	GLU	C	196	−11.772	−31.498	24.353	1.00	46.52	D000	C
ATOM	3731	OE1	GLU	C	196	−11.002	−32.155	25.092	1.00	42.32	D000	O
ATOM	3732	OE2	GLU	C	196	−11.406	−30.973	23.281	1.00	46.49	D000	O
ATOM	3733	N	GLU	C	197	−13.297	−32.404	29.245	1.00	29.50	D000	N
ATOM	3734	CA	GLU	C	197	−13.899	−32.854	30.489	1.00	26.78	D000	C
ATOM	3735	C	GLU	C	197	−13.708	−31.790	31.574	1.00	26.09	D000	C
ATOM	3736	O	GLU	C	197	−14.631	−31.493	32.329	1.00	27.28	D000	O
ATOM	3737	CB	GLU	C	197	−13.305	−34.198	30.930	1.00	26.61	D000	C
ATOM	3738	CG	GLU	C	197	−14.055	−34.841	32.100	1.00	27.35	D000	C
ATOM	3739	CD	GLU	C	197	−13.518	−36.215	32.488	1.00	37.87	D000	C
ATOM	3740	OE1	GLU	C	197	−12.434	−36.602	32.003	1.00	33.97	D000	O
ATOM	3741	OE2	GLU	C	197	−14.187	−36.910	33.285	1.00	39.22	D000	O
ATOM	3742	N	GLN	C	198	−12.514	−31.205	31.629	1.00	25.72	D000	N
ATOM	3743	CA	GLN	C	198	−12.214	−30.140	32.588	1.00	25.80	D000	C
ATOM	3744	C	GLN	C	198	−13.189	−28.975	32.463	1.00	29.00	D000	C
ATOM	3745	O	GLN	C	198	−13.685	−28.458	33.464	1.00	24.52	D000	O
ATOM	3746	CB	GLN	C	198	−10.783	−29.632	32.394	1.00	23.78	D000	C
ATOM	3747	CG	GLN	C	198	−10.506	−28.288	33.045	1.00	25.75	D000	C
ATOM	3748	CD	GLN	C	198	−10.246	−28.397	34.537	1.00	33.71	D000	C
ATOM	3749	NE2	GLN	C	198	−10.599	−27.350	35.279	1.00	25.10	D000	N
ATOM	3750	OE1	GLN	C	198	−9.734	−29.410	35.017	1.00	28.06	D000	O
ATOM	3751	N	LYS	C	199	−13.466	−28.574	31.226	1.00	30.60	D000	N
ATOM	3752	CA	LYS	C	199	−14.326	−27.424	30.974	1.00	34.08	D000	C
ATOM	3753	C	LYS	C	199	−15.770	−27.743	31.319	1.00	28.60	D000	C
ATOM	3754	O	LYS	C	199	−16.489	−26.895	31.848	1.00	25.57	D000	O
ATOM	3755	CB	LYS	C	199	−14.212	−26.978	29.517	1.00	28.25	D000	C
ATOM	3756	CG	LYS	C	199	−12.855	−26.386	29.183	1.00	34.79	D000	C
ATOM	3757	CD	LYS	C	199	−12.532	−26.545	27.711	1.00	43.54	D000	C
ATOM	3758	CE	LYS	C	199	−13.150	−25.447	26.892	1.00	38.89	D000	C
ATOM	3759	NZ	LYS	C	199	−12.740	−25.539	25.453	1.00	35.02	D000	N
ATOM	3760	N	PHE	C	200	−16.188	−28.968	31.013	1.00	29.54	D000	N
ATOM	3761	CA	PHE	C	200	−17.515	−29.436	31.393	1.00	30.79	D000	C
ATOM	3762	C	PHE	C	200	−17.682	−29.381	32.909	1.00	25.62	D000	C
ATOM	3763	O	PHE	C	200	−18.651	−28.807	33.414	1.00	25.66	D000	O
ATOM	3764	CB	PHE	C	200	−17.762	−30.861	30.891	1.00	27.79	D000	C
ATOM	3765	CG	PHE	C	200	−18.939	−31.530	31.541	1.00	33.05	D000	C
ATOM	3766	CD1	PHE	C	200	−20.230	−31.216	31.154	1.00	29.57	D000	C
ATOM	3767	CD2	PHE	C	200	−18.754	−32.467	32.547	1.00	33.93	D000	C
ATOM	3768	CE1	PHE	C	200	−21.315	−31.826	31.753	1.00	31.19	D000	C
ATOM	3769	CE2	PHE	C	200	−19.837	−33.077	33.154	1.00	30.44	D000	C
ATOM	3770	CZ	PHE	C	200	−21.118	−32.756	32.755	1.00	33.80	D000	C
ATOM	3771	N	VAL	C	201	−16.730	−29.971	33.627	1.00	27.40	D000	N
ATOM	3772	CA	VAL	C	201	−16.756	−29.964	35.088	1.00	26.65	D000	C
ATOM	3773	C	VAL	C	201	−16.750	−28.533	35.609	1.00	33.34	D000	C
ATOM	3774	O	VAL	C	201	−17.593	−28.149	36.428	1.00	25.82	D000	O
ATOM	3775	CB	VAL	C	201	−15.557	−30.727	35.679	1.00	30.52	D000	C
ATOM	3776	CG1	VAL	C	201	−15.448	−30.466	37.173	1.00	27.81	D000	C
ATOM	3777	CG2	VAL	C	201	−15.677	−32.219	35.392	1.00	24.80	D000	C
ATOM	3778	N	GLN	C	202	−15.804	−27.748	35.098	1.00	28.75	D000	N
ATOM	3779	CA	GLN	C	202	−15.629	−26.353	35.482	1.00	28.03	D000	C
ATOM	3780	C	GLN	C	202	−16.905	−25.544	35.295	1.00	26.50	D000	C
ATOM	3781	O	GLN	C	202	−17.221	−24.662	36.097	1.00	30.81	D000	O
ATOM	3782	CB	GLN	C	202	−14.495	−25.736	34.663	1.00	28.31	D000	C
ATOM	3783	CG	GLN	C	202	−13.779	−24.603	35.333	1.00	34.63	D000	C
ATOM	3784	CD	GLN	C	202	−12.592	−24.127	34.524	1.00	36.40	D000	C
ATOM	3785	NE2	GLN	C	202	−12.382	−22.815	34.494	1.00	34.64	D000	N
ATOM	3786	OE1	GLN	C	202	−11.874	−24.931	33.924	1.00	33.68	D000	O
ATOM	3787	N	HIS	C	203	−17.640	−25.848	34.232	1.00	28.19	D000	N
ATOM	3788	CA	HIS	C	203	−18.895	−25.158	33.971	1.00	28.76	D000	C
ATOM	3789	C	HIS	C	203	−19.921	−25.389	35.081	1.00	37.82	D000	C
ATOM	3790	O	HIS	C	203	−20.664	−24.477	35.450	1.00	30.91	D000	O
ATOM	3791	CB	HIS	C	203	−19.490	−25.597	32.633	1.00	27.45	D000	C
ATOM	3792	CG	HIS	C	203	−20.836	−25.002	32.361	1.00	35.85	D000	C
ATOM	3793	CD2	HIS	C	203	−21.189	−23.825	31.791	1.00	40.47	D000	C
ATOM	3794	ND1	HIS	C	203	−22.010	−25.619	32.728	1.00	42.36	D000	N
ATOM	3795	CE1	HIS	C	203	−23.035	−24.857	32.380	1.00	38.39	D000	C
ATOM	3796	NE2	HIS	C	203	−22.561	−23.764	31.810	1.00	42.37	D000	N
ATOM	3797	N	HIS	C	204	−19.970	−26.608	35.612	1.00	31.47	D000	N
ATOM	3798	CA	HIS	C	204	−20.992	−26.941	36.602	1.00	30.96	D000	C
ATOM	3799	C	HIS	C	204	−20.619	−26.543	38.023	1.00	29.48	D000	C
ATOM	3800	O	HIS	C	204	−21.489	−26.143	38.796	1.00	28.82	D000	O
ATOM	3801	CB	HIS	C	204	−21.317	−28.434	36.545	1.00	30.72	D000	C
ATOM	3802	CG	HIS	C	204	−22.172	−28.808	35.376	1.00	31.65	D000	C
ATOM	3803	CD2	HIS	C	204	−21.889	−29.495	34.244	1.00	34.41	D000	C
ATOM	3804	ND1	HIS	C	204	−23.494	−28.433	35.274	1.00	39.82	D000	N
ATOM	3805	CE1	HIS	C	204	−23.993	−28.884	34.138	1.00	35.14	D000	C
ATOM	3806	NE2	HIS	C	204	−23.038	−29.531	33.493	1.00	39.82	D000	N
ATOM	3807	N	ILE	C	205	−19.340	−26.628	38.375	1.00	26.45	D000	N
ATOM	3808	CA	ILE	C	205	−18.942	−26.275	39.735	1.00	32.57	D000	C
ATOM	3809	C	ILE	C	205	−18.811	−24.758	39.911	1.00	29.31	D000	C
ATOM	3810	O	ILE	C	205	−18.976	−24.244	41.015	1.00	30.32	D000	O
ATOM	3811	CB	ILE	C	205	−17.613	−26.955	40.152	1.00	31.86	D000	C
ATOM	3812	CG1	ILE	C	205	−16.437	−26.421	39.339	1.00	31.34	D000	C
ATOM	3813	CG2	ILE	C	205	−17.710	−28.477	40.014	1.00	29.23	D000	C
ATOM	3814	CD1	ILE	C	205	−15.107	−26.968	39.802	1.00	32.36	D000	C
ATOM	3815	N	GLY	C	206	−18.540	−24.043	38.825	1.00	24.89	D000	N
ATOM	3816	CA	GLY	C	206	−18.307	−22.613	38.912	1.00	26.12	D000	C
ATOM	3817	C	GLY	C	206	−17.033	−22.318	39.688	1.00	33.16	D000	C
ATOM	3818	O	GLY	C	206	−16.182	−23.197	39.845	1.00	27.62	D000	O
ATOM	3819	N	PRO	C	207	−16.895	−21.081	40.189	1.00	27.47	D000	N
ATOM	3820	CA	PRO	C	207	−15.679	−20.657	40.895	1.00	28.28	D000	C
ATOM	3821	C	PRO	C	207	−15.651	−21.107	42.360	1.00	33.47	D000	C
ATOM	3822	O	PRO	C	207	−15.598	−20.266	43.255	1.00	30.13	D000	O
ATOM	3823	CB	PRO	C	207	−15.741	−19.130	40.792	1.00	27.65	D000	C
ATOM	3824	CG	PRO	C	207	−17.204	−18.830	40.787	1.00	30.21	D000	C
ATOM	3825	CD	PRO	C	207	−17.873	−19.984	40.065	1.00	29.69	D000	C
ATOM	3826	N	VAL	C	208	−15.674	−22.417	42.594	1.00	36.48	D000	N
ATOM	3827	CA	VAL	C	208	−15.803	−22.969	43.944	1.00	29.83	D000	C
ATOM	3828	C	VAL	C	208	−14.809	−24.105	44.182	1.00	33.04	D000	C
ATOM	3829	O	VAL	C	208	−14.697	−25.001	43.351	1.00	26.89	D000	O
ATOM	3830	CB	VAL	C	208	−17.233	−23.504	44.191	1.00	35.14	D000	C
ATOM	3831	CG1	VAL	C	208	−17.349	−24.108	45.585	1.00	33.92	D000	C
ATOM	3832	CG2	VAL	C	208	−18.271	−22.402	43.981	1.00	32.86	D000	C
ATOM	3833	N	ASN	C	209	−14.092	−24.071	45.306	1.00	30.99	D000	N
ATOM	3834	CA	ASN	C	209	−13.164	−25.153	45.649	1.00	31.35	D000	C
ATOM	3835	C	ASN	C	209	−13.881	−26.500	45.682	1.00	32.29	D000	C
ATOM	3836	O	ASN	C	209	−14.881	−26.666	46.379	1.00	29.08	D000	O
ATOM	3837	CB	ASN	C	209	−12.486	−24.895	46.994	1.00	25.98	D000	C
ATOM	3838	CG	ASN	C	209	−11.461	−23.781	46.931	1.00	30.97	D000	C
ATOM	3839	ND2	ASN	C	209	−11.376	−22.997	48.000	1.00	35.10	D000	N
ATOM	3840	OD1	ASN	C	209	−10.750	−23.626	45.938	1.00	30.97	D000	O
ATOM	3841	N	THR	C	210	−13.363	−27.457	44.919	1.00	30.16	D000	N
ATOM	3842	CA	THR	C	210	−14.049	−28.725	44.705	1.00	26.80	D000	C
ATOM	3843	C	THR	C	210	−13.049	−29.865	44.549	1.00	26.68	D000	C
ATOM	3844	O	THR	C	210	−12.182	−29.822	43.673	1.00	30.56	D000	O
ATOM	3845	CB	THR	C	210	−14.949	−28.655	43.456	1.00	29.42	D000	C
ATOM	3846	CG2	THR	C	210	−15.785	−29.916	43.312	1.00	22.22	D000	C
ATOM	3847	OG1	THR	C	210	−15.813	−27.515	43.556	1.00	26.16	D000	O
ATOM	3848	N	TRP	C	211	−13.165	−30.872	45.410	1.00	25.09	D000	N
ATOM	3849	CA	TRP	C	211	−12.294	−32.041	45.357	1.00	30.07	D000	C
ATOM	3850	C	TRP	C	211	−12.423	−32.796	44.038	1.00	36.81	D000	C
ATOM	3851	O	TRP	C	211	−13.510	−32.874	43.456	1.00	27.60	D000	O
ATOM	3852	CB	TRP	C	211	−12.605	−33.013	46.501	1.00	27.04	D000	C
ATOM	3853	CG	TRP	C	211	−12.261	−32.549	47.900	1.00	28.12	D000	C
ATOM	3854	CD1	TRP	C	211	−13.097	−32.529	48.983	1.00	28.01	D000	C
ATOM	3855	CD2	TRP	C	211	−10.991	−32.072	48.366	1.00	26.23	D000	C
ATOM	3856	CE2	TRP	C	211	−11.136	−31.771	49.739	1.00	31.66	D000	C
ATOM	3857	CE3	TRP	C	211	−9.751	−31.857	47.756	1.00	23.53	D000	C
ATOM	3858	NE1	TRP	C	211	−12.428	−32.060	50.091	1.00	29.06	D000	N
ATOM	3859	CZ2	TRP	C	211	−10.084	−31.274	50.509	1.00	31.81	D000	C
ATOM	3860	CZ3	TRP	C	211	−8.709	−31.361	48.522	1.00	26.50	D000	C
ATOM	3861	CH2	TRP	C	211	−8.881	−31.078	49.885	1.00	32.71	D000	C
ATOM	3862	N	MET	C	212	−11.310	−33.363	43.585	1.00	29.78	D000	N
ATOM	3863	CA	MET	C	212	−11.327	−34.332	42.500	1.00	26.98	D000	C
ATOM	3864	C	MET	C	212	−10.681	−35.620	43.009	1.00	30.71	D000	C
ATOM	3865	O	MET	C	212	−10.179	−35.655	44.134	1.00	26.90	D000	O
ATOM	3866	CB	MET	C	212	−10.598	−33.793	41.266	1.00	28.53	D000	C
ATOM	3867	CG	MET	C	212	−9.082	−33.872	41.344	1.00	27.04	D000	C
ATOM	3868	SD	MET	C	212	−8.287	−32.882	40.061	1.00	30.51	D000	S
ATOM	3869	CE	MET	C	212	−8.761	−31.231	40.597	1.00	22.33	D000	C
ATOM	3870	N	GLY	C	213	−10.693	−36.673	42.195	1.00	23.24	D000	N
ATOM	3871	CA	GLY	C	213	−10.149	−37.955	42.612	1.00	21.72	D000	C
ATOM	3872	C	GLY	C	213	−8.655	−38.108	42.405	1.00	27.75	D000	C
ATOM	3873	O	GLY	C	213	−8.199	−39.106	41.851	1.00	28.41	D000	O
ATOM	3874	N	LEU	C	214	−7.891	−37.124	42.870	1.00	25.92	D000	N
ATOM	3875	CA	LEU	C	214	−6.443	−37.109	42.691	1.00	26.73	D000	C
ATOM	3876	C	LEU	C	214	−5.755	−36.799	44.018	1.00	25.75	D000	C
ATOM	3877	O	LEU	C	214	−6.073	−35.802	44.659	1.00	25.95	D000	O
ATOM	3878	CB	LEU	C	214	−6.049	−36.076	41.629	1.00	24.90	D000	C
ATOM	3879	CG	LEU	C	214	−4.566	−35.777	41.383	1.00	25.82	D000	C
ATOM	3880	CD1	LEU	C	214	−3.840	−37.006	40.861	1.00	22.24	D000	C
ATOM	3881	CD2	LEU	C	214	−4.428	−34.615	40.402	1.00	20.00	D000	C
ATOM	3882	N	HIS	C	215	−4.819	−37.653	44.426	1.00	28.82	D000	N
ATOM	3883	CA	HIS	C	215	−4.139	−37.488	45.709	1.00	25.47	D000	C
ATOM	3884	C	HIS	C	215	−2.797	−38.207	45.727	1.00	27.39	D000	C
ATOM	3885	O	HIS	C	215	−2.570	−39.123	44.938	1.00	28.76	D000	O
ATOM	3886	CB	HIS	C	215	−5.011	−38.011	46.850	1.00	25.17	D000	C
ATOM	3887	CG	HIS	C	215	−5.082	−39.505	46.915	1.00	33.85	D000	C
ATOM	3888	CD2	HIS	C	215	−5.484	−40.419	45.999	1.00	36.27	D000	C
ATOM	3889	ND1	HIS	C	215	−4.705	−40.221	48.030	1.00	43.52	D000	N
ATOM	3890	CE1	HIS	C	215	−4.874	−41.511	47.800	1.00	45.66	D000	C
ATOM	3891	NE2	HIS	C	215	−5.347	−41.657	46.575	1.00	38.89	D000	N
ATOM	3892	N	ASP	C	216	−1.908	−37.803	46.632	1.00	31.91	D000	N
ATOM	3893	CA	ASP	C	216	−0.623	−38.485	46.760	1.00	28.17	D000	C
ATOM	3894	C	ASP	C	216	−0.369	−38.944	48.199	1.00	35.16	D000	C
ATOM	3895	O	ASP	C	216	0.764	−38.955	48.668	1.00	31.36	D000	O
ATOM	3896	CB	ASP	C	216	0.518	−37.585	46.258	1.00	28.42	D000	C
ATOM	3897	CG	ASP	C	216	0.795	−36.394	47.171	1.00	35.01	D000	C
ATOM	3898	OD1	ASP	C	216	0.013	−36.142	48.110	1.00	28.86	D000	O
ATOM	3899	OD2	ASP	C	216	1.805	−35.695	46.936	1.00	31.47	D000	O
ATOM	3900	N	GLN	C	217	−1.432	−39.332	48.894	1.00	31.06	D000	N
ATOM	3901	CA	GLN	C	217	−1.305	−39.781	50.278	1.00	41.47	D000	C
ATOM	3902	C	GLN	C	217	−0.531	−41.103	50.385	1.00	38.57	D000	C
ATOM	3903	O	GLN	C	217	0.157	−41.346	51.374	1.00	44.82	D000	O
ATOM	3904	CB	GLN	C	217	−2.688	−39.926	50.918	1.00	37.52	D000	C
ATOM	3905	CG	GLN	C	217	−3.504	−38.644	50.919	1.00	33.20	D000	C
ATOM	3906	CD	GLN	C	217	−4.837	−38.799	51.626	1.00	39.32	D000	C
ATOM	3907	NE2	GLN	C	217	−5.810	−39.389	50.941	1.00	31.27	D000	N
ATOM	3908	OE1	GLN	C	217	−4.989	−38.391	52.775	1.00	48.65	D000	O
ATOM	3909	N	ASN	C	218	−0.630	−41.939	49.356	1.00	38.48	D000	N
ATOM	3910	CA	ASN	C	218	0.018	−43.251	49.363	1.00	53.29	D000	C
ATOM	3911	C	ASN	C	218	1.205	−43.357	48.405	1.00	47.43	D000	C
ATOM	3912	O	ASN	C	218	1.397	−44.389	47.761	1.00	58.53	D000	O
ATOM	3913	CB	ASN	C	218	−1.004	−44.339	49.018	1.00	57.61	D000	C
ATOM	3914	CG	ASN	C	218	−2.213	−44.313	49.933	1.00	65.75	D000	C
ATOM	3915	ND2	ASN	C	218	−1.966	−44.302	51.241	1.00	59.68	D000	N
ATOM	3916	OD1	ASN	C	218	−3.356	−44.293	49.471	1.00	59.70	D000	O
ATOM	3917	N	GLY	C	219	2.001	−42.299	48.313	1.00	35.56	D000	N
ATOM	3918	CA	GLY	C	219	3.081	−42.255	47.344	1.00	36.85	D000	C
ATOM	3919	C	GLY	C	219	2.873	−41.128	46.353	1.00	34.18	D000	C
ATOM	3920	O	GLY	C	219	2.347	−40.080	46.716	1.00	32.25	D000	O
ATOM	3921	N	PRO	C	220	3.284	−41.332	45.092	1.00	35.79	D000	N
ATOM	3922	CA	PRO	C	220	3.144	−40.284	44.072	1.00	33.07	D000	C
ATOM	3923	C	PRO	C	220	1.683	−40.001	43.728	1.00	31.10	D000	C
ATOM	3924	O	PRO	C	220	0.801	−40.767	44.117	1.00	29.49	D000	O
ATOM	3925	CB	PRO	C	220	3.897	−40.859	42.867	1.00	37.25	D000	C
ATOM	3926	CG	PRO	C	220	3.868	−42.336	43.073	1.00	41.99	D000	C
ATOM	3927	CD	PRO	C	220	3.925	−42.547	44.558	1.00	34.70	D000	C
ATOM	3928	N	TRP	C	221	1.433	−38.904	43.019	1.00	28.69	D000	N
ATOM	3929	CA	TRP	C	221	0.070	−38.514	42.668	1.00	29.66	D000	C
ATOM	3930	C	TRP	C	221	−0.626	−39.607	41.857	1.00	29.27	D000	C
ATOM	3931	O	TRP	C	221	−0.081	−40.110	40.879	1.00	26.36	D000	O
ATOM	3932	CB	TRP	C	221	0.075	−37.185	41.900	1.00	27.58	D000	C
ATOM	3933	CG	TRP	C	221	0.406	−36.020	42.782	1.00	30.86	D000	C
ATOM	3934	CD1	TRP	C	221	1.629	−35.437	42.947	1.00	32.27	D000	C
ATOM	3935	CD2	TRP	C	221	−0.495	−35.311	43.643	1.00	27.75	D000	C
ATOM	3936	CE2	TRP	C	221	0.253	−34.309	44.298	1.00	32.54	D000	C
ATOM	3937	CE3	TRP	C	221	−1.861	−35.428	43.926	1.00	25.76	D000	C
ATOM	3938	NE1	TRP	C	221	1.545	−34.406	43.853	1.00	32.24	D000	N
ATOM	3939	CZ2	TRP	C	221	−0.320	−33.425	45.219	1.00	27.09	D000	C
ATOM	3940	CZ3	TRP	C	221	−2.430	−34.549	44.841	1.00	29.33	D000	C
ATOM	3941	CH2	TRP	C	221	−1.658	−33.560	45.474	1.00	29.04	D000	C
ATOM	3942	N	LYS	C	222	−1.826	−39.981	42.289	1.00	30.12	D000	N
ATOM	3943	CA	LYS	C	222	−2.585	−41.046	41.643	1.00	30.34	D000	C
ATOM	3944	C	LYS	C	222	−4.058	−40.687	41.502	1.00	27.82	D000	C
ATOM	3945	O	LYS	C	222	−4.627	−40.026	42.370	1.00	29.51	D000	O
ATOM	3946	CB	LYS	C	222	−2.453	−42.351	42.436	1.00	35.42	D000	C
ATOM	3947	CG	LYS	C	222	−1.072	−42.983	42.388	1.00	42.04	D000	C
ATOM	3948	CD	LYS	C	222	−0.966	−44.138	43.373	1.00	62.76	D000	C
ATOM	3949	CE	LYS	C	222	0.452	−44.687	43.443	1.00	66.16	D000	C
ATOM	3950	NZ	LYS	C	222	0.599	−45.699	44.533	1.00	72.02	D000	N
ATOM	3951	N	TRP	C	223	−4.670	−41.121	40.406	1.00	29.14	D000	N
ATOM	3952	CA	TRP	C	223	−6.119	−41.022	40.249	1.00	31.28	D000	C
ATOM	3953	C	TRP	C	223	−6.787	−42.218	40.920	1.00	29.31	D000	C
ATOM	3954	O	TRP	C	223	−6.254	−43.321	40.883	1.00	30.17	D000	O
ATOM	3955	CB	TRP	C	223	−6.512	−40.959	38.774	1.00	23.94	D000	C
ATOM	3956	CG	TRP	C	223	−6.104	−39.694	38.085	1.00	27.95	D000	C
ATOM	3957	CD1	TRP	C	223	−5.059	−39.530	37.226	1.00	23.23	D000	C
ATOM	3958	CD2	TRP	C	223	−6.742	−38.414	38.191	1.00	24.93	D000	C
ATOM	3959	CE2	TRP	C	223	−6.026	−37.523	37.365	1.00	23.92	D000	C
ATOM	3960	CE3	TRP	C	223	−7.851	−37.938	38.901	1.00	23.92	D000	C
ATOM	3961	NE1	TRP	C	223	−5.002	−38.228	36.790	1.00	25.78	D000	N
ATOM	3962	CZ2	TRP	C	223	−6.382	−36.182	37.228	1.00	28.71	D000	C
ATOM	3963	CZ3	TRP	C	223	−8.201	−36.603	38.771	1.00	28.69	D000	C
ATOM	3964	CH2	TRP	C	223	−7.468	−35.740	37.941	1.00	27.80	D000	C
ATOM	3965	N	VAL	C	224	−7.958	−42.001	41.514	1.00	28.47	D000	N
ATOM	3966	CA	VAL	C	224	−8.620	−43.038	42.302	1.00	29.16	D000	C
ATOM	3967	C	VAL	C	224	−9.055	−44.259	41.486	1.00	31.96	D000	C
ATOM	3968	O	VAL	C	224	−9.186	−45.349	42.038	1.00	33.21	D000	O
ATOM	3969	CB	VAL	C	224	−9.866	−42.485	43.037	1.00	27.95	D000	C
ATOM	3970	CG1	VAL	C	224	−9.463	−41.450	44.071	1.00	29.62	D000	C
ATOM	3971	CG2	VAL	C	224	−10.863	−41.900	42.050	1.00	31.35	D000	C
ATOM	3972	N	ASP	C	225	−9.272	−44.083	40.184	1.00	30.51	D000	N
ATOM	3973	CA	ASP	C	225	−9.755	−45.182	39.347	1.00	33.42	D000	C
ATOM	3974	C	ASP	C	225	−8.622	−45.903	38.615	1.00	35.01	D000	C
ATOM	3975	O	ASP	C	225	−8.866	−46.705	37.717	1.00	45.07	D000	O
ATOM	3976	CB	ASP	C	225	−10.798	−44.673	38.337	1.00	34.24	D000	C
ATOM	3977	CG	ASP	C	225	−10.187	−43.849	37.205	1.00	39.60	D000	C
ATOM	3978	OD1	ASP	C	225	−9.032	−43.379	37.334	1.00	35.30	D000	O
ATOM	3979	OD2	ASP	C	225	−10.878	−43.658	36.179	1.00	41.15	D000	O
ATOM	3980	N	GLY	C	226	−7.383	−45.605	38.989	1.00	34.08	D000	N
ATOM	3981	CA	GLY	C	226	−6.241	−46.272	38.389	1.00	29.68	D000	C
ATOM	3982	C	GLY	C	226	−5.723	−45.631	37.115	1.00	34.65	D000	C
ATOM	3983	O	GLY	C	226	−4.725	−46.086	36.555	1.00	35.05	D000	O
ATOM	3984	N	THR	C	227	−6.394	−44.578	36.652	1.00	34.54	D000	N
ATOM	3985	CA	THR	C	227	−5.926	−43.829	35.486	1.00	32.36	D000	C
ATOM	3986	C	THR	C	227	−4.500	−43.333	35.721	1.00	35.82	D000	C
ATOM	3987	O	THR	C	227	−4.196	−42.779	36.779	1.00	36.25	D000	O
ATOM	3988	CB	THR	C	227	−6.840	−42.625	35.175	1.00	36.95	D000	C
ATOM	3989	CG2	THR	C	227	−6.315	−41.834	33.980	1.00	37.07	D000	C
ATOM	3990	OG1	THR	C	227	−8.164	−43.089	34.891	1.00	40.09	D000	O
ATOM	3991	N	ASP	C	228	−3.625	−43.540	34.743	1.00	35.21	D000	N
ATOM	3992	CA	ASP	C	228	−2.227	−43.165	34.900	1.00	35.66	D000	C
ATOM	3993	C	ASP	C	228	−2.063	−41.648	34.951	1.00	40.45	D000	C
ATOM	3994	O	ASP	C	228	−2.550	−40.926	34.080	1.00	33.72	D000	O
ATOM	3995	CB	ASP	C	228	−1.378	−43.748	33.773	1.00	36.06	D000	C
ATOM	3996	CG	ASP	C	228	0.098	−43.451	33.953	1.00	42.86	D000	C
ATOM	3997	OD1	ASP	C	228	0.720	−44.052	34.855	1.00	52.83	D000	O
ATOM	3998	OD2	ASP	C	228	0.636	−42.613	33.199	1.00	43.62	D000	O
ATOM	3999	N	TYR	C	229	−1.372	−41.168	35.978	1.00	34.02	D000	N
ATOM	4000	CA	TYR	C	229	−1.267	−39.735	36.202	1.00	35.25	D000	C
ATOM	4001	C	TYR	C	229	−0.210	−39.078	35.320	1.00	32.64	D000	C
ATOM	4002	O	TYR	C	229	−0.470	−38.045	34.713	1.00	32.76	D000	O
ATOM	4003	CB	TYR	C	229	−0.967	−39.448	37.676	1.00	34.94	D000	C
ATOM	4004	CG	TYR	C	229	−0.488	−38.039	37.936	1.00	31.42	D000	C
ATOM	4005	CD1	TYR	C	229	−1.381	−36.975	37.988	1.00	28.67	D000	C
ATOM	4006	CD2	TYR	C	229	0.860	−37.773	38.129	1.00	36.14	D000	C
ATOM	4007	CE1	TYR	C	229	−0.941	−35.684	38.220	1.00	24.57	D000	C
ATOM	4008	CE2	TYR	C	229	1.309	−36.493	38.366	1.00	33.76	D000	C
ATOM	4009	CZ	TYR	C	229	0.407	−35.452	38.412	1.00	34.92	D000	C
ATOM	4010	OH	TYR	C	229	0.869	−34.176	38.646	1.00	35.23	D000	O
ATOM	4011	N	GLU	C	230	0.973	−39.679	35.244	1.00	32.24	D000	N
ATOM	4012	CA	GLU	C	230	2.108	−39.042	34.578	1.00	40.08	D000	C
ATOM	4013	C	GLU	C	230	1.866	−38.810	33.086	1.00	34.17	D000	C
ATOM	4014	O	GLU	C	230	2.253	−37.777	32.545	1.00	32.51	D000	O
ATOM	4015	CB	GLU	C	230	3.381	−39.869	34.774	1.00	40.46	D000	C
ATOM	4016	CG	GLU	C	230	4.639	−39.157	34.302	1.00	62.30	D000	C
ATOM	4017	CD	GLU	C	230	5.913	−39.799	34.821	1.00	100.35	D000	C
ATOM	4018	OE1	GLU	C	230	5.824	−40.683	35.701	1.00	96.71	D000	O
ATOM	4019	OE2	GLU	C	230	7.006	−39.416	34.349	1.00	104.16	D000	O
ATOM	4020	N	THR	C	231	1.210	−39.760	32.428	1.00	32.37	D000	N
ATOM	4021	CA	THR	C	231	0.942	−39.638	31.001	1.00	35.98	D000	C
ATOM	4022	C	THR	C	231	−0.426	−39.018	30.742	1.00	40.00	D000	C
ATOM	4023	O	THR	C	231	−0.829	−38.837	29.593	1.00	34.33	D000	O
ATOM	4024	CB	THR	C	231	1.015	−41.005	30.291	1.00	45.18	D000	C
ATOM	4025	CG2	THR	C	231	2.392	−41.634	30.485	1.00	36.03	D000	C
ATOM	4026	OG1	THR	C	231	0.004	−41.878	30.813	1.00	40.41	D000	O
ATOM	4027	N	GLY	C	232	−1.135	−38.685	31.815	1.00	31.90	D000	N
ATOM	4028	CA	GLY	C	232	−2.478	−38.155	31.689	1.00	35.88	D000	C
ATOM	4029	C	GLY	C	232	−2.556	−36.641	31.641	1.00	31.67	D000	C
ATOM	4030	O	GLY	C	232	−1.569	−35.940	31.855	1.00	34.20	D000	O
ATOM	4031	N	PHE	C	233	−3.754	−36.148	31.351	1.00	34.66	D000	N
ATOM	4032	CA	PHE	C	233	−4.057	−34.723	31.357	1.00	30.10	D000	C
ATOM	4033	C	PHE	C	233	−3.792	−34.089	32.730	1.00	28.30	D000	C
ATOM	4034	O	PHE	C	233	−4.053	−34.702	33.766	1.00	31.59	D000	O
ATOM	4035	CB	PHE	C	233	−5.520	−34.520	30.932	1.00	29.82	D000	C
ATOM	4036	CG	PHE	C	233	−6.022	−33.115	31.094	1.00	33.74	D000	C
ATOM	4037	CD1	PHE	C	233	−5.829	−32.175	30.088	1.00	27.88	D000	C
ATOM	4038	CD2	PHE	C	233	−6.715	−32.739	32.240	1.00	24.62	D000	C
ATOM	4039	CE1	PHE	C	233	−6.298	−30.878	30.231	1.00	27.56	D000	C
ATOM	4040	CE2	PHE	C	233	−7.184	−31.441	32.389	1.00	32.64	D000	C
ATOM	4041	CZ	PHE	C	233	−6.975	−30.510	31.381	1.00	27.36	D000	C
ATOM	4042	N	LYS	C	234	−3.267	−32.866	32.730	1.00	29.76	D000	N
ATOM	4043	CA	LYS	C	234	−3.045	−32.109	33.963	1.00	29.48	D000	C
ATOM	4044	C	LYS	C	234	−3.455	−30.646	33.789	1.00	31.02	D000	C
ATOM	4045	O	LYS	C	234	−3.316	−30.077	32.704	1.00	25.86	D000	O
ATOM	4046	CB	LYS	C	234	−1.579	−32.189	34.397	1.00	32.09	D000	C
ATOM	4047	CG	LYS	C	234	−1.056	−33.603	34.611	1.00	30.92	D000	C
ATOM	4048	CD	LYS	C	234	0.422	−33.598	34.955	1.00	34.48	D000	C
ATOM	4049	CE	LYS	C	234	1.026	−34.993	34.843	1.00	34.77	D000	C
ATOM	4050	NZ	LYS	C	234	1.050	−35.479	33.432	1.00	34.51	D000	N
ATOM	4051	N	ASN	C	235	−3.957	−30.040	34.861	1.00	29.35	D000	N
ATOM	4052	CA	ASN	C	235	−4.382	−28.644	34.822	1.00	26.46	D000	C
ATOM	4053	C	ASN	C	235	−4.012	−27.912	36.116	1.00	26.48	D000	C
ATOM	4054	O	ASN	C	235	−4.814	−27.157	36.659	1.00	29.79	D000	O
ATOM	4055	CB	ASN	C	235	−5.896	−28.559	34.573	1.00	25.06	D000	C
ATOM	4056	CG	ASN	C	235	−6.345	−27.173	34.127	1.00	27.67	D000	C
ATOM	4057	ND2	ASN	C	235	−7.464	−26.705	34.673	1.00	26.28	D000	N
ATOM	4058	OD1	ASN	C	235	−5.692	−26.533	33.308	1.00	27.02	D000	O
ATOM	4059	N	TRP	C	236	−2.795	−28.145	36.607	1.00	27.50	D000	N
ATOM	4060	CA	TRP	C	236	−2.325	−27.526	37.850	1.00	27.74	D000	C
ATOM	4061	C	TRP	C	236	−2.206	−26.010	37.747	1.00	27.99	D000	C
ATOM	4062	O	TRP	C	236	−1.870	−25.474	36.690	1.00	31.33	D000	O
ATOM	4063	CB	TRP	C	236	−0.960	−28.092	38.264	1.00	23.47	D000	C
ATOM	4064	CG	TRP	C	236	−0.967	−29.533	38.710	1.00	24.40	D000	C
ATOM	4065	CD1	TRP	C	236	−0.544	−30.616	37.990	1.00	25.63	D000	C
ATOM	4066	CD2	TRP	C	236	−1.407	−30.040	39.979	1.00	27.52	D000	C
ATOM	4067	CE2	TRP	C	236	−1.224	−31.442	39.955	1.00	25.85	D000	C
ATOM	4068	CE3	TRP	C	236	−1.940	−29.450	41.132	1.00	25.98	D000	C
ATOM	4069	NE1	TRP	C	236	−0.696	−31.766	38.732	1.00	26.26	D000	N
ATOM	4070	CZ2	TRP	C	236	−1.551	−32.258	41.037	1.00	25.53	D000	C
ATOM	4071	CZ3	TRP	C	236	−2.267	−30.263	42.208	1.00	25.29	D000	C
ATOM	4072	CH2	TRP	C	236	−2.071	−31.654	42.152	1.00	26.90	D000	C
ATOM	4073	N	ARG	C	237	−2.473	−25.323	38.855	1.00	29.23	D000	N
ATOM	4074	CA	ARG	C	237	−2.100	−23.918	38.983	1.00	34.44	D000	C
ATOM	4075	C	ARG	C	237	−0.586	−23.790	38.820	1.00	34.81	D000	C
ATOM	4076	O	ARG	C	237	0.147	−24.755	39.052	1.00	28.62	D000	O
ATOM	4077	CB	ARG	C	237	−2.547	−23.349	40.337	1.00	30.99	D000	C
ATOM	4078	CG	ARG	C	237	−4.048	−23.189	40.474	1.00	37.60	D000	C
ATOM	4079	CD	ARG	C	237	−4.455	−21.737	40.591	1.00	42.14	D000	C
ATOM	4080	NE	ARG	C	237	−4.482	−21.299	41.980	1.00	49.94	D000	N
ATOM	4081	CZ	ARG	C	237	−5.493	−20.641	42.538	1.00	55.18	D000	C
ATOM	4082	NH1	ARG	C	237	−6.568	−20.334	41.822	1.00	41.85	D000	N
ATOM	4083	NH2	ARG	C	237	−5.428	−20.287	43.814	1.00	55.93	D000	N
ATOM	4084	N	PRO	C	238	−0.113	−22.606	38.401	1.00	36.47	D000	N
ATOM	4085	CA	PRO	C	238	1.334	−22.380	38.314	1.00	36.67	D000	C
ATOM	4086	C	PRO	C	238	2.051	−22.730	39.619	1.00	31.29	D000	C
ATOM	4087	O	PRO	C	238	1.581	−22.352	40.692	1.00	39.20	D000	O
ATOM	4088	CB	PRO	C	238	1.435	−20.881	38.015	1.00	41.44	D000	C
ATOM	4089	CG	PRO	C	238	0.172	−20.566	37.297	1.00	41.47	D000	C
ATOM	4090	CD	PRO	C	238	−0.886	−21.461	37.885	1.00	34.59	D000	C
ATOM	4091	N	GLU	C	239	3.149	−23.473	39.502	1.00	34.14	D000	N
ATOM	4092	CA	GLU	C	239	4.016	−23.854	40.624	1.00	40.34	D000	C
ATOM	4093	C	GLU	C	239	3.405	−24.898	41.566	1.00	40.27	D000	C
ATOM	4094	O	GLU	C	239	3.952	−25.164	42.636	1.00	43.88	D000	O
ATOM	4095	CB	GLU	C	239	4.428	−22.615	41.426	1.00	43.42	D000	C
ATOM	4096	CG	GLU	C	239	5.157	−21.571	40.598	1.00	50.20	D000	C
ATOM	4097	CD	GLU	C	239	5.859	−20.539	41.453	1.00	75.90	D000	C
ATOM	4098	OE1	GLU	C	239	5.212	−19.540	41.836	1.00	82.09	D000	O
ATOM	4099	OE2	GLU	C	239	7.059	−20.732	41.744	1.00	84.44	D000	O
ATOM	4100	N	GLN	C	240	2.285	−25.493	41.165	1.00	33.28	D000	N
ATOM	4101	CA	GLN	C	240	1.703	−26.611	41.904	1.00	31.36	D000	C
ATOM	4102	C	GLN	C	240	1.873	−27.891	41.082	1.00	31.46	D000	C
ATOM	4103	O	GLN	C	240	1.926	−27.827	39.856	1.00	30.03	D000	O
ATOM	4104	CB	GLN	C	240	0.224	−26.354	42.208	1.00	28.17	D000	C
ATOM	4105	CG	GLN	C	240	−0.065	−25.007	42.862	1.00	36.91	D000	C
ATOM	4106	CD	GLN	C	240	0.799	−24.737	44.083	1.00	42.84	D000	C
ATOM	4107	NE2	GLN	C	240	1.452	−23.580	44.095	1.00	37.20	D000	N
ATOM	4108	OE1	GLN	C	240	0.885	−25.559	45.001	1.00	41.85	D000	O
ATOM	4109	N	PRO	C	241	1.968	−29.060	41.746	1.00	31.89	D000	N
ATOM	4110	CA	PRO	C	241	1.952	−29.276	43.200	1.00	36.63	D000	C
ATOM	4111	C	PRO	C	241	3.307	−28.999	43.845	1.00	34.40	D000	C
ATOM	4112	O	PRO	C	241	4.332	−29.013	43.162	1.00	31.05	D000	O
ATOM	4113	CB	PRO	C	241	1.583	−30.757	43.326	1.00	30.98	D000	C
ATOM	4114	CG	PRO	C	241	2.166	−31.380	42.097	1.00	28.05	D000	C
ATOM	4115	CD	PRO	C	241	2.042	−30.334	41.004	1.00	28.29	D000	C
ATOM	4116	N	ASP	C	242	3.306	−28.762	45.151	1.00	31.20	D000	N
ATOM	4117	CA	ASP	C	242	4.534	−28.429	45.869	1.00	33.88	D000	C
ATOM	4118	C	ASP	C	242	5.428	−29.640	46.150	1.00	36.07	D000	C
ATOM	4119	O	ASP	C	242	6.583	−29.482	46.545	1.00	35.39	D000	O
ATOM	4120	CB	ASP	C	242	4.189	−27.712	47.176	1.00	30.91	D000	C
ATOM	4121	CG	ASP	C	242	3.796	−26.257	46.953	1.00	42.15	D000	C
ATOM	4122	OD2	ASP	C	242	2.709	−25.848	47.409	1.00	41.70	D000	O
ATOM	4123	OD1	ASP	C	242	4.571	−25.527	46.298	1.00	38.03	D000	O
ATOM	4124	N	ASP	C	243	4.894	−30.841	45.935	1.00	33.28	D000	N
ATOM	4125	CA	ASP	C	243	5.659	−32.080	46.098	1.00	33.76	D000	C
ATOM	4126	C	ASP	C	243	5.140	−33.135	45.123	1.00	36.43	D000	C
ATOM	4127	O	ASP	C	243	4.000	−33.045	44.662	1.00	31.00	D000	O
ATOM	4128	CB	ASP	C	243	5.562	−32.592	47.539	1.00	33.56	D000	C
ATOM	4129	CG	ASP	C	243	6.805	−33.360	47.980	1.00	45.01	D000	C
ATOM	4130	OD1	ASP	C	243	7.510	−33.935	47.118	1.00	32.68	D000	O
ATOM	4131	OD2	ASP	C	243	7.073	−33.389	49.201	1.00	41.68	D000	O
ATOM	4132	O	TRP	C	244	4.635	−37.408	43.978	1.00	29.40	D000	O
ATOM	4133	N	TRP	C	244	5.959	−34.135	44.811	1.00	26.76	D000	N
ATOM	4134	CA	TRP	C	244	5.530	−35.179	43.886	1.00	32.96	D000	C
ATOM	4135	C	TRP	C	244	5.096	−36.460	44.610	1.00	33.98	D000	C
ATOM	4136	CB	TRP	C	244	6.635	−35.486	42.872	1.00	22.49	D000	C
ATOM	4137	CG	TRP	C	244	7.926	−35.939	43.487	1.00	31.66	D000	C
ATOM	4138	CD1	TRP	C	244	8.985	−35.153	43.851	1.00	35.24	D000	C
ATOM	4139	CD2	TRP	C	244	8.301	−37.286	43.797	1.00	28.87	D000	C
ATOM	4140	NE1	TRP	C	244	9.992	−35.930	44.374	1.00	39.02	D000	N
ATOM	4141	CE2	TRP	C	244	9.597	−37.243	44.351	1.00	34.79	D000	C
ATOM	4142	CE3	TRP	C	244	7.666	−38.526	43.661	1.00	27.95	D000	C
ATOM	4143	CZ2	TRP	C	244	10.267	−38.390	44.770	1.00	32.14	D000	C
ATOM	4144	CZ3	TRP	C	244	8.333	−39.662	44.076	1.00	30.86	D000	C
ATOM	4145	CH2	TRP	C	244	9.621	−39.586	44.624	1.00	31.78	D000	C
ATOM	4146	O	TYR	C	245	4.758	−35.925	48.510	1.00	29.36	D000	O
ATOM	4147	N	TYR	C	245	5.250	−36.491	45.930	1.00	32.02	D000	N
ATOM	4148	CA	TYR	C	245	4.614	−37.534	46.735	1.00	28.48	D000	C
ATOM	4149	C	TYR	C	245	4.247	−36.969	48.099	1.00	30.14	D000	C
ATOM	4150	CB	TYR	C	245	5.502	−38.778	46.871	1.00	25.38	D000	C
ATOM	4151	CG	TYR	C	245	6.734	−38.633	47.739	1.00	32.91	D000	C
ATOM	4152	CD2	TYR	C	245	6.785	−39.200	49.009	1.00	31.25	D000	C
ATOM	4153	CD1	TYR	C	245	7.865	−37.975	47.270	1.00	30.40	D000	C
ATOM	4154	CE2	TYR	C	245	7.920	−39.093	49.795	1.00	28.79	D000	C
ATOM	4155	CE1	TYR	C	245	8.999	−37.860	48.049	1.00	32.06	D000	C
ATOM	4156	CZ	TYR	C	245	9.025	−38.420	49.307	1.00	29.81	D000	C
ATOM	4157	OH	TYR	C	245	10.159	−38.300	50.077	1.00	27.57	D000	O
ATOM	4158	O	GLY	C	246	4.628	−37.473	51.323	1.00	34.84	D000	O
ATOM	4159	N	GLY	C	246	3.340	−37.650	48.789	1.00	31.19	D000	N
ATOM	4160	CA	GLY	C	246	2.703	−37.067	49.955	1.00	35.76	D000	C
ATOM	4161	C	GLY	C	246	3.427	−37.207	51.272	1.00	33.62	D000	C
ATOM	4162	O	HIS	C	247	2.259	−37.710	55.785	1.00	43.05	D000	O
ATOM	4163	N	HIS	C	247	2.664	−37.031	52.345	1.00	38.43	D000	N
ATOM	4164	CA	HIS	C	247	3.202	−36.998	53.694	1.00	39.05	D000	C
ATOM	4165	C	HIS	C	247	2.411	−37.945	54.588	1.00	38.77	D000	C
ATOM	4166	CB	HIS	C	247	3.164	−35.565	54.234	1.00	39.25	D000	C
ATOM	4167	CG	HIS	C	247	3.692	−34.553	53.266	1.00	36.64	D000	C
ATOM	4168	ND1	HIS	C	247	4.970	−34.039	53.346	1.00	46.82	D000	N
ATOM	4169	CD2	HIS	C	247	3.126	−33.978	52.179	1.00	35.16	D000	C
ATOM	4170	CE1	HIS	C	247	5.163	−33.185	52.358	1.00	42.11	D000	C
ATOM	4171	NE2	HIS	C	247	4.059	−33.130	51.632	1.00	47.04	D000	N
ATOM	4172	O	GLY	C	248	−0.747	−38.509	54.445	1.00	40.24	D000	O
ATOM	4173	N	GLY	C	248	1.903	−39.018	53.991	1.00	40.96	D000	N
ATOM	4174	CA	GLY	C	248	1.118	−39.995	54.720	1.00	37.66	D000	C
ATOM	4175	C	GLY	C	248	−0.330	−39.578	54.902	1.00	47.53	D000	C
ATOM	4176	O	LEU	C	249	−3.773	−38.603	57.140	1.00	54.25	D000	O
ATOM	4177	N	LEU	C	249	−1.097	−40.433	55.574	1.00	52.35	D000	N
ATOM	4178	CA	LEU	C	249	−2.508	−40.173	55.842	1.00	52.11	D000	C
ATOM	4179	C	LEU	C	249	−2.689	−39.160	56.968	1.00	52.40	D000	C
ATOM	4180	CB	LEU	C	249	−3.233	−41.474	56.202	1.00	42.33	D000	C
ATOM	4181	CG	LEU	C	249	−3.333	−42.572	55.139	1.00	60.62	D000	C
ATOM	4182	CD2	LEU	C	249	−4.287	−42.165	54.027	1.00	56.35	D000	C
ATOM	4183	CD1	LEU	C	249	−3.789	−43.874	55.773	1.00	55.71	D000	C
ATOM	4184	O	GLY	C	250	−1.984	−35.849	59.639	1.00	57.54	D000	O
ATOM	4185	N	GLY	C	250	−1.622	−38.924	57.727	1.00	52.24	D000	N
ATOM	4186	CA	GLY	C	250	−1.698	−38.112	58.930	1.00	50.41	D000	C
ATOM	4187	C	GLY	C	250	−1.663	−36.608	58.725	1.00	57.93	D000	C
ATOM	4188	N	GLY	C	251	−1.269	−36.168	57.535	1.00	52.64	D000	N
ATOM	4189	CA	GLY	C	251	−1.203	−34.746	57.250	1.00	44.98	D000	C
ATOM	4190	C	GLY	C	251	−0.639	−34.433	55.880	1.00	46.45	D000	C
ATOM	4191	O	GLY	C	251	−0.459	−35.329	55.051	1.00	43.28	D000	O
ATOM	4192	N	GLY	C	252	−0.369	−33.152	55.642	1.00	37.49	D000	N
ATOM	4193	CA	GLY	C	252	0.205	−32.710	54.387	1.00	32.69	D000	C
ATOM	4194	C	GLY	C	252	−0.831	−32.272	53.366	1.00	34.76	D000	C
ATOM	4195	O	GLY	C	252	−2.005	−32.646	53.445	1.00	30.54	D000	O
ATOM	4196	N	GLU	C	253	−0.385	−31.472	52.402	1.00	33.99	D000	N
ATOM	4197	CA	GLU	C	253	−1.250	−30.989	51.331	1.00	40.45	D000	C
ATOM	4198	C	GLU	C	253	−1.285	−32.029	50.222	1.00	29.00	D000	C
ATOM	4199	O	GLU	C	253	−0.676	−31.860	49.168	1.00	35.30	D000	O
ATOM	4200	CB	GLU	C	253	−0.757	−29.632	50.821	1.00	34.32	D000	C
ATOM	4201	CG	GLU	C	253	−0.717	−28.572	51.926	1.00	42.40	D000	C
ATOM	4202	CD	GLU	C	253	−0.225	−27.217	51.444	1.00	58.06	D000	C
ATOM	4203	OE1	GLU	C	253	−0.620	−26.792	50.337	1.00	59.58	D000	O
ATOM	4204	OE2	GLU	C	253	0.557	−26.574	52.177	1.00	57.93	D000	O
ATOM	4205	N	ASP	C	254	−2.015	−33.109	50.484	1.00	27.38	D000	N
ATOM	4206	CA	ASP	C	254	−1.921	−34.327	49.693	1.00	31.18	D000	C
ATOM	4207	C	ASP	C	254	−3.140	−34.599	48.805	1.00	33.58	D000	C
ATOM	4208	O	ASP	C	254	−3.216	−35.646	48.158	1.00	27.45	D000	O
ATOM	4209	CB	ASP	C	254	−1.700	−35.535	50.623	1.00	29.94	D000	C
ATOM	4210	CG	ASP	C	254	−0.346	−35.504	51.328	1.00	36.48	D000	C
ATOM	4211	OD1	ASP	C	254	0.494	−34.630	51.013	1.00	28.05	D000	O
ATOM	4212	OD2	ASP	C	254	−0.117	−36.374	52.196	1.00	35.72	D000	O
ATOM	4213	N	CYS	C	255	−4.090	−33.670	48.768	1.00	26.75	D000	N
ATOM	4214	CA	CYS	C	255	−5.294	−33.867	47.963	1.00	26.33	D000	C
ATOM	4215	C	CYS	C	255	−5.518	−32.727	46.977	1.00	32.54	D000	C
ATOM	4216	O	CYS	C	255	−5.323	−31.559	47.316	1.00	27.66	D000	O
ATOM	4217	CB	CYS	C	255	−6.514	−34.024	48.869	1.00	27.73	D000	C
ATOM	4218	SG	CYS	C	255	−6.407	−35.447	49.969	1.00	35.91	D000	S
ATOM	4219	N	ALA	C	256	−5.930	−33.072	45.758	1.00	28.09	D000	N
ATOM	4220	CA	ALA	C	256	−6.116	−32.073	44.710	1.00	28.14	D000	C
ATOM	4221	C	ALA	C	256	−7.560	−31.598	44.637	1.00	28.47	D000	C
ATOM	4222	O	ALA	C	256	−8.500	−32.389	44.749	1.00	30.35	D000	O
ATOM	4223	CB	ALA	C	256	−5.678	−32.627	43.357	1.00	25.70	D000	C
ATOM	4224	N	HIS	C	257	−7.732	−30.298	44.444	1.00	28.56	D000	N
ATOM	4225	CA	HIS	C	257	−9.054	−29.742	44.223	1.00	25.18	D000	C
ATOM	4226	C	HIS	C	257	−9.020	−28.689	43.127	1.00	31.48	D000	C
ATOM	4227	O	HIS	C	257	−7.990	−28.054	42.895	1.00	26.66	D000	O
ATOM	4228	CB	HIS	C	257	−9.615	−29.139	45.514	1.00	24.94	D000	C
ATOM	4229	CG	HIS	C	257	−8.842	−27.958	46.023	1.00	29.72	D000	C
ATOM	4230	CD2	HIS	C	257	−7.685	−27.880	46.715	1.00	26.19	D000	C
ATOM	4231	ND1	HIS	C	257	−9.275	−26.658	45.852	1.00	31.92	D000	N
ATOM	4232	CE1	HIS	C	257	−8.411	−25.834	46.415	1.00	33.33	D000	C
ATOM	4233	NE2	HIS	C	257	−7.434	−26.546	46.943	1.00	31.64	D000	N
ATOM	4234	N	PHE	C	258	−10.146	−28.528	42.441	1.00	25.00	D000	N
ATOM	4235	CA	PHE	C	258	−10.340	−27.385	41.567	1.00	28.97	D000	C
ATOM	4236	C	PHE	C	258	−10.347	−26.129	42.421	1.00	30.92	D000	C
ATOM	4237	O	PHE	C	258	−10.917	−26.128	43.511	1.00	27.46	D000	O
ATOM	4238	CB	PHE	C	258	−11.655	−27.491	40.788	1.00	28.67	D000	C
ATOM	4239	CG	PHE	C	258	−11.790	−28.752	39.975	1.00	28.57	D000	C
ATOM	4240	CD1	PHE	C	258	−11.253	−28.831	38.699	1.00	24.14	D000	C
ATOM	4241	CD2	PHE	C	258	−12.475	−29.845	40.477	1.00	26.98	D000	C
ATOM	4242	CE1	PHE	C	258	−11.385	−29.982	37.944	1.00	27.83	D000	C
ATOM	4243	CE2	PHE	C	258	−12.610	−31.002	39.727	1.00	29.05	D000	C
ATOM	4244	CZ	PHE	C	258	−12.064	−31.067	38.458	1.00	26.68	D000	C
ATOM	4245	N	THR	C	259	−9.709	−25.068	41.935	1.00	31.52	D000	N
ATOM	4246	CA	THR	C	259	−9.778	−23.766	42.596	1.00	27.35	D000	C
ATOM	4247	C	THR	C	259	−10.853	−22.908	41.947	1.00	32.37	D000	C
ATOM	4248	O	THR	C	259	−11.547	−23.361	41.038	1.00	28.98	D000	O
ATOM	4249	CB	THR	C	259	−8.450	−23.013	42.517	1.00	30.50	D000	C
ATOM	4250	CG2	THR	C	259	−7.336	−23.832	43.146	1.00	29.47	D000	C
ATOM	4251	OG1	THR	C	259	−8.141	−22.759	41.139	1.00	26.60	D000	O
ATOM	4252	N	ASP	C	260	−10.966	−21.657	42.383	1.00	33.47	D000	N
ATOM	4253	CA	ASP	C	260	−11.989	−20.772	41.841	1.00	32.04	D000	C
ATOM	4254	C	ASP	C	260	−11.660	−20.274	40.432	1.00	28.10	D000	C
ATOM	4255	O	ASP	C	260	−12.469	−19.571	39.833	1.00	35.94	D000	O
ATOM	4256	CB	ASP	C	260	−12.232	−19.574	42.774	1.00	31.62	D000	C
ATOM	4257	CG	ASP	C	260	−10.952	−18.844	43.150	1.00	39.51	D000	C
ATOM	4258	OD1	ASP	C	260	−9.894	−19.114	42.544	1.00	46.04	D000	O
ATOM	4259	OD2	ASP	C	260	−11.010	−17.986	44.057	1.00	48.87	D000	O
ATOM	4260	N	ASP	C	261	−10.494	−20.631	39.890	1.00	32.99	D000	N
ATOM	4261	CA	ASP	C	261	−10.219	−20.308	38.483	1.00	33.63	D000	C
ATOM	4262	C	ASP	C	261	−10.169	−21.568	37.618	1.00	34.02	D000	C
ATOM	4263	O	ASP	C	261	−9.808	−21.517	36.440	1.00	35.61	D000	O
ATOM	4264	CB	ASP	C	261	−8.920	−19.493	38.330	1.00	34.41	D000	C
ATOM	4265	CG	ASP	C	261	−7.663	−20.257	38.749	1.00	41.30	D000	C
ATOM	4266	OD1	ASP	C	261	−7.662	−21.504	38.780	1.00	38.03	D000	O
ATOM	4267	OD2	ASP	C	261	−6.644	−19.591	39.031	1.00	47.65	D000	O
ATOM	4268	N	GLY	C	262	−10.525	−22.701	38.214	1.00	34.67	D000	N
ATOM	4269	CA	GLY	C	262	−10.608	−23.949	37.477	1.00	29.76	D000	C
ATOM	4270	C	GLY	C	262	−9.366	−24.810	37.571	1.00	25.05	D000	C
ATOM	4271	O	GLY	C	262	−9.449	−26.038	37.513	1.00	31.23	D000	O
ATOM	4272	N	ARG	C	263	−8.207	−24.177	37.710	1.00	26.83	D000	N
ATOM	4273	CA	ARG	C	263	−6.952	−24.919	37.778	1.00	26.39	D000	C
ATOM	4274	C	ARG	C	263	−6.771	−25.578	39.148	1.00	30.19	D000	C
ATOM	4275	O	ARG	C	263	−7.392	−25.172	40.135	1.00	28.43	D000	O
ATOM	4276	CB	ARG	C	263	−5.775	−24.000	37.443	1.00	27.07	D000	C
ATOM	4277	CG	ARG	C	263	−5.652	−23.711	35.943	1.00	29.33	D000	C
ATOM	4278	CD	ARG	C	263	−4.595	−22.643	35.649	1.00	33.17	D000	C
ATOM	4279	NE	ARG	C	263	−5.071	−21.305	35.982	1.00	44.51	D000	N
ATOM	4280	CZ	ARG	C	263	−5.787	−20.547	35.156	1.00	52.96	D000	C
ATOM	4281	NH1	ARG	C	263	−6.105	−21.002	33.951	1.00	49.17	D000	N
ATOM	4282	NH2	ARG	C	263	−6.188	−19.340	35.532	1.00	51.57	D000	N
ATOM	4283	N	TRP	C	264	−5.916	−26.596	39.202	1.00	26.05	D000	N
ATOM	4284	CA	TRP	C	264	−5.847	−27.477	40.365	1.00	28.26	D000	C
ATOM	4285	C	TRP	C	264	−4.859	−27.000	41.415	1.00	27.92	D000	C
ATOM	4286	O	TRP	C	264	−3.844	−26.385	41.097	1.00	28.53	D000	O
ATOM	4287	CB	TRP	C	264	−5.460	−28.897	39.938	1.00	24.67	D000	C
ATOM	4288	CG	TRP	C	264	−6.268	−29.456	38.814	1.00	25.08	D000	C
ATOM	4289	CD1	TRP	C	264	−7.436	−28.958	38.304	1.00	26.48	D000	C
ATOM	4290	CD2	TRP	C	264	−5.963	−30.627	38.048	1.00	26.55	D000	C
ATOM	4291	CE2	TRP	C	264	−6.994	−30.785	37.098	1.00	22.22	D000	C
ATOM	4292	CE3	TRP	C	264	−4.923	−31.565	38.081	1.00	25.16	D000	C
ATOM	4293	NE1	TRP	C	264	−7.879	−29.752	37.276	1.00	26.28	D000	N
ATOM	4294	CZ2	TRP	C	264	−7.012	−31.837	36.181	1.00	27.60	D000	C
ATOM	4295	CZ3	TRP	C	264	−4.944	−32.616	37.170	1.00	22.92	D000	C
ATOM	4296	CH2	TRP	C	264	−5.979	−32.739	36.232	1.00	24.94	D000	C
ATOM	4297	N	ASN	C	265	−5.155	−27.313	42.670	1.00	30.65	D000	N
ATOM	4298	CA	ASN	C	265	−4.243	−27.018	43.762	1.00	29.62	D000	C
ATOM	4299	C	ASN	C	265	−4.178	−28.182	44.735	1.00	27.94	D000	C
ATOM	4300	O	ASN	C	265	−5.157	−28.904	44.910	1.00	27.71	D000	O
ATOM	4301	CB	ASN	C	265	−4.668	−25.746	44.490	1.00	31.63	D000	C
ATOM	4302	CG	ASN	C	265	−3.717	−25.373	45.608	1.00	37.30	D000	C
ATOM	4303	ND2	ASN	C	265	−4.220	−25.357	46.839	1.00	35.10	D000	N
ATOM	4304	OD1	ASN	C	265	−2.541	−25.102	45.367	1.00	39.83	D000	O
ATOM	4305	N	ASP	C	266	−3.021	−28.364	45.358	1.00	24.21	D000	N
ATOM	4306	CA	ASP	C	266	−2.850	−29.405	46.366	1.00	28.45	D000	C
ATOM	4307	C	ASP	C	266	−3.066	−28.832	47.763	1.00	36.19	D000	C
ATOM	4308	O	ASP	C	266	−2.397	−27.880	48.157	1.00	35.56	D000	O
ATOM	4309	CB	ASP	C	266	−1.463	−30.046	46.253	1.00	25.57	D000	C
ATOM	4310	CG	ASP	C	266	−0.349	−29.020	46.030	1.00	36.15	D000	C
ATOM	4311	OD1	ASP	C	266	−0.572	−28.006	45.326	1.00	34.08	D000	O
ATOM	4312	OD2	ASP	C	266	0.762	−29.236	46.554	1.00	38.58	D000	O
ATOM	4313	N	ASP	C	267	−4.007	−29.412	48.507	1.00	32.84	D000	N
ATOM	4314	CA	ASP	C	267	−4.386	−28.883	49.817	1.00	30.12	D000	C
ATOM	4315	C	ASP	C	267	−4.571	−30.002	50.845	1.00	33.99	D000	C
ATOM	4316	O	ASP	C	267	−4.684	−31.181	50.488	1.00	23.96	D000	O
ATOM	4317	CB	ASP	C	267	−5.675	−28.058	49.701	1.00	33.91	D000	C
ATOM	4318	CG	ASP	C	267	−5.729	−26.898	50.691	1.00	39.18	D000	C
ATOM	4319	OD1	ASP	C	267	−4.872	−26.833	51.601	1.00	39.63	D000	O
ATOM	4320	OD2	ASP	C	267	−6.640	−26.051	50.560	1.00	41.15	D000	O
ATOM	4321	N	VAL	C	268	−4.610	−29.625	52.121	1.00	30.38	D000	N
ATOM	4322	CA	VAL	C	268	−4.808	−30.587	53.202	1.00	34.77	D000	C
ATOM	4323	C	VAL	C	268	−6.169	−31.260	53.054	1.00	31.59	D000	C
ATOM	4324	O	VAL	C	268	−7.157	−30.630	52.685	1.00	30.27	D000	O
ATOM	4325	CB	VAL	C	268	−4.683	−29.923	54.596	1.00	36.31	D000	C
ATOM	4326	CG1	VAL	C	268	−3.302	−29.294	54.757	1.00	31.26	D000	C
ATOM	4327	CG2	VAL	C	268	−5.770	−28.881	54.801	1.00	33.82	D000	C
ATOM	4328	N	CYS	C	269	−6.209	−32.555	53.334	1.00	32.86	D000	N
ATOM	4329	CA	CYS	C	269	−7.369	−33.364	52.991	1.00	31.61	D000	C
ATOM	4330	C	CYS	C	269	−8.559	−33.098	53.917	1.00	36.95	D000	C
ATOM	4331	O	CYS	C	269	−9.684	−33.504	53.627	1.00	36.14	D000	O
ATOM	4332	CB	CYS	C	269	−6.984	−34.839	53.009	1.00	44.62	D000	C
ATOM	4333	SG	CYS	C	269	−5.637	−35.218	51.830	1.00	60.76	D000	S
ATOM	4334	N	GLN	C	270	−8.305	−32.384	55.009	1.00	31.38	D000	N
ATOM	4335	CA	GLN	C	270	−9.324	−32.047	55.992	1.00	34.32	D000	C
ATOM	4336	C	GLN	C	270	−10.328	−30.995	55.495	1.00	35.28	D000	C
ATOM	4337	O	GLN	C	270	−11.434	−30.895	56.022	1.00	38.13	D000	O
ATOM	4338	CB	GLN	C	270	−8.640	−31.552	57.265	1.00	41.74	D000	C
ATOM	4339	CG	GLN	C	270	−9.526	−31.531	58.491	1.00	57.53	D000	C
ATOM	4340	CD	GLN	C	270	−8.755	−31.148	59.743	1.00	62.03	D000	C
ATOM	4341	NE2	GLN	C	270	−9.057	−29.975	60.280	1.00	54.32	D000	N
ATOM	4342	OE1	GLN	C	270	−7.898	−31.898	60.222	1.00	60.58	D000	O
ATOM	4343	N	ARG	C	271	−9.940	−30.207	54.495	1.00	30.92	D000	N
ATOM	4344	CA	ARG	C	271	−10.790	−29.124	53.996	1.00	30.72	D000	C
ATOM	4345	C	ARG	C	271	−12.159	−29.633	53.533	1.00	38.04	D000	C
ATOM	4346	O	ARG	C	271	−12.246	−30.543	52.709	1.00	31.45	D000	O
ATOM	4347	CB	ARG	C	271	−10.096	−28.385	52.849	1.00	34.39	D000	C
ATOM	4348	CG	ARG	C	271	−8.799	−27.676	53.234	1.00	35.61	D000	C
ATOM	4349	CD	ARG	C	271	−9.066	−26.393	53.999	1.00	43.95	D000	C
ATOM	4350	NE	ARG	C	271	−7.837	−25.661	54.292	1.00	42.12	D000	N
ATOM	4351	CZ	ARG	C	271	−7.169	−25.750	55.438	1.00	45.47	D000	C
ATOM	4352	NH1	ARG	C	271	−7.606	−26.547	56.406	1.00	42.46	D000	N
ATOM	4353	NH2	ARG	C	271	−6.059	−25.048	55.614	1.00	47.94	D000	N
ATOM	4354	N	PRO	C	272	−13.237	−29.045	54.074	1.00	35.02	D000	N
ATOM	4355	CA	PRO	C	272	−14.604	−29.446	53.724	1.00	34.48	D000	C
ATOM	4356	C	PRO	C	272	−15.064	−28.856	52.392	1.00	34.36	D000	C
ATOM	4357	O	PRO	C	272	−16.036	−28.104	52.355	1.00	37.58	D000	O
ATOM	4358	CB	PRO	C	272	−15.433	−28.887	54.881	1.00	36.83	D000	C
ATOM	4359	CG	PRO	C	272	−14.678	−27.668	55.306	1.00	32.07	D000	C
ATOM	4360	CD	PRO	C	272	−13.217	−28.007	55.121	1.00	35.31	D000	C
ATOM	4361	N	TYR	C	273	−14.370	−29.197	51.312	1.00	34.00	D000	N
ATOM	4362	CA	TYR	C	273	−14.725	−28.690	49.994	1.00	34.47	D000	C
ATOM	4363	C	TYR	C	273	−15.886	−29.467	49.399	1.00	31.88	D000	C
ATOM	4364	O	TYR	C	273	−16.205	−30.571	49.848	1.00	34.84	D000	O
ATOM	4365	CB	TYR	C	273	−13.523	−28.760	49.048	1.00	33.39	D000	C
ATOM	4366	CG	TYR	C	273	−12.391	−27.827	49.412	1.00	29.84	D000	C
ATOM	4367	CD1	TYR	C	273	−12.634	−26.642	50.096	1.00	31.84	D000	C
ATOM	4368	CD2	TYR	C	273	−11.077	−28.131	49.065	1.00	27.54	D000	C
ATOM	4369	CE1	TYR	C	273	−11.595	−25.778	50.431	1.00	30.36	D000	C
ATOM	4370	CE2	TYR	C	273	−10.036	−27.280	49.391	1.00	31.31	D000	C
ATOM	4371	CZ	TYR	C	273	−10.303	−26.104	50.075	1.00	31.94	D000	C
ATOM	4372	OH	TYR	C	273	−9.273	−25.261	50.404	1.00	32.60	D000	O
ATOM	4373	N	ARG	C	274	−16.510	−28.891	48.377	1.00	29.76	D000	N
ATOM	4374	CA	ARG	C	274	−17.470	−29.627	47.566	1.00	28.81	D000	C
ATOM	4375	C	ARG	C	274	−16.750	−30.733	46.802	1.00	30.11	D000	C
ATOM	4376	O	ARG	C	274	−15.520	−30.772	46.766	1.00	28.45	D000	O
ATOM	4377	CB	ARG	C	274	−18.191	−28.689	46.601	1.00	31.26	D000	C
ATOM	4378	CG	ARG	C	274	−19.110	−27.703	47.298	1.00	35.55	D000	C
ATOM	4379	CD	ARG	C	274	−19.871	−26.844	46.309	1.00	33.61	D000	C
ATOM	4380	NE	ARG	C	274	−20.885	−26.046	46.984	1.00	39.40	D000	N
ATOM	4381	CZ	ARG	C	274	−21.630	−25.121	46.389	1.00	48.65	D000	C
ATOM	4382	NH1	ARG	C	274	−21.474	−24.867	45.097	1.00	48.98	D000	N
ATOM	4383	NH2	ARG	C	274	−22.531	−24.446	47.090	1.00	55.24	D000	N
ATOM	4384	N	TRP	C	275	−17.507	−31.639	46.198	1.00	28.06	D000	N
ATOM	4385	CA	TRP	C	275	−16.887	−32.709	45.432	1.00	28.84	D000	C
ATOM	4386	C	TRP	C	275	−17.754	−33.114	44.252	1.00	29.72	D000	C
ATOM	4387	O	TRP	C	275	−18.905	−32.693	44.130	1.00	26.78	D000	O
ATOM	4388	CB	TRP	C	275	−16.601	−33.927	46.322	1.00	29.81	D000	C
ATOM	4389	CG	TRP	C	275	−17.824	−34.715	46.717	1.00	31.96	D000	C
ATOM	4390	CD1	TRP	C	275	−18.293	−35.855	46.125	1.00	31.44	D000	C
ATOM	4391	CD2	TRP	C	275	−18.726	−34.423	47.795	1.00	29.40	D000	C
ATOM	4392	CE2	TRP	C	275	−19.718	−35.426	47.793	1.00	31.93	D000	C
ATOM	4393	CE3	TRP	C	275	−18.791	−33.412	48.759	1.00	32.50	D000	C
ATOM	4394	NE1	TRP	C	275	−19.430	−36.288	46.767	1.00	36.68	D000	N
ATOM	4395	CZ2	TRP	C	275	−20.761	−35.447	48.718	1.00	33.08	D000	C
ATOM	4396	CZ3	TRP	C	275	−19.829	−33.433	49.676	1.00	33.96	D000	C
ATOM	4397	CH2	TRP	C	275	−20.801	−34.443	49.648	1.00	35.93	D000	C
ATOM	4398	N	VAL	C	276	−17.178	−33.926	43.376	1.00	28.10	D000	N
ATOM	4399	CA	VAL	C	276	−17.870	−34.412	42.195	1.00	29.03	D000	C
ATOM	4400	C	VAL	C	276	−17.737	−35.924	42.114	1.00	27.19	D000	C
ATOM	4401	O	VAL	C	276	−16.628	−36.454	42.177	1.00	28.31	D000	O
ATOM	4402	CB	VAL	C	276	−17.302	−33.780	40.905	1.00	28.00	D000	C
ATOM	4403	CG1	VAL	C	276	−18.046	−34.293	39.688	1.00	27.41	D000	C
ATOM	4404	CG2	VAL	C	276	−17.364	−32.259	40.982	1.00	28.48	D000	C
ATOM	4405	N	CYS	C	277	−18.862	−36.619	41.988	1.00	26.93	D000	N
ATOM	4406	CA	CYS	C	277	−18.832	−38.058	41.751	1.00	33.14	D000	C
ATOM	4407	C	CYS	C	277	−18.994	−38.338	40.262	1.00	37.44	D000	C
ATOM	4408	O	CYS	C	277	−19.699	−37.612	39.564	1.00	33.29	D000	O
ATOM	4409	CB	CYS	C	277	−19.922	−38.770	42.562	1.00	32.89	D000	C
ATOM	4410	SG	CYS	C	277	−19.660	−38.700	44.364	1.00	47.93	D000	S
ATOM	4411	N	GLU	C	278	−18.324	−39.386	39.787	1.00	30.10	D000	N
ATOM	4412	CA	GLU	C	278	−18.367	−39.774	38.386	1.00	28.53	D000	C
ATOM	4413	C	GLU	C	278	−18.528	−41.288	38.252	1.00	32.73	D000	C
ATOM	4414	O	GLU	C	278	−17.931	−42.050	39.008	1.00	29.46	D000	O
ATOM	4415	CB	GLU	C	278	−17.095	−39.315	37.655	1.00	32.72	D000	C
ATOM	4416	CG	GLU	C	278	−16.913	−39.932	36.260	1.00	32.26	D000	C
ATOM	4417	CD	GLU	C	278	−15.636	−39.483	35.555	1.00	39.23	D000	C
ATOM	4418	OE1	GLU	C	278	−14.646	−39.151	36.241	1.00	36.80	D000	O
ATOM	4419	OE2	GLU	C	278	−15.622	−39.463	34.303	1.00	40.68	D000	O
ATOM	4420	N	THR	C	279	−19.346	−41.717	37.297	1.00	27.04	D000	N
ATOM	4421	CA	THR	C	279	−19.453	−43.132	36.963	1.00	34.21	D000	C
ATOM	4422	C	THR	C	279	−19.688	−43.285	35.460	1.00	36.69	D000	C
ATOM	4423	O	THR	C	279	−19.848	−42.296	34.746	1.00	39.25	D000	O
ATOM	4424	CB	THR	C	279	−20.586	−43.826	37.758	1.00	39.26	D000	C
ATOM	4425	CG2	THR	C	279	−21.950	−43.311	37.326	1.00	34.73	D000	C
ATOM	4426	OG1	THR	C	279	−20.522	−45.244	37.554	1.00	42.37	D000	O
ATOM	4427	N	GLU	C	280	−19.704	−44.522	34.980	1.00	32.85	D000	N
ATOM	4428	CA	GLU	C	280	−19.835	−44.782	33.548	1.00	50.68	D000	C
ATOM	4429	C	GLU	C	280	−21.239	−45.225	33.156	1.00	52.22	D000	C
ATOM	4430	O	GLU	C	280	−22.086	−45.481	34.011	1.00	55.73	D000	O
ATOM	4431	CB	GLU	C	280	−18.829	−45.846	33.118	1.00	52.68	D000	C
ATOM	4432	CG	GLU	C	280	−17.416	−45.583	33.593	1.00	64.50	D000	C
ATOM	4433	CD	GLU	C	280	−16.653	−46.863	33.862	1.00	89.69	D000	C
ATOM	4434	OE1	GLU	C	280	−17.283	−47.943	33.861	1.00	93.00	D000	O
ATOM	4435	OE2	GLU	C	280	−15.424	−46.790	34.078	1.00	104.15	D000	O
ATOM	4436	O	LEU	C	281	−22.641	−47.686	29.761	1.00	76.02	D000	O
ATOM	4437	N	LEU	C	281	−21.477	−45.319	31.852	1.00	63.81	D000	N
ATOM	4438	CA	LEU	C	281	−22.728	−45.870	31.340	1.00	65.22	D000	C
ATOM	4439	C	LEU	C	281	−22.565	−47.338	30.941	1.00	72.08	D000	C
ATOM	4440	CB	LEU	C	281	−23.228	−45.044	30.158	1.00	59.22	D000	C
ATOM	4441	CG	LEU	C	281	−23.879	−43.727	30.578	1.00	63.11	D000	C
ATOM	4442	CD1	LEU	C	281	−24.279	−42.891	29.370	1.00	48.41	D000	C
ATOM	4443	CD2	LEU	C	281	−25.083	−44.021	31.458	1.00	67.92	D000	C
ATOM	4444	O	ASP	C	282	−20.760	−51.176	30.617	1.00	50.93	D000	O
ATOM	4445	N	ASP	C	282	−22.342	−48.183	31.947	1.00	77.43	D000	N
ATOM	4446	CA	ASP	C	282	−22.184	−49.629	31.778	1.00	80.26	D000	C
ATOM	4447	C	ASP	C	282	−21.144	−50.009	30.726	1.00	71.14	D000	C
ATOM	4448	CB	ASP	C	282	−23.529	−50.272	31.433	1.00	81.46	D000	C
ATOM	4449	CG	ASP	C	282	−24.448	−50.366	32.632	1.00	80.75	D000	C
ATOM	4450	OD1	ASP	C	282	−24.417	−49.445	33.476	1.00	77.18	D000	O
ATOM	4451	OD2	ASP	C	282	−25.192	−51.364	32.736	1.00	78.02	D000	O
TER

TABLE 10.3
ATOM	1	N	GLN	C	1	12.778	87.875	6.343	1.00	63.46		N
ATOM	2	CA	GLN	C	1	12.935	86.437	6.168	1.00	57.97		C
ATOM	3	C	GLN	C	1	11.798	85.716	6.845	1.00	55.78		C
ATOM	4	O	GLN	C	1	11.088	86.308	7.656	1.00	58.48		O
ATOM	5	CB	GLN	C	1	14.271	85.946	6.714	1.00	51.88		C
ATOM	6	CG	GLN	C	1	14.814	84.739	5.974	1.00	59.79		C
ATOM	7	CD	GLN	C	1	14.717	84.869	4.445	1.00	78.61		C
ATOM	8	OE1	GLN	C	1	14.676	85.980	3.896	1.00	61.52		O
ATOM	9	NE2	GLN	C	1	14.669	83.721	3.753	1.00	84.10		N
ATOM	10	N	VAL	C	2	11.615	84.445	6.497	1.00	50.14		N
ATOM	11	CA	VAL	C	2	10.404	83.710	6.828	1.00	46.16		C
ATOM	12	C	VAL	C	2	10.800	82.363	7.396	1.00	45.45		C
ATOM	13	O	VAL	C	2	11.642	81.667	6.822	1.00	49.37		O
ATOM	14	CB	VAL	C	2	9.493	83.521	5.596	1.00	45.22		C
ATOM	15	CG1	VAL	C	2	8.322	82.567	5.911	1.00	45.47		C
ATOM	16	CG2	VAL	C	2	8.965	84.848	5.109	1.00	40.64		C
ATOM	17	N	GLN	C	3	10.163	81.983	8.498	1.00	50.52		N
ATOM	18	CA	GLN	C	3	10.262	80.648	9.066	1.00	49.86		C
ATOM	19	C	GLN	C	3	8.856	80.074	9.158	1.00	45.53		C
ATOM	20	O	GLN	C	3	7.924	80.766	9.596	1.00	40.46		O
ATOM	21	CB	GLN	C	3	10.933	80.674	10.449	1.00	52.58		C
ATOM	22	CG	GLN	C	3	12.476	80.689	10.448	1.00	67.48		C
ATOM	23	CD	GLN	C	3	13.103	82.051	10.135	1.00	74.06		C
ATOM	24	OE1	GLN	C	3	12.444	83.102	10.186	1.00	75.22		O
ATOM	25	NE2	GLN	C	3	14.394	82.033	9.811	1.00	80.56		N
ATOM	26	N	LEU	C	4	8.702	78.828	8.714	1.00	36.58		N
ATOM	27	CA	LEU	C	4	7.451	78.093	8.811	1.00	35.24		C
ATOM	28	C	LEU	C	4	7.674	76.836	9.634	1.00	35.32		C
ATOM	29	O	LEU	C	4	8.563	76.043	9.319	1.00	34.10		O
ATOM	30	CB	LEU	C	4	6.925	77.728	7.417	1.00	35.59		C
ATOM	31	CG	LEU	C	4	6.747	78.896	6.452	1.00	38.97		C
ATOM	32	CD1	LEU	C	4	6.422	78.423	5.045	1.00	39.74		C
ATOM	33	CD2	LEU	C	4	5.653	79.806	6.970	1.00	42.54		C
ATOM	34	N	VAL	C	5	6.835	76.623	10.647	1.00	40.31		N
ATOM	35	CA	VAL	C	5	6.970	75.492	11.568	1.00	38.30		C
ATOM	36	C	VAL	C	5	5.625	74.776	11.675	1.00	41.55		C
ATOM	37	O	VAL	C	5	4.663	75.325	12.232	1.00	47.07		O
ATOM	38	CB	VAL	C	5	7.451	75.939	12.956	1.00	35.88		C
ATOM	39	CG1	VAL	C	5	7.568	74.743	13.871	1.00	36.28		C
ATOM	40	CG2	VAL	C	5	8.763	76.660	12.847	1.00	26.29		C
ATOM	41	N	GLU	C	6	5.558	73.556	11.169	1.00	42.37		N
ATOM	42	CA	GLU	C	6	4.354	72.741	11.241	1.00	43.70		C
ATOM	43	C	GLU	C	6	4.281	71.970	12.559	1.00	43.98		C
ATOM	44	O	GLU	C	6	5.290	71.677	13.196	1.00	49.49		O
ATOM	45	CB	GLU	C	6	4.290	71.749	10.081	1.00	44.93		C
ATOM	46	CG	GLU	C	6	4.481	72.363	8.699	1.00	44.29		C
ATOM	47	CD	GLU	C	6	5.949	72.419	8.267	1.00	44.27		C
ATOM	48	OE1	GLU	C	6	6.215	72.317	7.041	1.00	42.60		O
ATOM	49	OE2	GLU	C	6	6.832	72.490	9.153	1.00	47.85		O1−
ATOM	50	N	SER	C	7	3.061	71.619	12.950	1.00	48.19		N
ATOM	51	CA	SER	C	7	2.851	70.788	14.128	1.00	51.74		C
ATOM	52	C	SER	C	7	1.509	70.084	13.994	1.00	45.51		C
ATOM	53	O	SER	C	7	0.681	70.437	13.151	1.00	43.94		O
ATOM	54	CB	SER	C	7	2.904	71.620	15.410	1.00	38.38		C
ATOM	55	OG	SER	C	7	1.907	72.623	15.354	1.00	49.56		O
ATOM	56	N	GLY	C	8	1.310	69.067	14.829	1.00	48.93		N
ATOM	57	CA	GLY	C	8	0.030	68.405	14.930	1.00	34.09		C
ATOM	58	C	GLY	C	8	−0.065	67.069	14.246	1.00	43.11		C
ATOM	59	O	GLY	C	8	−1.148	66.466	14.255	1.00	46.79		O
ATOM	60	N	GLY	C	9	1.015	66.567	13.666	1.00	37.58		N
ATOM	61	CA	GLY	C	9	0.947	65.229	13.116	1.00	47.86		C
ATOM	62	C	GLY	C	9	0.747	64.199	14.226	1.00	51.47		C
ATOM	63	O	GLY	C	9	0.716	64.509	15.419	1.00	54.50		O
ATOM	64	N	GLY	C	10	0.731	62.943	13.833	1.00	46.74		N
ATOM	65	CA	GLY	C	10	0.618	61.871	14.804	1.00	46.77		C
ATOM	66	C	GLY	C	10	−0.035	60.648	14.193	1.00	52.50		C
ATOM	67	O	GLY	C	10	−0.310	60.586	12.994	1.00	47.51		O
ATOM	68	N	VAL	C	11	−0.256	59.651	15.049	1.00	51.48		N
ATOM	69	CA	VAL	C	11	−0.832	58.380	14.625	1.00	53.97		C
ATOM	70	C	VAL	C	11	−2.320	58.434	14.900	1.00	52.43		C
ATOM	71	O	VAL	C	11	−2.739	58.881	15.975	1.00	50.83		O
ATOM	72	CB	VAL	C	11	−0.183	57.184	15.345	1.00	43.91		C
ATOM	73	CG1	VAL	C	11	−0.742	55.891	14.787	1.00	43.96		C
ATOM	74	CG2	VAL	C	11	1.317	57.226	15.201	1.00	43.94		C
ATOM	75	N	VAL	C	12	−3.117	58.015	13.916	1.00	45.99		N
ATOM	76	CA	VAL	C	12	−4.570	58.072	13.996	1.00	46.88		C
ATOM	77	C	VAL	C	12	−5.115	56.950	13.139	1.00	46.73		C
ATOM	78	O	VAL	C	12	−4.469	56.494	12.191	1.00	47.91		O
ATOM	79	CB	VAL	C	12	−5.179	59.425	13.540	1.00	47.29		C
ATOM	80	CG1	VAL	C	12	−4.763	60.547	14.468	1.00	46.14		C
ATOM	81	CG2	VAL	C	12	−4.755	59.739	12.130	1.00	48.50		C
ATOM	82	N	GLN	C	13	−6.316	56.547	13.443	1.00	51.98		N
ATOM	83	CA	GLN	C	13	−7.001	55.451	12.787	1.00	48.11		C
ATOM	84	C	GLN	C	13	−7.748	55.950	11.559	1.00	42.02		C
ATOM	85	O	GLN	C	13	−8.237	57.082	11.548	1.00	45.22		O
ATOM	86	CB	GLN	C	13	−8.005	54.841	13.740	1.00	57.37		C
ATOM	87	CG	GLN	C	13	−7.409	54.422	15.035	1.00	67.65		C
ATOM	88	CD	GLN	C	13	−8.286	53.439	15.730	1.00	79.97		C
ATOM	89	OE1	GLN	C	13	−8.845	53.737	16.788	1.00	93.60		O
ATOM	90	NE2	GLN	C	13	−8.446	52.258	15.130	1.00	91.83		N
ATOM	91	N	PRO	C	14	−7.878	55.101	10.541	1.00	38.64		N
ATOM	92	CA	PRO	C	14	−8.652	55.475	9.351	1.00	37.32		C
ATOM	93	C	PRO	C	14	−10.050	55.954	9.725	1.00	48.06		C
ATOM	94	O	PRO	C	14	−10.688	55.419	10.634	1.00	50.66		O
ATOM	95	CB	PRO	C	14	−8.711	54.174	8.539	1.00	35.18		C
ATOM	96	CG	PRO	C	14	−7.556	53.370	9.005	1.00	40.76		C
ATOM	97	CD	PRO	C	14	−7.351	53.727	10.456	1.00	40.72		C
ATOM	98	N	GLY	C	15	−10.525	56.982	9.023	1.00	45.47		N
ATOM	99	CA	GLY	C	15	−11.836	57.526	9.264	1.00	39.13		C
ATOM	100	C	GLY	C	15	−11.886	58.622	10.303	1.00	40.65		C
ATOM	101	O	GLY	C	15	−12.887	59.331	10.374	1.00	51.10		O
ATOM	102	N	ARG	C	16	−10.842	58.781	11.109	1.00	42.12		N
ATOM	103	CA	ARG	C	16	−10.775	59.854	12.087	1.00	42.11		C
ATOM	104	C	ARG	C	16	−10.275	61.158	11.450	1.00	49.72		C
ATOM	105	O	ARG	C	16	−10.040	61.255	10.237	1.00	41.14		O
ATOM	106	CB	ARG	C	16	−9.865	59.456	13.243	1.00	48.99		C
ATOM	107	CG	ARG	C	16	−10.287	58.203	13.961	1.00	58.16		C
ATOM	108	CD	ARG	C	16	−11.621	58.360	14.645	1.00	60.17		C
ATOM	109	NE	ARG	C	16	−11.592	57.775	15.983	1.00	78.30		N
ATOM	110	CZ	ARG	C	16	−12.669	57.597	16.743	1.00	90.64		C
ATOM	111	NH1	ARG	C	16	−13.866	57.952	16.295	1.00	92.41		N1+
ATOM	112	NH2	ARG	C	16	−12.552	57.058	17.950	1.00	96.43		N
ATOM	113	N	SER	C	17	−10.093	62.174	12.299	1.00	44.14		N
ATOM	114	CA	SER	C	17	−9.731	63.516	11.876	1.00	45.83		C
ATOM	115	C	SER	C	17	−8.490	63.998	12.604	1.00	44.89		C
ATOM	116	O	SER	C	17	−8.207	63.600	13.738	1.00	51.51		O
ATOM	117	CB	SER	C	17	−10.853	64.535	12.132	1.00	45.46		C
ATOM	118	OG	SER	C	17	−11.938	64.263	11.274	1.00	59.74		O
ATOM	119	N	LEU	C	18	−7.817	64.947	11.961	1.00	41.62		N
ATOM	120	CA	LEU	C	18	−6.610	65.573	12.473	1.00	44.03		C
ATOM	121	C	LEU	C	18	−6.536	66.971	11.886	1.00	41.33		C
ATOM	122	O	LEU	C	18	−6.961	67.203	10.756	1.00	44.87		O
ATOM	123	CB	LEU	C	18	−5.366	64.772	12.079	1.00	41.97		C
ATOM	124	CG	LEU	C	18	−4.114	64.794	12.940	1.00	54.29		C
ATOM	125	CD1	LEU	C	18	−4.440	64.407	14.380	1.00	50.61		C
ATOM	126	CD2	LEU	C	18	−3.075	63.836	12.334	1.00	49.38		C
ATOM	127	N	ARG	C	19	−6.000	67.902	12.654	1.00	39.81		N
ATOM	128	CA	ARG	C	19	−5.810	69.262	12.189	1.00	40.64		C
ATOM	129	C	ARG	C	19	−4.334	69.605	12.283	1.00	48.86		C
ATOM	130	O	ARG	C	19	−3.778	69.652	13.386	1.00	48.74		O
ATOM	131	CB	ARG	C	19	−6.650	70.222	13.021	1.00	41.19		C
ATOM	132	CG	ARG	C	19	−6.806	71.632	12.452	1.00	46.04		C
ATOM	133	CD	ARG	C	19	−6.323	72.509	13.554	1.00	49.64		C
ATOM	134	NE	ARG	C	19	−7.182	73.633	13.872	1.00	52.33		N
ATOM	135	CZ	ARG	C	19	−6.947	74.447	14.900	1.00	60.69		C
ATOM	136	NH1	ARG	C	19	−5.914	74.205	15.702	1.00	60.16		N1+
ATOM	137	NH2	ARG	C	19	−7.741	75.487	15.142	1.00	61.67		N
ATOM	138	N	LEU	C	20	−3.716	69.890	11.137	1.00	44.47		N
ATOM	139	CA	LEU	C	20	−2.328	70.331	11.121	1.00	42.17		C
ATOM	140	C	LEU	C	20	−2.270	71.840	11.202	1.00	40.77		C
ATOM	141	O	LEU	C	20	−3.145	72.544	10.691	1.00	39.38		O
ATOM	142	CB	LEU	C	20	−1.591	69.860	9.864	1.00	32.38		C
ATOM	143	CG	LEU	C	20	−1.658	68.360	9.649	1.00	39.39		C
ATOM	144	CD1	LEU	C	20	−0.808	67.907	8.483	1.00	38.47		C
ATOM	145	CD2	LEU	C	20	−1.266	67.633	10.930	1.00	41.15		C
ATOM	146	N	SER	C	21	−1.221	72.328	11.845	1.00	39.02		N
ATOM	147	CA	SER	C	21	−0.951	73.748	11.950	1.00	40.69		C
ATOM	148	C	SER	C	21	0.423	74.053	11.372	1.00	47.84		C
ATOM	149	O	SER	C	21	1.339	73.221	11.416	1.00	45.59		O
ATOM	150	CB	SER	C	21	−1.011	74.211	13.397	1.00	38.57		C
ATOM	151	OG	SER	C	21	−2.330	74.127	13.871	1.00	56.62		O
ATOM	152	N	CYS	C	22	0.546	75.263	10.834	1.00	38.99		N
ATOM	153	CA	CYS	C	22	1.795	75.794	10.299	1.00	44.99		C
ATOM	154	C	CYS	C	22	1.951	77.220	10.827	1.00	46.04		C
ATOM	155	O	CYS	C	22	1.172	78.113	10.465	1.00	41.82		O
ATOM	156	CB	CYS	C	22	1.788	75.761	8.768	1.00	44.73		C
ATOM	157	SG	CYS	C	22	3.139	76.705	7.941	1.00	52.54		S
ATOM	158	N	ALA	C	23	2.921	77.417	11.717	1.00	39.89		N
ATOM	159	CA	ALA	C	23	3.158	78.694	12.375	1.00	39.98		C
ATOM	160	C	ALA	C	23	4.271	79.454	11.659	1.00	41.32		C
ATOM	161	O	ALA	C	23	5.359	78.912	11.428	1.00	44.39		O
ATOM	162	CB	ALA	C	23	3.522	78.488	13.850	1.00	35.18		C
ATOM	163	N	ALA	C	24	3.999	80.703	11.327	1.00	39.85		N
ATOM	164	CA	ALA	C	24	4.895	81.524	10.537	1.00	43.27		C
ATOM	165	C	ALA	C	24	5.477	82.657	11.372	1.00	46.72		C
ATOM	166	O	ALA	C	24	4.801	83.237	12.220	1.00	48.85		O
ATOM	167	CB	ALA	C	24	4.157	82.110	9.339	1.00	38.90		C
ATOM	168	N	SER	C	25	6.720	83.018	11.076	1.00	44.32		N
ATOM	169	CA	SER	C	25	7.328	84.177	11.710	1.00	46.12		C
ATOM	170	C	SER	C	25	8.226	84.874	10.695	1.00	44.36		C
ATOM	171	O	SER	C	25	8.623	84.304	9.673	1.00	43.53		O
ATOM	172	CB	SER	C	25	8.122	83.783	12.966	1.00	46.62		C
ATOM	173	OG	SER	C	25	9.191	82.915	12.642	1.00	42.94		O
ATOM	174	N	GLY	C	26	8.563	86.112	11.001	1.00	46.40		N
ATOM	175	CA	GLY	C	26	9.394	86.915	10.124	1.00	42.45		C
ATOM	176	C	GLY	C	26	8.527	87.884	9.326	1.00	52.00		C
ATOM	177	O	GLY	C	26	7.673	88.572	9.891	1.00	48.03		O
ATOM	178	N	PHE	C	27	8.729	87.910	8.013	1.00	49.49		N
ATOM	179	CA	PHE	C	27	7.986	88.820	7.151	1.00	45.04		C
ATOM	180	C	PHE	C	27	6.479	88.576	7.273	1.00	44.14		C
ATOM	181	O	PHE	C	27	6.025	87.430	7.293	1.00	47.90		O
ATOM	182	CB	PHE	C	27	8.449	88.611	5.712	1.00	45.76		C
ATOM	183	CG	PHE	C	27	7.704	89.421	4.711	1.00	48.04		C
ATOM	184	CD1	PHE	C	27	7.470	90.769	4.937	1.00	50.27		C
ATOM	185	CD2	PHE	C	27	7.236	88.838	3.539	1.00	49.31		C
ATOM	186	CE1	PHE	C	27	6.784	91.537	4.011	1.00	53.69		C
ATOM	187	CE2	PHE	C	27	6.550	89.591	2.606	1.00	47.82		C
ATOM	188	CZ	PHE	C	27	6.320	90.951	2.846	1.00	49.54		C
ATOM	189	N	THR	C	28	5.709	89.671	7.335	1.00	44.86		N
ATOM	190	CA	THR	C	28	4.261	89.693	7.577	1.00	38.38		C
ATOM	191	C	THR	C	28	3.475	88.544	6.941	1.00	42.91		C
ATOM	192	O	THR	C	28	3.343	88.483	5.711	1.00	36.78		O
ATOM	193	CB	THR	C	28	3.679	90.998	7.038	1.00	49.68		C
ATOM	194	OG1	THR	C	28	4.434	92.106	7.536	1.00	46.23		O
ATOM	195	CG2	THR	C	28	2.208	91.133	7.410	1.00	44.54		C
ATOM	196	N	PHE	C	29	2.891	87.687	7.790	1.00	38.44		N
ATOM	197	CA	PHE	C	29	2.154	86.502	7.350	1.00	40.01		C
ATOM	198	C	PHE	C	29	1.089	86.822	6.304	1.00	36.82		C
ATOM	199	O	PHE	C	29	0.942	86.092	5.316	1.00	36.46		O
ATOM	200	CB	PHE	C	29	1.508	85.858	8.571	1.00	39.47		C
ATOM	201	CG	PHE	C	29	0.772	84.586	8.296	1.00	41.07		C
ATOM	202	CD1	PHE	C	29	1.443	83.470	7.809	1.00	39.25		C
ATOM	203	CD2	PHE	C	29	−0.586	84.484	8.581	1.00	37.61		C
ATOM	204	CE1	PHE	C	29	0.782	82.271	7.600	1.00	37.53		C
ATOM	205	CE2	PHE	C	29	−1.260	83.280	8.380	1.00	42.81		C
ATOM	206	CZ	PHE	C	29	−0.575	82.170	7.878	1.00	41.35		C
ATOM	207	N	SER	C	30	0.352	87.917	6.489	1.00	34.06		N
ATOM	208	CA	SER	C	30	−0.719	88.270	5.564	1.00	37.45		C
ATOM	209	C	SER	C	30	−0.200	88.707	4.203	1.00	39.61		C
ATOM	210	O	SER	C	30	−1.018	88.991	3.319	1.00	35.46		O
ATOM	211	CB	SER	C	30	−1.587	89.392	6.141	1.00	31.23		C
ATOM	212	OG	SER	C	30	−0.804	90.566	6.341	1.00	38.68		O
ATOM	213	N	SER	C	31	1.115	88.752	3.998	1.00	31.95		N
ATOM	214	CA	SER	C	31	1.653	89.144	2.705	1.00	42.10		C
ATOM	215	C	SER	C	31	1.858	87.979	1.743	1.00	36.93		C
ATOM	216	O	SER	C	31	2.347	88.199	0.629	1.00	40.45		O
ATOM	217	CB	SER	C	31	2.975	89.887	2.883	1.00	38.00		C
ATOM	218	OG	SER	C	31	2.725	91.165	3.425	1.00	50.55		O
ATOM	219	N	TYR	C	32	1.476	86.759	2.103	1.00	32.77		N
ATOM	220	CA	TYR	C	32	1.671	85.678	1.145	1.00	37.31		C
ATOM	221	C	TYR	C	32	0.613	84.597	1.312	1.00	35.54		C
ATOM	222	O	TYR	C	32	0.059	84.403	2.401	1.00	33.81		O
ATOM	223	CB	TYR	C	32	3.083	85.087	1.282	1.00	33.59		C
ATOM	224	CG	TYR	C	32	3.516	84.779	2.701	1.00	29.77		C
ATOM	225	CD1	TYR	C	32	3.130	83.599	3.315	1.00	33.82		C
ATOM	226	CD2	TYR	C	32	4.353	85.643	3.405	1.00	38.18		C
ATOM	227	CE1	TYR	C	32	3.550	83.271	4.603	1.00	38.72		C
ATOM	228	CE2	TYR	C	32	4.781	85.340	4.703	1.00	39.15		C
ATOM	229	CZ	TYR	C	32	4.365	84.145	5.296	1.00	45.73		C
ATOM	230	OH	TYR	C	32	4.741	83.816	6.579	1.00	41.78		O
ATOM	231	N	GLY	C	33	0.344	83.893	0.209	1.00	34.05		N
ATOM	232	CA	GLY	C	33	−0.428	82.670	0.260	1.00	32.21		C
ATOM	233	C	GLY	C	33	0.446	81.497	0.679	1.00	39.56		C
ATOM	234	O	GLY	C	33	1.665	81.640	0.823	1.00	32.33		O
ATOM	235	N	LEU	C	34	−0.196	80.340	0.907	1.00	32.53		N
ATOM	236	CA	LEU	C	34	0.521	79.169	1.401	1.00	34.46		C
ATOM	237	C	LEU	C	34	−0.060	77.886	0.824	1.00	30.24		C
ATOM	238	O	LEU	C	34	−1.200	77.841	0.360	1.00	33.75		O
ATOM	239	CB	LEU	C	34	0.515	79.085	2.933	1.00	38.99		C
ATOM	240	CG	LEU	C	34	1.236	80.236	3.655	1.00	41.08		C
ATOM	241	CD1	LEU	C	34	0.223	81.245	4.217	1.00	33.75		C
ATOM	242	CD2	LEU	C	34	2.165	79.704	4.725	1.00	35.97		C
ATOM	243	N	HIS	C	35	0.768	76.846	0.863	1.00	31.72		N
ATOM	244	CA	HIS	C	35	0.503	75.507	0.371	1.00	29.96		C
ATOM	245	C	HIS	C	35	0.618	74.498	1.498	1.00	33.37		C
ATOM	246	O	HIS	C	35	1.323	74.717	2.484	1.00	34.65		O
ATOM	247	CB	HIS	C	35	1.534	75.064	−0.671	1.00	31.82		C
ATOM	248	CG	HIS	C	35	1.514	75.835	−1.949	1.00	38.58		C
ATOM	249	ND1	HIS	C	35	0.781	75.435	−3.047	1.00	31.99		N
ATOM	250	CD2	HIS	C	35	2.200	76.940	−2.333	1.00	34.19		C
ATOM	251	CE1	HIS	C	35	1.008	76.269	−4.046	1.00	28.49		C
ATOM	252	NE2	HIS	C	35	1.855	77.197	−3.635	1.00	33.84		N
ATOM	253	N	TRP	C	36	−0.010	73.347	1.298	1.00	29.55		N
ATOM	254	CA	TRP	C	36	0.381	72.110	1.957	1.00	30.04		C
ATOM	255	C	TRP	C	36	0.870	71.151	0.887	1.00	32.99		C
ATOM	256	O	TRP	C	36	0.217	70.995	−0.149	1.00	33.39		O
ATOM	257	CB	TRP	C	36	−0.771	71.490	2.735	1.00	30.51		C
ATOM	258	CG	TRP	C	36	−1.084	72.233	3.977	1.00	36.65		C
ATOM	259	CD1	TRP	C	36	−2.063	73.191	4.152	1.00	36.08		C
ATOM	260	CD2	TRP	C	36	−0.447	72.073	5.246	1.00	33.16		C
ATOM	261	NE1	TRP	C	36	−2.055	73.637	5.456	1.00	34.80		N
ATOM	262	CE2	TRP	C	36	−1.073	72.972	6.146	1.00	31.89		C
ATOM	263	CE3	TRP	C	36	0.602	71.272	5.706	1.00	33.27		C
ATOM	264	CZ2	TRP	C	36	−0.690	73.079	7.475	1.00	35.29		C
ATOM	265	CZ3	TRP	C	36	0.976	71.373	7.022	1.00	36.31		C
ATOM	266	CH2	TRP	C	36	0.334	72.276	7.898	1.00	37.43		C
ATOM	267	N	VAL	C	37	2.037	70.544	1.114	1.00	31.46		N
ATOM	268	CA	VAL	C	37	2.588	69.540	0.215	1.00	28.53		C
ATOM	269	C	VAL	C	37	2.937	68.334	1.066	1.00	37.43		C
ATOM	270	O	VAL	C	37	3.354	68.473	2.221	1.00	38.22		O
ATOM	271	CB	VAL	C	37	3.832	70.056	−0.554	1.00	32.46		C
ATOM	272	CG1	VAL	C	37	4.424	68.959	−1.463	1.00	28.26		C
ATOM	273	CG2	VAL	C	37	3.501	71.313	−1.364	1.00	25.69		C
ATOM	274	N	ARG	C	38	2.787	67.142	0.503	1.00	30.65		N
ATOM	275	CA	ARG	C	38	3.030	65.960	1.303	1.00	35.42		C
ATOM	276	C	ARG	C	38	3.936	64.983	0.565	1.00	33.75		C
ATOM	277	O	ARG	C	38	4.133	65.061	−0.657	1.00	31.48		O
ATOM	278	CB	ARG	C	38	1.721	65.273	1.714	1.00	31.04		C
ATOM	279	CG	ARG	C	38	1.037	64.459	0.654	1.00	31.84		C
ATOM	280	CD	ARG	C	38	−0.318	63.986	1.190	1.00	28.76		C
ATOM	281	NE	ARG	C	38	−1.059	63.233	0.184	1.00	33.40		N
ATOM	282	CZ	ARG	C	38	−2.280	62.718	0.368	1.00	33.79		C
ATOM	283	NH1	ARG	C	38	−2.940	62.867	1.523	1.00	29.44		N1+
ATOM	284	NH2	ARG	C	38	−2.845	62.057	−0.617	1.00	27.56		N
ATOM	285	N	GLN	C	39	4.517	64.077	1.344	1.00	31.44		N
ATOM	286	CA	GLN	C	39	5.466	63.101	0.809	1.00	33.90		C
ATOM	287	C	GLN	C	39	5.299	61.833	1.621	1.00	30.60		C
ATOM	288	O	GLN	C	39	5.589	61.823	2.816	1.00	37.53		O
ATOM	289	CB	GLN	C	39	6.908	63.606	0.880	1.00	29.62		C
ATOM	290	CG	GLN	C	39	7.950	62.614	0.336	1.00	33.68		C
ATOM	291	CD	GLN	C	39	9.317	63.272	0.142	1.00	38.26		C
ATOM	292	OE1	GLN	C	39	9.832	63.941	1.041	1.00	36.27		O
ATOM	293	NE2	GLN	C	39	9.884	63.121	−1.051	1.00	31.46		N
ATOM	294	N	ALA	C	40	4.806	60.795	0.980	1.00	33.74		N
ATOM	295	CA	ALA	C	40	4.687	59.501	1.621	1.00	42.24		C
ATOM	296	C	ALA	C	40	6.082	58.868	1.723	1.00	41.93		C
ATOM	297	O	ALA	C	40	6.967	59.180	0.921	1.00	39.79		O
ATOM	298	CB	ALA	C	40	3.726	58.625	0.811	1.00	21.89		C
ATOM	299	N	PRO	C	41	6.304	57.974	2.691	1.00	47.02		N
ATOM	300	CA	PRO	C	41	7.671	57.444	2.920	1.00	46.31		C
ATOM	301	C	PRO	C	41	8.252	56.774	1.681	1.00	40.48		C
ATOM	302	O	PRO	C	41	7.677	55.834	1.127	1.00	49.95		O
ATOM	303	CB	PRO	C	41	7.475	56.438	4.065	1.00	38.60		C
ATOM	304	CG	PRO	C	41	6.179	56.872	4.754	1.00	43.78		C
ATOM	305	CD	PRO	C	41	5.319	57.433	3.651	1.00	44.84		C
ATOM	306	N	GLY	C	42	9.416	57.254	1.256	1.00	49.67		N
ATOM	307	CA	GLY	C	42	10.049	56.738	0.054	1.00	47.19		C
ATOM	308	C	GLY	C	42	9.476	57.189	−1.279	1.00	48.22		C
ATOM	309	O	GLY	C	42	9.825	56.588	−2.300	1.00	45.62		O
ATOM	310	N	LYS	C	43	8.627	58.223	−1.325	1.00	42.77		N
ATOM	311	CA	LYS	C	43	7.904	58.581	−2.556	1.00	40.19		C
ATOM	312	C	LYS	C	43	8.149	60.040	−2.956	1.00	36.26		C
ATOM	313	O	LYS	C	43	8.895	60.789	−2.310	1.00	41.39		O
ATOM	314	CB	LYS	C	43	6.402	58.338	−2.390	1.00	43.74		C
ATOM	315	CG	LYS	C	43	6.020	56.900	−2.068	1.00	44.39		C
ATOM	316	CD	LYS	C	43	6.527	55.936	−3.112	1.00	56.25		C
ATOM	317	CE	LYS	C	43	5.920	54.540	−2.918	1.00	72.49		C
ATOM	318	NZ	LYS	C	43	6.709	53.467	−3.617	1.00	73.82		N1+
ATOM	319	N	GLY	C	44	7.498	60.457	−4.036	1.00	35.63		N
ATOM	320	CA	GLY	C	44	7.709	61.788	−4.551	1.00	29.55		C
ATOM	321	C	GLY	C	44	6.833	62.802	−3.843	1.00	34.99		C
ATOM	322	O	GLY	C	44	6.008	62.475	−2.990	1.00	36.77		O
ATOM	323	N	LEU	C	45	7.026	64.067	−4.205	1.00	30.55		N
ATOM	324	CA	LEU	C	45	6.192	65.134	−3.664	1.00	32.18		C
ATOM	325	C	LEU	C	45	4.783	65.057	−4.257	1.00	31.76		C
ATOM	326	O	LEU	C	45	4.597	64.740	−5.440	1.00	25.93		O
ATOM	327	CB	LEU	C	45	6.820	66.508	−3.939	1.00	31.66		C
ATOM	328	CG	LEU	C	45	8.233	66.714	−3.370	1.00	32.55		C
ATOM	329	CD1	LEU	C	45	8.776	68.091	−3.682	1.00	27.48		C
ATOM	330	CD2	LEU	C	45	8.219	66.491	−1.871	1.00	28.43		C
ATOM	331	N	GLU	C	46	3.784	65.298	−3.413	1.00	27.12		N
ATOM	332	CA	GLU	C	46	2.404	65.402	−3.865	1.00	32.84		C
ATOM	333	C	GLU	C	46	1.799	66.669	−3.286	1.00	32.06		C
ATOM	334	O	GLU	C	46	1.754	66.837	−2.062	1.00	31.76		O
ATOM	335	CB	GLU	C	46	1.579	64.183	−3.451	1.00	36.78		C
ATOM	336	CG	GLU	C	46	0.226	64.173	−4.126	1.00	44.38		C
ATOM	337	CD	GLU	C	46	−0.758	63.166	−3.539	1.00	46.89		C
ATOM	338	OE1	GLU	C	46	−0.435	62.467	−2.548	1.00	45.34		O
ATOM	339	OE2	GLU	C	46	−1.871	63.088	−4.092	1.00	50.23		O1−
ATOM	340	N	TRP	C	47	1.330	67.548	−4.162	1.00	27.92		N
ATOM	341	CA	TRP	C	47	0.676	68.764	−3.715	1.00	31.90		C
ATOM	342	C	TRP	C	47	−0.664	68.439	−3.079	1.00	31.01		C
ATOM	343	O	TRP	C	47	−1.386	67.555	−3.546	1.00	32.31		O
ATOM	344	CB	TRP	C	47	0.485	69.713	−4.900	1.00	35.33		C
ATOM	345	CG	TRP	C	47	−0.297	70.972	−4.630	1.00	30.11		C
ATOM	346	CD1	TRP	C	47	0.104	72.068	−3.910	1.00	29.39		C
ATOM	347	CD2	TRP	C	47	−1.616	71.270	−5.118	1.00	29.40		C
ATOM	348	NE1	TRP	C	47	−0.886	73.032	−3.925	1.00	32.24		N
ATOM	349	CE2	TRP	C	47	−1.952	72.563	−4.660	1.00	34.57		C
ATOM	350	CE3	TRP	C	47	−2.534	70.575	−5.913	1.00	30.62		C
ATOM	351	CZ2	TRP	C	47	−3.190	73.165	−4.958	1.00	29.29		C
ATOM	352	CZ3	TRP	C	47	−3.764	71.177	−6.215	1.00	31.59		C
ATOM	353	CH2	TRP	C	47	−4.075	72.459	−5.736	1.00	32.18		C
ATOM	354	N	VAL	C	48	−1.010	69.189	−2.031	1.00	31.17		N
ATOM	355	CA	VAL	C	48	−2.268	69.019	−1.303	1.00	28.29		C
ATOM	356	C	VAL	C	48	−3.239	70.192	−1.553	1.00	34.03		C
ATOM	357	O	VAL	C	48	−4.371	69.989	−2.002	1.00	29.40		O
ATOM	358	CB	VAL	C	48	−2.007	68.824	0.206	1.00	29.92		C
ATOM	359	CG1	VAL	C	48	−3.321	68.671	0.944	1.00	32.67		C
ATOM	360	CG2	VAL	C	48	−1.117	67.606	0.433	1.00	28.26		C
ATOM	361	N	ALA	C	49	−2.825	71.421	−1.237	1.00	30.79		N
ATOM	362	CA	ALA	C	49	−3.747	72.546	−1.373	1.00	31.82		C
ATOM	363	C	ALA	C	49	−2.974	73.854	−1.325	1.00	32.29		C
ATOM	364	O	ALA	C	49	−1.845	73.908	−0.823	1.00	30.87		O
ATOM	365	CB	ALA	C	49	−4.821	72.517	−0.277	1.00	30.36		C
ATOM	366	N	AVAL	C	50	−3.605	74.914	−1.835	0.50	31.84		N
ATOM	367	CA	AVAL	C	50	−3.060	76.269	−1.763	0.50	30.56		C
ATOM	368	C	AVAL	C	50	−4.179	77.222	−1.373	0.50	31.68		C
ATOM	369	O	AVAL	C	50	−5.333	77.047	−1.784	0.50	29.47		O
ATOM	370	CB	AVAL	C	50	−2.408	76.711	−3.093	0.50	30.12		C
ATOM	371	CG1	AVAL	C	50	−3.459	76.855	−4.204	0.50	28.96		C
ATOM	372	CG2	AVAL	C	50	−1.624	77.987	−2.912	0.50	24.87		C
ATOM	373	N	BVAL	C	50	−3.584	74.900	−1.900	0.50	32.14		N
ATOM	374	CA	BVAL	C	50	−3.117	76.279	−1.776	0.50	30.77		C
ATOM	375	C	BVAL	C	50	−4.231	77.106	−1.160	0.50	31.70		C
ATOM	376	O	BVAL	C	50	−5.415	76.765	−1.240	0.50	30.32		O
ATOM	377	CB	BVAL	C	50	−2.698	76.932	−3.115	0.50	30.01		C
ATOM	378	CG1	BVAL	C	50	−2.103	75.960	−4.000	0.50	36.11		C
ATOM	379	CG2	BVAL	C	50	−3.896	77.491	−3.831	0.50	31.66		C
ATOM	380	N	ILE	C	51	−3.834	78.232	−0.574	1.00	31.49		N
ATOM	381	CA	ILE	C	51	−4.770	79.260	−0.151	1.00	28.89		C
ATOM	382	C	ILE	C	51	−4.143	80.593	−0.519	1.00	37.27		C
ATOM	383	O	ILE	C	51	−2.913	80.736	−0.534	1.00	32.74		O
ATOM	384	CB	ILE	C	51	−5.085	79.203	1.356	1.00	33.18		C
ATOM	385	CG1	ILE	C	51	−6.238	80.154	1.691	1.00	31.97		C
ATOM	386	CG2	ILE	C	51	−3.837	79.550	2.210	1.00	26.57		C
ATOM	387	CD1	ILE	C	51	−6.766	79.971	3.093	1.00	31.63		C
ATOM	388	N	TRP	C	52	−5.000	81.561	−0.838	1.00	30.70		N
ATOM	389	CA	TRP	C	52	−4.563	82.882	−1.241	1.00	25.99		C
ATOM	390	C	TRP	C	52	−4.040	83.652	−0.036	1.00	29.12		C
ATOM	391	O	TRP	C	52	−4.302	83.303	1.117	1.00	36.14		O
ATOM	392	CB	TRP	C	52	−5.722	83.638	−1.898	1.00	27.78		C
ATOM	393	CG	TRP	C	52	−5.405	84.135	−3.270	1.00	33.59		C
ATOM	394	CD1	TRP	C	52	−5.333	85.445	−3.676	1.00	32.68		C
ATOM	395	CD2	TRP	C	52	−5.102	83.340	−4.426	1.00	30.76		C
ATOM	396	NE1	TRP	C	52	−5.004	85.510	−5.010	1.00	32.81		N
ATOM	397	CE2	TRP	C	52	−4.853	84.235	−5.495	1.00	33.10		C
ATOM	398	CE3	TRP	C	52	−4.989	81.962	−4.657	1.00	33.14		C
ATOM	399	CZ2	TRP	C	52	−4.516	83.792	−6.779	1.00	32.67		C
ATOM	400	CZ3	TRP	C	52	−4.670	81.524	−5.941	1.00	33.56		C
ATOM	401	CH2	TRP	C	52	−4.435	82.436	−6.983	1.00	32.43		C
ATOM	402	N	TYR	C	53	−3.304	84.726	−0.315	1.00	29.93		N
ATOM	403	CA	TYR	C	53	−2.784	85.558	0.768	1.00	38.06		C
ATOM	404	C	TYR	C	53	−3.898	86.148	1.630	1.00	40.02		C
ATOM	405	O	TYR	C	53	−3.690	86.389	2.829	1.00	43.14		O
ATOM	406	CB	TYR	C	53	−1.915	86.685	0.203	1.00	36.99		C
ATOM	407	CG	TYR	C	53	−2.522	87.380	−0.992	1.00	42.26		C
ATOM	408	CD1	TYR	C	53	−3.449	88.409	−0.831	1.00	39.71		C
ATOM	409	CD2	TYR	C	53	−2.172	86.999	−2.290	1.00	38.52		C
ATOM	410	CE1	TYR	C	53	−4.015	89.042	−1.927	1.00	38.70		C
ATOM	411	CE2	TYR	C	53	−2.720	87.631	−3.397	1.00	43.88		C
ATOM	412	CZ	TYR	C	53	−3.647	88.654	−3.211	1.00	46.93		C
ATOM	413	OH	TYR	C	53	−4.205	89.264	−4.318	1.00	49.29		O
ATOM	414	N	ASP	C	54	−5.082	86.385	1.058	1.00	35.51		N
ATOM	415	CA	ASP	C	54	−6.200	86.943	1.811	1.00	38.58		C
ATOM	416	C	ASP	C	54	−7.258	85.899	2.166	1.00	37.13		C
ATOM	417	O	ASP	C	54	−8.397	86.262	2.468	1.00	42.80		O
ATOM	418	CB	ASP	C	54	−6.839	88.093	1.036	1.00	35.61		C
ATOM	419	CG	ASP	C	54	−7.319	87.664	−0.336	1.00	39.47		C
ATOM	420	OD1	ASP	C	54	−7.355	86.435	−0.617	1.00	40.37		O
ATOM	421	OD2	ASP	C	54	−7.678	88.551	−1.129	1.00	40.04		O1−
ATOM	422	N	GLY	C	55	−6.921	84.614	2.110	1.00	38.50		N
ATOM	423	CA	GLY	C	55	−7.878	83.579	2.451	1.00	30.61		C
ATOM	424	C	GLY	C	55	−9.007	83.374	1.465	1.00	39.39		C
ATOM	425	O	GLY	C	55	−9.946	82.625	1.773	1.00	37.86		O
ATOM	426	N	SER	C	56	−8.944	83.988	0.276	1.00	37.78		N
ATOM	427	CA	SER	C	56	−10.036	83.866	−0.689	1.00	30.88		C
ATOM	428	C	SER	C	56	−9.948	82.566	−1.485	1.00	29.51		C
ATOM	429	O	SER	C	56	−10.561	81.560	−1.107	1.00	35.66		O
ATOM	430	CB	SER	C	56	−10.050	85.075	−1.634	1.00	31.22		C
ATOM	431	OG	SER	C	56	−8.824	85.214	−2.331	1.00	32.22		O
ATOM	432	N	ASN	C	57	−9.192	82.555	−2.578	1.00	28.37		N
ATOM	433	CA	ASN	C	57	−9.143	81.363	−3.423	1.00	35.02		C
ATOM	434	C	ASN	C	57	−8.480	80.196	−2.691	1.00	32.70		C
ATOM	435	O	ASN	C	57	−7.544	80.388	−1.909	1.00	29.84		O
ATOM	436	CB	ASN	C	57	−8.407	81.655	−4.733	1.00	29.59		C
ATOM	437	CG	ASN	C	57	−9.224	82.532	−5.682	1.00	35.30		C
ATOM	438	OD1	ASN	C	57	−10.082	83.295	−5.248	1.00	31.05		O
ATOM	439	ND2	ASN	C	57	−8.982	82.390	−6.988	1.00	33.63		N
ATOM	440	N	LYS	C	58	−9.018	78.992	−2.915	1.00	28.81		N
ATOM	441	CA	LYS	C	58	−8.510	77.731	−2.374	1.00	33.21		C
ATOM	442	C	LYS	C	58	−8.561	76.699	−3.485	1.00	31.65		C
ATOM	443	O	LYS	C	58	−9.609	76.539	−4.111	1.00	31.96		O
ATOM	444	CB	LYS	C	58	−9.356	77.210	−1.201	1.00	29.22		C
ATOM	445	CG	LYS	C	58	−9.438	78.136	−0.030	1.00	39.00		C
ATOM	446	CD	LYS	C	58	−10.443	77.655	1.024	1.00	28.02		C
ATOM	447	CE	LYS	C	58	−10.456	78.663	2.179	1.00	29.93		C
ATOM	448	NZ	LYS	C	58	−11.039	78.171	3.465	1.00	34.24		N1+
ATOM	449	N	TYR	C	59	−7.465	75.969	−3.693	1.00	33.17		N
ATOM	450	CA	TYR	C	59	−7.402	74.893	−4.680	1.00	31.69		C
ATOM	451	C	TYR	C	59	−6.931	73.623	−3.988	1.00	32.39		C
ATOM	452	O	TYR	C	59	−6.165	73.681	−3.025	1.00	32.73		O
ATOM	453	CB	TYR	C	59	−6.450	75.203	−5.856	1.00	33.11		C
ATOM	454	CG	TYR	C	59	−6.646	76.536	−6.574	1.00	41.69		C
ATOM	455	CD1	TYR	C	59	−6.539	77.741	−5.914	1.00	48.94		C
ATOM	456	CD2	TYR	C	59	−6.892	76.574	−7.925	1.00	52.57		C
ATOM	457	CE1	TYR	C	59	−6.714	78.936	−6.579	1.00	54.05		C
ATOM	458	CE2	TYR	C	59	−7.055	77.762	−8.590	1.00	51.75		C
ATOM	459	CZ	TYR	C	59	−6.973	78.936	−7.916	1.00	42.38		C
ATOM	460	OH	TYR	C	59	−7.155	80.120	−8.583	1.00	40.63		O
ATOM	461	N	TYR	C	60	−7.401	72.470	−4.475	1.00	28.26		N
ATOM	462	CA	TYR	C	60	−7.080	71.205	−3.835	1.00	26.89		C
ATOM	463	C	TYR	C	60	−6.720	70.156	−4.864	1.00	32.21		C
ATOM	464	O	TYR	C	60	−7.276	70.128	−5.967	1.00	30.27		O
ATOM	465	CB	TYR	C	60	−8.232	70.657	−3.004	1.00	28.01		C
ATOM	466	CG	TYR	C	60	−8.665	71.517	−1.854	1.00	34.24		C
ATOM	467	CD1	TYR	C	60	−9.607	72.540	−2.036	1.00	31.75		C
ATOM	468	CD2	TYR	C	60	−8.169	71.297	−0.570	1.00	31.69		C
ATOM	469	CE1	TYR	C	60	−10.020	73.341	−0.963	1.00	28.22		C
ATOM	470	CE2	TYR	C	60	−8.595	72.093	0.512	1.00	30.87		C
ATOM	471	CZ	TYR	C	60	−9.516	73.111	0.301	1.00	28.55		C
ATOM	472	OH	TYR	C	60	−9.924	73.903	1.354	1.00	30.94		O
ATOM	473	N	ALA	C	61	−5.807	69.267	−4.468	1.00	27.28		N
ATOM	474	CA	ALA	C	61	−5.533	68.075	−5.252	1.00	28.59		C
ATOM	475	C	ALA	C	61	−6.745	67.149	−5.238	1.00	34.61		C
ATOM	476	O	ALA	C	61	−7.493	67.080	−4.260	1.00	31.50		O
ATOM	477	CB	ALA	C	61	−4.315	67.342	−4.706	1.00	23.81		C
ATOM	478	N	ASP	C	62	−6.920	66.423	−6.341	1.00	38.58		N
ATOM	479	CA	ASP	C	62	−8.069	65.537	−6.487	1.00	40.90		C
ATOM	480	C	ASP	C	62	−8.129	64.490	−5.382	1.00	41.29		C
ATOM	481	O	ASP	C	62	−9.210	64.175	−4.884	1.00	43.64		O
ATOM	482	CB	ASP	C	62	−8.027	64.862	−7.858	1.00	41.48		C
ATOM	483	CG	ASP	C	62	−8.775	65.657	−8.908	1.00	52.54		C
ATOM	484	OD1	ASP	C	62	−9.074	66.853	−8.639	1.00	50.91		O
ATOM	485	OD2	ASP	C	62	−9.074	65.083	−9.984	1.00	54.03		O1−
ATOM	486	N	SER	C	63	−6.978	63.960	−4.967	1.00	38.35		N
ATOM	487	CA	SER	C	63	−6.931	62.918	−3.948	1.00	40.77		C
ATOM	488	C	SER	C	63	−7.429	63.398	−2.589	1.00	41.73		C
ATOM	489	O	SER	C	63	−7.557	62.586	−1.666	1.00	37.97		O
ATOM	490	CB	SER	C	63	−5.493	62.386	−3.804	1.00	39.37		C
ATOM	491	OG	SER	C	63	−4.582	63.445	−3.547	1.00	39.82		O
ATOM	492	N	VAL	C	64	−7.730	64.681	−2.445	1.00	37.08		N
ATOM	493	CA	VAL	C	64	−7.937	65.265	−1.130	1.00	34.49		C
ATOM	494	C	VAL	C	64	−9.234	66.090	−1.105	1.00	35.91		C
ATOM	495	O	VAL	C	64	−9.766	66.419	−0.033	1.00	35.61		O
ATOM	496	CB	VAL	C	64	−6.652	66.052	−0.800	1.00	37.75		C
ATOM	497	CG1	VAL	C	64	−6.895	67.438	−0.272	1.00	34.28		C
ATOM	498	CG2	VAL	C	64	−5.734	65.214	0.078	1.00	37.52		C
ATOM	499	N	LYS	C	65	−9.774	66.389	−2.294	1.00	33.05		N
ATOM	500	CA	LYS	C	65	−11.007	67.169	−2.424	1.00	35.12		C
ATOM	501	C	LYS	C	65	−12.143	66.581	−1.599	1.00	41.45		C
ATOM	502	O	LYS	C	65	−12.378	65.368	−1.600	1.00	37.85		O
ATOM	503	CB	LYS	C	65	−11.463	67.244	−3.888	1.00	35.87		C
ATOM	504	CG	LYS	C	65	−10.771	68.290	−4.714	1.00	35.54		C
ATOM	505	CD	LYS	C	65	−11.454	68.428	−6.057	1.00	42.42		C
ATOM	506	CE	LYS	C	65	−10.975	69.680	−6.795	1.00	38.45		C
ATOM	507	NZ	LYS	C	65	−9.588	69.479	−7.281	1.00	40.01		N1+
ATOM	508	N	GLY	C	66	−12.876	67.460	−0.925	1.00	38.42		N
ATOM	509	CA	GLY	C	66	−14.008	67.048	−0.131	1.00	34.79		C
ATOM	510	C	GLY	C	66	−13.656	66.580	1.252	1.00	43.32		C
ATOM	511	O	GLY	C	66	−14.504	66.628	2.139	1.00	44.56		O
ATOM	512	N	ARG	C	67	−12.416	66.177	1.488	1.00	42.85		N
ATOM	513	CA	ARG	C	67	−12.040	65.681	2.798	1.00	33.59		C
ATOM	514	C	ARG	C	67	−11.185	66.653	3.587	1.00	38.28		C
ATOM	515	O	ARG	C	67	−11.308	66.698	4.812	1.00	35.39		O
ATOM	516	CB	ARG	C	67	−11.317	64.333	2.663	1.00	38.43		C
ATOM	517	CG	ARG	C	67	−12.241	63.220	2.171	1.00	33.48		C
ATOM	518	CD	ARG	C	67	−11.540	61.860	2.172	1.00	39.76		C
ATOM	519	NE	ARG	C	67	−10.284	61.891	1.423	1.00	38.65		N
ATOM	520	CZ	ARG	C	67	−9.081	61.717	1.967	1.00	39.28		C
ATOM	521	NH1	ARG	C	67	−8.981	61.482	3.259	1.00	31.68		N1+
ATOM	522	NH2	ARG	C	67	−7.977	61.785	1.224	1.00	36.70		N
ATOM	523	N	PHE	C	68	−10.304	67.413	2.922	1.00	37.96		N
ATOM	524	CA	PHE	C	68	−9.395	68.344	3.576	1.00	30.65		C
ATOM	525	C	PHE	C	68	−9.874	69.766	3.351	1.00	34.00		C
ATOM	526	O	PHE	C	68	−10.488	70.071	2.325	1.00	36.05		O
ATOM	527	CB	PHE	C	68	−7.959	68.224	3.047	1.00	37.02		C
ATOM	528	CG	PHE	C	68	−7.264	66.900	3.360	1.00	38.71		C
ATOM	529	CD1	PHE	C	68	−7.954	65.814	3.888	1.00	35.33		C
ATOM	530	CD2	PHE	C	68	−5.894	66.767	3.140	1.00	37.81		C
ATOM	531	CE1	PHE	C	68	−7.299	64.615	4.164	1.00	36.61		C
ATOM	532	CE2	PHE	C	68	−5.218	65.569	3.425	1.00	33.40		C
ATOM	533	CZ	PHE	C	68	−5.919	64.498	3.934	1.00	40.51		C
ATOM	534	N	THR	C	69	−9.582	70.646	4.307	1.00	35.34		N
ATOM	535	CA	THR	C	69	−9.924	72.055	4.163	1.00	29.08		C
ATOM	536	C	THR	C	69	−8.743	72.900	4.621	1.00	31.52		C
ATOM	537	O	THR	C	69	−8.229	72.710	5.725	1.00	33.87		O
ATOM	538	CB	THR	C	69	−11.198	72.407	4.954	1.00	32.76		C
ATOM	539	OG1	THR	C	69	−12.294	71.663	4.427	1.00	36.96		O
ATOM	540	CG2	THR	C	69	−11.545	73.923	4.828	1.00	25.39		C
ATOM	541	N	ILE	C	70	−8.309	73.827	3.778	1.00	33.09		N
ATOM	542	CA	ILE	C	70	−7.201	74.720	4.113	1.00	29.02		C
ATOM	543	C	ILE	C	70	−7.786	76.038	4.602	1.00	32.22		C
ATOM	544	O	ILE	C	70	−8.810	76.503	4.093	1.00	33.11		O
ATOM	545	CB	ILE	C	70	−6.265	74.911	2.899	1.00	35.27		C
ATOM	546	CG1	ILE	C	70	−4.942	75.579	3.288	1.00	31.47		C
ATOM	547	CG2	ILE	C	70	−6.939	75.726	1.800	1.00	23.76		C
ATOM	548	CD1	ILE	C	70	−3.965	75.590	2.138	1.00	31.12		C
ATOM	549	N	SER	C	71	−7.174	76.618	5.627	1.00	35.69		N
ATOM	550	CA	SER	C	71	−7.670	77.883	6.153	1.00	38.73		C
ATOM	551	C	SER	C	71	−6.513	78.588	6.845	1.00	37.39		C
ATOM	552	O	SER	C	71	−5.444	78.009	7.046	1.00	41.40		O
ATOM	553	CB	SER	C	71	−8.849	77.655	7.100	1.00	37.80		C
ATOM	554	OG	SER	C	71	−8.444	76.880	8.217	1.00	38.72		O
ATOM	555	N	ARG	C	72	−6.726	79.852	7.204	1.00	35.68		N
ATOM	556	CA	ARG	C	72	−5.674	80.600	7.876	1.00	36.89		C
ATOM	557	C	ARG	C	72	−6.274	81.545	8.908	1.00	40.29		C
ATOM	558	O	ARG	C	72	−7.421	81.973	8.791	1.00	38.24		O
ATOM	559	CB	ARG	C	72	−4.825	81.385	6.864	1.00	35.87		C
ATOM	560	CG	ARG	C	72	−5.636	82.390	6.057	1.00	34.72		C
ATOM	561	CD	ARG	C	72	−4.828	82.983	4.903	1.00	30.54		C
ATOM	562	NE	ARG	C	72	−3.674	83.722	5.397	1.00	39.63		N
ATOM	563	CZ	ARG	C	72	−2.575	83.951	4.694	1.00	41.45		C
ATOM	564	NH1	ARG	C	72	−2.475	83.499	3.449	1.00	37.50		N1+
ATOM	565	NH2	ARG	C	72	−1.579	84.643	5.240	1.00	38.82		N
ATOM	566	N	ASP	C	73	−5.478	81.878	9.920	1.00	38.55		N
ATOM	567	CA	ASP	C	73	−5.852	82.875	10.919	1.00	40.45		C
ATOM	568	C	ASP	C	73	−4.704	83.871	11.015	1.00	44.31		C
ATOM	569	O	ASP	C	73	−3.699	83.601	11.676	1.00	47.19		O
ATOM	570	CB	ASP	C	73	−6.142	82.239	12.277	1.00	45.34		C
ATOM	571	CG	ASP	C	73	−6.685	83.247	13.303	1.00	48.06		C
ATOM	572	OD1	ASP	C	73	−6.492	84.479	13.138	1.00	54.90		O
ATOM	573	OD2	ASP	C	73	−7.277	82.797	14.305	1.00	53.87		O1−
ATOM	574	N	ASN	C	74	−4.865	85.028	10.374	1.00	39.84		N
ATOM	575	CA	ASN	C	74	−3.778	85.991	10.341	1.00	43.99		C
ATOM	576	C	ASN	C	74	−3.450	86.497	11.739	1.00	48.38		C
ATOM	577	O	ASN	C	74	−2.282	86.767	12.040	1.00	55.63		O
ATOM	578	CB	ASN	C	74	−4.126	87.136	9.385	1.00	39.05		C
ATOM	579	CG	ASN	C	74	−3.974	86.735	7.922	1.00	46.52		C
ATOM	580	OD1	ASN	C	74	−3.620	85.591	7.606	1.00	45.49		O
ATOM	581	ND2	ASN	C	74	−4.238	87.668	7.024	1.00	41.67		N
ATOM	582	N	SER	C	75	−4.444	86.570	12.626	1.00	52.35		N
ATOM	583	CA	SER	C	75	−4.172	87.063	13.973	1.00	49.93		C
ATOM	584	C	SER	C	75	−3.251	86.138	14.759	1.00	51.44		C
ATOM	585	O	SER	C	75	−2.606	86.596	15.705	1.00	53.63		O
ATOM	586	CB	SER	C	75	−5.480	87.277	14.735	1.00	45.73		C
ATOM	587	OG	SER	C	75	−6.025	86.059	15.205	1.00	53.39		O
ATOM	588	N	LYS	C	76	−3.158	84.860	14.387	1.00	49.51		N
ATOM	589	CA	LYS	C	76	−2.235	83.925	15.018	1.00	43.14		C
ATOM	590	C	LYS	C	76	−1.069	83.563	14.114	1.00	50.55		C
ATOM	591	O	LYS	C	76	−0.325	82.632	14.440	1.00	45.43		O
ATOM	592	CB	LYS	C	76	−2.951	82.633	15.422	1.00	45.66		C
ATOM	593	CG	LYS	C	76	−4.185	82.802	16.282	1.00	49.74		C
ATOM	594	CD	LYS	C	76	−4.789	81.447	16.612	1.00	50.31		C
ATOM	595	CE	LYS	C	76	−6.149	81.588	17.303	1.00	56.50		C
ATOM	596	NZ	LYS	C	76	−6.769	80.256	17.607	1.00	68.70		N1+
ATOM	597	N	ASN	C	77	−0.896	84.275	12.992	1.00	47.54		N
ATOM	598	CA	ASN	C	77	0.093	83.953	11.963	1.00	44.06		C
ATOM	599	C	ASN	C	77	0.174	82.458	11.667	1.00	45.22		C
ATOM	600	O	ASN	C	77	1.278	81.913	11.537	1.00	43.31		O
ATOM	601	CB	ASN	C	77	1.470	84.476	12.358	1.00	41.59		C
ATOM	602	CG	ASN	C	77	1.530	85.984	12.365	1.00	44.41		C
ATOM	603	OD1	ASN	C	77	0.827	86.646	11.609	1.00	48.47		O
ATOM	604	ND2	ASN	C	77	2.354	86.535	13.232	1.00	44.19		N
ATOM	605	N	THR	C	78	−0.981	81.789	11.547	1.00	36.70		N
ATOM	606	CA	THR	C	78	−1.021	80.336	11.472	1.00	40.83		C
ATOM	607	C	THR	C	78	−1.861	79.905	10.280	1.00	44.26		C
ATOM	608	O	THR	C	78	−2.909	80.500	10.003	1.00	37.17		O
ATOM	609	CB	THR	C	78	−1.599	79.724	12.774	1.00	40.36		C
ATOM	610	OG1	THR	C	78	−0.819	80.156	13.888	1.00	45.18		O
ATOM	611	CG2	THR	C	78	−1.572	78.205	12.739	1.00	38.53		C
ATOM	612	N	LEU	C	79	−1.365	78.886	9.574	1.00	39.56		N
ATOM	613	CA	LEU	C	79	−2.067	78.174	8.513	1.00	33.74		C
ATOM	614	C	LEU	C	79	−2.557	76.821	9.033	1.00	37.68		C
ATOM	615	O	LEU	C	79	−1.875	76.162	9.822	1.00	39.25		O
ATOM	616	CB	LEU	C	79	−1.133	77.969	7.307	1.00	40.59		C
ATOM	617	CG	LEU	C	79	−1.615	77.032	6.178	1.00	40.09		C
ATOM	618	CD1	LEU	C	79	−2.574	77.739	5.277	1.00	28.75		C
ATOM	619	CD2	LEU	C	79	−0.476	76.386	5.372	1.00	31.11		C
ATOM	620	N	TYR	C	80	−3.738	76.399	8.599	1.00	35.37		N
ATOM	621	CA	TYR	C	80	−4.296	75.136	9.067	1.00	38.96		C
ATOM	622	C	TYR	C	80	−4.592	74.197	7.909	1.00	36.52		C
ATOM	623	O	TYR	C	80	−4.895	74.629	6.798	1.00	37.65		O
ATOM	624	CB	TYR	C	80	−5.592	75.328	9.872	1.00	36.20		C
ATOM	625	CG	TYR	C	80	−5.421	76.193	11.073	1.00	41.77		C
ATOM	626	CD1	TYR	C	80	−4.830	75.697	12.234	1.00	41.02		C
ATOM	627	CD2	TYR	C	80	−5.845	77.516	11.052	1.00	39.70		C
ATOM	628	CE1	TYR	C	80	−4.655	76.511	13.345	1.00	44.22		C
ATOM	629	CE2	TYR	C	80	−5.685	78.340	12.152	1.00	40.29		C
ATOM	630	CZ	TYR	C	80	−5.089	77.837	13.297	1.00	49.44		C
ATOM	631	OH	TYR	C	80	−4.938	78.666	14.388	1.00	54.21		O
ATOM	632	N	LEU	C	81	−4.520	72.901	8.194	1.00	36.72		N
ATOM	633	CA	LEU	C	81	−5.055	71.869	7.317	1.00	41.79		C
ATOM	634	C	LEU	C	81	−5.970	70.979	8.151	1.00	40.31		C
ATOM	635	O	LEU	C	81	−5.497	70.223	9.006	1.00	40.72		O
ATOM	636	CB	LEU	C	81	−3.943	71.050	6.665	1.00	36.53		C
ATOM	637	CG	LEU	C	81	−4.473	70.006	5.677	1.00	29.95		C
ATOM	638	CD1	LEU	C	81	−5.070	70.688	4.452	1.00	35.27		C
ATOM	639	CD2	LEU	C	81	−3.369	69.024	5.277	1.00	31.44		C
ATOM	640	N	GLN	C	82	−7.274	71.101	7.926	1.00	38.93		N
ATOM	641	CA	GLN	C	82	−8.277	70.254	8.566	1.00	35.95		C
ATOM	642	C	GLN	C	82	−8.454	68.996	7.728	1.00	36.48		C
ATOM	643	O	GLN	C	82	−8.834	69.081	6.557	1.00	41.11		O
ATOM	644	CB	GLN	C	82	−9.606	71.009	8.718	1.00	32.87		C
ATOM	645	CG	GLN	C	82	−10.720	70.190	9.383	1.00	27.13		C
ATOM	646	CD	GLN	C	82	−10.339	69.723	10.783	1.00	41.21		C
ATOM	647	OE1	GLN	C	82	−9.875	70.511	11.621	1.00	41.00		O
ATOM	648	NE2	GLN	C	82	−10.466	68.418	11.018	1.00	37.49		N
ATOM	649	N	MET	C	83	−8.136	67.839	8.304	1.00	36.04		N
ATOM	650	CA	MET	C	83	−8.151	66.557	7.594	1.00	39.43		C
ATOM	651	C	MET	C	83	−9.242	65.670	8.174	1.00	41.49		C
ATOM	652	O	MET	C	83	−9.145	65.225	9.321	1.00	46.39		O
ATOM	653	CB	MET	C	83	−6.791	65.854	7.669	1.00	42.85		C
ATOM	654	CG	MET	C	83	−5.616	66.618	7.030	1.00	44.37		C
ATOM	655	SD	MET	C	83	−4.047	65.719	7.166	1.00	45.89		S
ATOM	656	CE	MET	C	83	−3.833	65.851	8.911	1.00	41.39		C
ATOM	657	N	ASN	C	84	−10.284	65.432	7.400	1.00	37.96		N
ATOM	658	CA	ASN	C	84	−11.368	64.560	7.811	1.00	38.76		C
ATOM	659	C	ASN	C	84	−11.332	63.268	7.002	1.00	40.86		C
ATOM	660	O	ASN	C	84	−10.744	63.205	5.918	1.00	40.04		O
ATOM	661	CB	ASN	C	84	−12.715	65.273	7.649	1.00	33.01		C
ATOM	662	CG	ASN	C	84	−12.807	66.525	8.498	1.00	37.92		C
ATOM	663	OD1	ASN	C	84	−12.179	66.617	9.548	1.00	46.79		O
ATOM	664	ND2	ASN	C	84	−13.617	67.480	8.071	1.00	40.77		N
ATOM	665	N	SER	C	85	−11.956	62.226	7.547	1.00	43.43		N
ATOM	666	CA	SER	C	85	−12.072	60.945	6.852	1.00	40.65		C
ATOM	667	C	SER	C	85	−10.714	60.421	6.406	1.00	39.67		C
ATOM	668	O	SER	C	85	−10.529	60.022	5.252	1.00	36.84		O
ATOM	669	CB	SER	C	85	−13.010	61.055	5.654	1.00	38.73		C
ATOM	670	OG	SER	C	85	−14.333	61.254	6.094	1.00	48.16		O
ATOM	671	N	LEU	C	86	−9.757	60.421	7.331	1.00	38.73		N
ATOM	672	CA	LEU	C	86	−8.390	60.056	6.977	1.00	37.86		C
ATOM	673	C	LEU	C	86	−8.328	58.625	6.457	1.00	38.76		C
ATOM	674	O	LEU	C	86	−9.063	57.749	6.909	1.00	43.94		O
ATOM	675	CB	LEU	C	86	−7.471	60.241	8.184	1.00	39.02		C
ATOM	676	CG	LEU	C	86	−7.098	61.711	8.395	1.00	38.85		C
ATOM	677	CD1	LEU	C	86	−6.467	61.983	9.765	1.00	37.48		C
ATOM	678	CD2	LEU	C	86	−6.157	62.137	7.290	1.00	41.68		C
ATOM	679	N	ARG	C	87	−7.468	58.400	5.470	1.00	41.40		N
ATOM	680	CA	ARG	C	87	−7.251	57.088	4.882	1.00	37.22		C
ATOM	681	C	ARG	C	87	−5.782	56.695	5.005	1.00	43.89		C
ATOM	682	O	ARG	C	87	−4.900	57.546	5.190	1.00	37.28		O
ATOM	683	CB	ARG	C	87	−7.661	57.052	3.409	1.00	41.43		C
ATOM	684	CG	ARG	C	87	−8.995	57.661	3.103	1.00	47.94		C
ATOM	685	CD	ARG	C	87	−9.556	57.025	1.858	1.00	52.28		C
ATOM	686	NE	ARG	C	87	−9.802	57.968	0.770	1.00	59.65		N
ATOM	687	CZ	ARG	C	87	−10.945	58.629	0.592	1.00	56.84		C
ATOM	688	NH1	ARG	C	87	−11.947	58.483	1.459	1.00	62.30		N1+
ATOM	689	NH2	ARG	C	87	−11.079	59.444	−0.449	1.00	58.47		N
ATOM	690	N	VAL	C	88	−5.536	55.384	4.900	1.00	37.13		N
ATOM	691	CA	VAL	C	88	−4.184	54.851	5.067	1.00	40.40		C
ATOM	692	C	VAL	C	88	−3.218	55.550	4.113	1.00	41.32		C
ATOM	693	O	VAL	C	88	−2.142	56.021	4.510	1.00	39.20		O
ATOM	694	CB	VAL	C	88	−4.191	53.320	4.863	1.00	38.65		C
ATOM	695	CG1	VAL	C	88	−2.774	52.764	4.702	1.00	37.78		C
ATOM	696	CG2	VAL	C	88	−4.883	52.634	6.045	1.00	35.60		C
ATOM	697	N	GLU	C	89	−3.621	55.684	2.856	1.00	36.74		N
ATOM	698	CA	GLU	C	89	−2.794	56.334	1.849	1.00	37.93		C
ATOM	699	C	GLU	C	89	−2.629	57.845	2.082	1.00	39.72		C
ATOM	700	O	GLU	C	89	−1.953	58.480	1.274	1.00	41.02		O
ATOM	701	CB	GLU	C	89	−3.324	56.041	0.434	1.00	30.08		C
ATOM	702	CG	GLU	C	89	−4.747	56.489	0.150	1.00	44.00		C
ATOM	703	CD	GLU	C	89	−5.802	55.528	0.720	1.00	65.19		C
ATOM	704	OE1	GLU	C	89	−7.001	55.726	0.398	1.00	72.89		O
ATOM	705	OE2	GLU	C	89	−5.434	54.580	1.479	1.00	57.08		O1−
ATOM	706	N	ASP	C	90	−3.261	58.456	3.092	1.00	34.66		N
ATOM	707	CA	ASP	C	90	−2.892	59.824	3.461	1.00	35.63		C
ATOM	708	C	ASP	C	90	−1.648	59.885	4.344	1.00	36.64		C
ATOM	709	O	ASP	C	90	−1.213	60.994	4.704	1.00	34.03		O
ATOM	710	CB	ASP	C	90	−4.032	60.545	4.200	1.00	37.08		C
ATOM	711	CG	ASP	C	90	−5.265	60.761	3.338	1.00	41.53		C
ATOM	712	OD1	ASP	C	90	−5.126	61.135	2.135	1.00	39.64		O
ATOM	713	OD2	ASP	C	90	−6.380	60.541	3.882	1.00	36.67		O1−
ATOM	714	N	THR	C	91	−1.085	58.733	4.713	1.00	35.16		N
ATOM	715	CA	THR	C	91	0.114	58.684	5.552	1.00	38.29		C
ATOM	716	C	THR	C	91	1.260	59.354	4.826	1.00	31.75		C
ATOM	717	O	THR	C	91	1.572	58.989	3.690	1.00	36.79		O
ATOM	718	CB	THR	C	91	0.484	57.225	5.857	1.00	49.62		C
ATOM	719	OG1	THR	C	91	−0.561	56.594	6.611	1.00	40.91		O
ATOM	720	CG2	THR	C	91	1.824	57.138	6.602	1.00	35.10		C
ATOM	721	N	ALA	C	92	1.876	60.340	5.462	1.00	34.05		N
ATOM	722	CA	ALA	C	92	2.886	61.136	4.778	1.00	32.82		C
ATOM	723	C	ALA	C	92	3.495	62.111	5.760	1.00	30.84		C
ATOM	724	O	ALA	C	92	2.938	62.368	6.827	1.00	30.26		O
ATOM	725	CB	ALA	C	92	2.304	61.923	3.596	1.00	36.15		C
ATOM	726	N	VAL	C	93	4.648	62.657	5.382	1.00	35.57		N
ATOM	727	CA	VAL	C	93	5.111	63.910	5.967	1.00	35.12		C
ATOM	728	C	VAL	C	93	4.408	65.064	5.265	1.00	34.14		C
ATOM	729	O	VAL	C	93	4.322	65.099	4.032	1.00	35.63		O
ATOM	730	CB	VAL	C	93	6.633	64.038	5.857	1.00	34.90		C
ATOM	731	CG1	VAL	C	93	7.077	65.442	6.323	1.00	28.59		C
ATOM	732	CG2	VAL	C	93	7.297	62.925	6.680	1.00	31.28		C
ATOM	733	N	TYR	C	94	3.897	66.006	6.045	1.00	33.45		N
ATOM	734	CA	TYR	C	94	3.184	67.159	5.518	1.00	37.19		C
ATOM	735	C	TYR	C	94	4.043	68.395	5.707	1.00	36.22		C
ATOM	736	O	TYR	C	94	4.511	68.654	6.820	1.00	37.12		O
ATOM	737	CB	TYR	C	94	1.826	67.335	6.216	1.00	29.33		C
ATOM	738	CG	TYR	C	94	0.818	66.349	5.708	1.00	38.48		C
ATOM	739	CD1	TYR	C	94	0.931	64.986	6.003	1.00	33.38		C
ATOM	740	CD2	TYR	C	94	−0.223	66.760	4.887	1.00	34.11		C
ATOM	741	CE1	TYR	C	94	0.012	64.069	5.508	1.00	35.06		C
ATOM	742	CE2	TYR	C	94	−1.143	65.848	4.386	1.00	32.26		C
ATOM	743	CZ	TYR	C	94	−1.033	64.510	4.706	1.00	31.31		C
ATOM	744	OH	TYR	C	94	−1.955	63.614	4.184	1.00	29.76		O
ATOM	745	N	TYR	C	95	4.240	69.154	4.625	1.00	33.06		N
ATOM	746	CA	TYR	C	95	4.988	70.408	4.660	1.00	37.25		C
ATOM	747	C	TYR	C	95	4.091	71.583	4.292	1.00	38.95		C
ATOM	748	O	TYR	C	95	3.283	71.491	3.356	1.00	34.73		O
ATOM	749	CB	TYR	C	95	6.160	70.409	3.680	1.00	33.44		C
ATOM	750	CG	TYR	C	95	7.187	69.311	3.833	1.00	36.03		C
ATOM	751	CD1	TYR	C	95	8.260	69.444	4.718	1.00	30.51		C
ATOM	752	CD2	TYR	C	95	7.124	68.165	3.036	1.00	34.65		C
ATOM	753	CE1	TYR	C	95	9.231	68.431	4.825	1.00	35.04		C
ATOM	754	CE2	TYR	C	95	8.078	67.163	3.132	1.00	35.40		C
ATOM	755	CZ	TYR	C	95	9.124	67.295	4.023	1.00	36.07		C
ATOM	756	OH	TYR	C	95	10.054	66.281	4.097	1.00	43.55		O
ATOM	757	N	CYS	C	96	4.277	72.713	4.969	1.00	32.29		N
ATOM	758	CA	CYS	C	96	3.722	73.935	4.419	1.00	35.55		C
ATOM	759	C	CYS	C	96	4.819	74.668	3.674	1.00	34.71		C
ATOM	760	O	CYS	C	96	6.007	74.463	3.919	1.00	37.92		O
ATOM	761	CB	CYS	C	96	3.090	74.846	5.484	1.00	37.18		C
ATOM	762	SG	CYS	C	96	4.149	75.311	6.821	1.00	55.09		S
ATOM	763	N	ALA	C	97	4.391	75.493	2.720	1.00	37.06		N
ATOM	764	CA	ALA	C	97	5.252	76.388	1.965	1.00	33.86		C
ATOM	765	C	ALA	C	97	4.453	77.646	1.659	1.00	36.16		C
ATOM	766	O	ALA	C	97	3.224	77.620	1.638	1.00	37.96		O
ATOM	767	CB	ALA	C	97	5.744	75.736	0.667	1.00	31.03		C
ATOM	768	N	ASN	C	98	5.141	78.756	1.411	1.00	36.24		N
ATOM	769	CA	ASN	C	98	4.402	79.933	0.984	1.00	36.16		C
ATOM	770	C	ASN	C	98	4.643	80.154	−0.505	1.00	33.85		C
ATOM	771	O	ASN	C	98	5.379	79.405	−1.150	1.00	34.25		O
ATOM	772	CB	ASN	C	98	4.750	81.159	1.836	1.00	33.87		C
ATOM	773	CG	ASN	C	98	6.152	81.689	1.602	1.00	36.19		C
ATOM	774	OD1	ASN	C	98	6.912	81.172	0.781	1.00	35.81		O
ATOM	775	ND2	ASN	C	98	6.490	82.759	2.312	1.00	32.46		N
ATOM	776	N	TRP	C	99	4.001	81.179	−1.060	1.00	29.34		N
ATOM	777	CA	TRP	C	99	4.253	81.534	−2.451	1.00	32.42		C
ATOM	778	C	TRP	C	99	4.141	83.043	−2.609	1.00	34.35		C
ATOM	779	O	TRP	C	99	3.294	83.677	−1.978	1.00	36.87		O
ATOM	780	CB	TRP	C	99	3.301	80.808	−3.409	1.00	31.13		C
ATOM	781	CG	TRP	C	99	1.832	81.172	−3.311	1.00	38.60		C
ATOM	782	CD1	TRP	C	99	0.869	80.545	−2.558	1.00	36.35		C
ATOM	783	CD2	TRP	C	99	1.160	82.217	−4.028	1.00	33.13		C
ATOM	784	NE1	TRP	C	99	−0.359	81.151	−2.754	1.00	32.28		N
ATOM	785	CE2	TRP	C	99	−0.207	82.175	−3.653	1.00	36.97		C
ATOM	786	CE3	TRP	C	99	1.580	83.187	−4.949	1.00	33.81		C
ATOM	787	CZ2	TRP	C	99	−1.155	83.078	−4.160	1.00	35.91		C
ATOM	788	CZ3	TRP	C	99	0.639	84.078	−5.459	1.00	33.25		C
ATOM	789	CH2	TRP	C	99	−0.712	84.016	−5.059	1.00	34.18		C
ATOM	790	N	TYR	C	100	5.011	83.606	−3.443	1.00	35.97		N
ATOM	791	CA	TYR	C	100	5.148	85.048	−3.651	1.00	34.82		C
ATOM	792	C	TYR	C	100	4.693	85.512	−5.022	1.00	35.71		C
ATOM	793	O	TYR	C	100	4.101	86.591	−5.143	1.00	33.01		O
ATOM	794	CB	TYR	C	100	6.615	85.472	−3.493	1.00	28.22		C
ATOM	795	CG	TYR	C	100	7.184	85.286	−2.114	1.00	36.73		C
ATOM	796	CD1	TYR	C	100	6.415	85.536	−0.971	1.00	34.55		C
ATOM	797	CD2	TYR	C	100	8.496	84.852	−1.946	1.00	35.48		C
ATOM	798	CE1	TYR	C	100	6.951	85.365	0.299	1.00	36.55		C
ATOM	799	CE2	TYR	C	100	9.032	84.666	−0.684	1.00	33.46		C
ATOM	800	CZ	TYR	C	100	8.263	84.929	0.430	1.00	36.36		C
ATOM	801	OH	TYR	C	100	8.813	84.749	1.674	1.00	36.68		O
ATOM	802	N	TYR	C	101	4.990	84.731	−6.059	1.00	32.01		N
ATOM	803	CA	TYR	C	101	4.927	85.197	−7.439	1.00	35.14		C
ATOM	804	C	TYR	C	101	3.758	84.539	−8.159	1.00	31.46		C
ATOM	805	O	TYR	C	101	2.795	85.215	−8.492	1.00	32.52		O
ATOM	806	CB	TYR	C	101	6.249	84.921	−8.157	1.00	25.12		C
ATOM	807	CG	TYR	C	101	7.430	85.482	−7.409	1.00	31.29		C
ATOM	808	CD1	TYR	C	101	7.594	86.850	−7.307	1.00	30.52		C
ATOM	809	CD2	TYR	C	101	8.385	84.653	−6.796	1.00	34.01		C
ATOM	810	CE1	TYR	C	101	8.646	87.393	−6.644	1.00	31.83		C
ATOM	811	CE2	TYR	C	101	9.470	85.205	−6.099	1.00	29.33		C
ATOM	812	CZ	TYR	C	101	9.586	86.589	−6.042	1.00	34.04		C
ATOM	813	OH	TYR	C	101	10.613	87.238	−5.396	1.00	38.85		O
ATOM	814	N	TYR	C	102	3.818	83.241	−8.407	1.00	32.18		N
ATOM	815	CA	TYR	C	102	2.692	82.528	−8.984	1.00	26.83		C
ATOM	816	C	TYR	C	102	2.185	81.474	−8.000	1.00	34.57		C
ATOM	817	O	TYR	C	102	2.959	80.888	−7.237	1.00	30.16		O
ATOM	818	CB	TYR	C	102	3.069	81.916	−10.328	1.00	26.41		C
ATOM	819	CG	TYR	C	102	4.422	81.207	−10.424	1.00	31.59		C
ATOM	820	CD1	TYR	C	102	5.586	81.894	−10.776	1.00	25.87		C
ATOM	821	CD2	TYR	C	102	4.510	79.827	−10.218	1.00	34.03		C
ATOM	822	CE1	TYR	C	102	6.807	81.225	−10.900	1.00	28.32		C
ATOM	823	CE2	TYR	C	102	5.708	79.150	−10.339	1.00	29.44		C
ATOM	824	CZ	TYR	C	102	6.856	79.842	−10.677	1.00	37.60		C
ATOM	825	OH	TYR	C	102	8.030	79.125	−10.804	1.00	31.27		O
ATOM	826	N	TYR	C	103	0.861	81.255	−8.005	1.00	34.62		N
ATOM	827	CA	TYR	C	103	0.206	80.545	−6.908	1.00	30.24		C
ATOM	828	C	TYR	C	103	0.561	79.069	−6.860	1.00	33.90		C
ATOM	829	O	TYR	C	103	0.334	78.431	−5.826	1.00	33.35		O
ATOM	830	CB	TYR	C	103	−1.330	80.708	−6.981	1.00	32.59		C
ATOM	831	CG	TYR	C	103	−1.968	80.050	−8.196	1.00	30.66		C
ATOM	832	CD1	TYR	C	103	−2.097	80.744	−9.398	1.00	32.62		C
ATOM	833	CD2	TYR	C	103	−2.439	78.739	−8.145	1.00	31.75		C
ATOM	834	CE1	TYR	C	103	−2.677	80.151	−10.526	1.00	34.17		C
ATOM	835	CE2	TYR	C	103	−3.030	78.132	−9.277	1.00	35.45		C
ATOM	836	CZ	TYR	C	103	−3.140	78.851	−10.460	1.00	38.01		C
ATOM	837	OH	TYR	C	103	−3.707	78.286	−11.585	1.00	43.93		O
ATOM	838	N	TYR	C	104	1.090	78.503	−7.941	1.00	33.41		N
ATOM	839	CA	TYR	C	104	1.431	77.088	−7.959	1.00	31.54		C
ATOM	840	C	TYR	C	104	2.921	76.846	−7.775	1.00	35.80		C
ATOM	841	O	TYR	C	104	3.383	75.706	−7.933	1.00	34.83		O
ATOM	842	CB	TYR	C	104	0.942	76.437	−9.254	1.00	31.39		C
ATOM	843	CG	TYR	C	104	1.310	77.192	−10.505	1.00	35.92		C
ATOM	844	CD1	TYR	C	104	2.537	76.979	−11.134	1.00	29.90		C
ATOM	845	CD2	TYR	C	104	0.431	78.136	−11.058	1.00	37.72		C
ATOM	846	CE1	TYR	C	104	2.887	77.682	−12.297	1.00	31.96		C
ATOM	847	CE2	TYR	C	104	0.773	78.853	−12.216	1.00	33.33		C
ATOM	848	CZ	TYR	C	104	1.997	78.611	−12.832	1.00	37.08		C
ATOM	849	OH	TYR	C	104	2.322	79.290	−13.988	1.00	38.85		O
ATOM	850	N	GLY	C	105	3.677	77.881	−7.424	1.00	30.57		N
ATOM	851	CA	GLY	C	105	5.069	77.729	−7.046	1.00	31.29		C
ATOM	852	C	GLY	C	105	5.189	77.804	−5.536	1.00	35.97		C
ATOM	853	O	GLY	C	105	4.381	78.439	−4.880	1.00	39.78		O
ATOM	854	N	MET	C	106	6.174	77.104	−4.983	1.00	35.79		N
ATOM	855	CA	MET	C	106	6.477	77.149	−3.560	1.00	29.65		C
ATOM	856	C	MET	C	106	7.811	77.844	−3.359	1.00	34.76		C
ATOM	857	O	MET	C	106	8.814	77.447	−3.964	1.00	40.34		O
ATOM	858	CB	MET	C	106	6.531	75.749	−2.967	1.00	33.58		C
ATOM	859	CG	MET	C	106	5.200	75.079	−2.997	1.00	40.63		C
ATOM	860	SD	MET	C	106	5.175	73.827	−4.259	1.00	38.99		S
ATOM	861	CE	MET	C	106	3.449	73.894	−4.753	1.00	39.97		C
ATOM	862	N	ASP	C	107	7.833	78.872	−2.510	1.00	32.14		N
ATOM	863	CA	ASP	C	107	9.038	79.679	−2.359	1.00	36.28		C
ATOM	864	C	ASP	C	107	9.814	79.363	−1.087	1.00	36.05		C
ATOM	865	O	ASP	C	107	10.987	79.000	−1.168	1.00	43.22		O
ATOM	866	CB	ASP	C	107	8.684	81.166	−2.419	1.00	35.85		C
ATOM	867	CG	ASP	C	107	8.243	81.582	−3.791	1.00	36.58		C
ATOM	868	OD1	ASP	C	107	9.126	81.733	−4.663	1.00	39.74		O1−
ATOM	869	OD2	ASP	C	107	7.024	81.741	−4.005	1.00	38.36		O
ATOM	870	N	VAL	C	108	9.185	79.486	0.079	1.00	34.27		N
ATOM	871	CA	VAL	C	108	9.795	79.131	1.354	1.00	37.63		C
ATOM	872	C	VAL	C	108	9.081	77.906	1.893	1.00	35.71		C
ATOM	873	O	VAL	C	108	7.853	77.818	1.820	1.00	36.94		O
ATOM	874	CB	VAL	C	108	9.716	80.275	2.375	1.00	39.13		C
ATOM	875	CG1	VAL	C	108	10.395	79.854	3.662	1.00	34.94		C
ATOM	876	CG2	VAL	C	108	10.334	81.534	1.809	1.00	37.63		C
ATOM	877	N	TRP	C	109	9.845	76.969	2.442	1.00	35.86		N
ATOM	878	CA	TRP	C	109	9.305	75.713	2.950	1.00	38.43		C
ATOM	879	C	TRP	C	109	9.523	75.578	4.452	1.00	36.07		C
ATOM	880	O	TRP	C	109	10.470	76.127	5.011	1.00	34.83		O
ATOM	881	CB	TRP	C	109	9.935	74.510	2.270	1.00	28.64		C
ATOM	882	CG	TRP	C	109	9.627	74.379	0.834	1.00	32.20		C
ATOM	883	CD1	TRP	C	109	10.053	75.196	−0.178	1.00	33.19		C
ATOM	884	CD2	TRP	C	109	8.857	73.338	0.215	1.00	30.88		C
ATOM	885	NE1	TRP	C	109	9.589	74.729	−1.385	1.00	32.70		N
ATOM	886	CE2	TRP	C	109	8.853	73.589	−1.171	1.00	32.73		C
ATOM	887	CE3	TRP	C	109	8.175	72.219	0.696	1.00	31.39		C
ATOM	888	CZ2	TRP	C	109	8.183	72.759	−2.079	1.00	27.14		C
ATOM	889	CZ3	TRP	C	109	7.510	71.395	−0.205	1.00	25.68		C
ATOM	890	CH2	TRP	C	109	7.532	71.661	−1.575	1.00	25.11		C
ATOM	891	N	GLY	C	110	8.611	74.852	5.095	1.00	38.56		N
ATOM	892	CA	GLY	C	110	8.732	74.483	6.489	1.00	37.65		C
ATOM	893	C	GLY	C	110	9.578	73.243	6.689	1.00	38.90		C
ATOM	894	O	GLY	C	110	10.348	72.825	5.821	1.00	44.35		O
ATOM	895	N	GLN	C	111	9.417	72.638	7.864	1.00	37.08		N
ATOM	896	CA	GLN	C	111	10.257	71.526	8.265	1.00	37.72		C
ATOM	897	C	GLN	C	111	9.554	70.171	8.274	1.00	39.10		C
ATOM	898	O	GLN	C	111	10.241	69.143	8.268	1.00	46.62		O
ATOM	899	CB	GLN	C	111	10.854	71.823	9.646	1.00	41.49		C
ATOM	900	CG	GLN	C	111	9.971	71.407	10.795	1.00	57.57		C
ATOM	901	CD	GLN	C	111	10.317	72.142	12.083	1.00	71.42		C
ATOM	902	OE1	GLN	C	111	11.162	73.046	12.079	1.00	67.32		O
ATOM	903	NE2	GLN	C	111	9.662	71.761	13.194	1.00	62.29		N
ATOM	904	N	GLY	C	112	8.229	70.137	8.247	1.00	38.85		N
ATOM	905	CA	GLY	C	112	7.483	68.892	8.185	1.00	37.13		C
ATOM	906	C	GLY	C	112	6.892	68.477	9.528	1.00	40.61		C
ATOM	907	O	GLY	C	112	7.389	68.837	10.601	1.00	43.71		O
ATOM	908	N	THR	C	113	5.771	67.754	9.462	1.00	38.16		N
ATOM	909	CA	THR	C	113	5.125	67.066	10.574	1.00	37.93		C
ATOM	910	C	THR	C	113	4.592	65.777	9.967	1.00	40.18		C
ATOM	911	O	THR	C	113	4.106	65.791	8.834	1.00	43.97		O
ATOM	912	CB	THR	C	113	4.008	67.924	11.231	1.00	40.04		C
ATOM	913	OG1	THR	C	113	3.470	67.248	12.370	1.00	48.01		O
ATOM	914	CG2	THR	C	113	2.863	68.248	10.265	1.00	39.86		C
ATOM	915	N	ATHR	C	114	4.716	64.665	10.689	0.50	39.81		N
ATOM	916	CA	ATHR	C	114	4.418	63.359	10.110	0.50	39.05		C
ATOM	917	C	ATHR	C	114	3.038	62.873	10.545	0.50	39.83		C
ATOM	918	O	ATHR	C	114	2.650	63.015	11.709	0.50	39.84		O
ATOM	919	CB	ATHR	C	114	5.484	62.320	10.487	0.50	39.38		C
ATOM	920	OG1	ATHR	C	114	5.310	61.937	11.853	0.50	49.44		O
ATOM	921	CG2	ATHR	C	114	6.901	62.878	10.295	0.50	34.14		C
ATOM	922	N	BTHR	C	114	4.722	64.656	10.669	0.50	39.81		N
ATOM	923	CA	BTHR	C	114	4.413	63.376	10.040	0.50	39.04		C
ATOM	924	C	BTHR	C	114	3.083	62.819	10.539	0.50	39.82		C
ATOM	925	O	BTHR	C	114	2.766	62.880	11.731	0.50	39.90		O
ATOM	926	CB	BTHR	C	114	5.554	62.360	10.232	0.50	39.16		C
ATOM	927	OG1	BTHR	C	114	5.037	61.021	10.248	0.50	33.47		O
ATOM	928	CG2	BTHR	C	114	6.343	62.647	11.490	0.50	42.84		C
ATOM	929	N	VAL	C	115	2.298	62.308	9.592	1.00	38.42		N
ATOM	930	CA	VAL	C	115	0.962	61.778	9.817	1.00	36.25		C
ATOM	931	C	VAL	C	115	0.968	60.298	9.446	1.00	37.55		C
ATOM	932	O	VAL	C	115	1.310	59.940	8.313	1.00	39.55		O
ATOM	933	CB	VAL	C	115	−0.092	62.536	8.991	1.00	37.32		C
ATOM	934	CG1	VAL	C	115	−1.443	61.798	9.049	1.00	33.92		C
ATOM	935	CG2	VAL	C	115	−0.223	63.961	9.492	1.00	31.70		C
ATOM	936	N	THR	C	116	0.580	59.443	10.388	1.00	35.49		N
ATOM	937	CA	THR	C	116	0.471	58.014	10.145	1.00	38.36		C
ATOM	938	C	THR	C	116	−0.987	57.603	10.309	1.00	43.76		C
ATOM	939	O	THR	C	116	−1.596	57.873	11.350	1.00	43.30		O
ATOM	940	CB	THR	C	116	1.379	57.223	11.096	1.00	45.91		C
ATOM	941	OG1	THR	C	116	2.734	57.660	10.937	1.00	47.40		O
ATOM	942	CG2	THR	C	116	1.342	55.751	10.742	1.00	42.59		C
ATOM	943	N	VAL	C	117	−1.553	56.977	9.283	1.00	36.12		N
ATOM	944	CA	VAL	C	117	−2.926	56.501	9.346	1.00	41.60		C
ATOM	945	C	VAL	C	117	−2.891	54.978	9.276	1.00	45.74		C
ATOM	946	O	VAL	C	117	−2.634	54.394	8.211	1.00	44.01		O
ATOM	947	CB	VAL	C	117	−3.813	57.107	8.244	1.00	42.69		C
ATOM	948	CG1	VAL	C	117	−5.257	56.664	8.437	1.00	34.13		C
ATOM	949	CG2	VAL	C	117	−3.720	58.666	8.235	1.00	38.65		C
ATOM	950	N	SER	C	118	−3.181	54.330	10.407	1.00	42.18		N
ATOM	951	CA	SER	C	118	−3.101	52.882	10.500	1.00	45.65		C
ATOM	952	C	SER	C	118	−4.244	52.329	11.345	1.00	46.76		C
ATOM	953	O	SER	C	118	−4.596	52.891	12.389	1.00	43.45		O
ATOM	954	CB	SER	C	118	−1.764	52.442	11.101	1.00	45.42		C
ATOM	955	OG	SER	C	118	−1.694	51.028	11.142	1.00	53.46		O
ATOM	956	N	SER	C	119	−4.800	51.204	10.901	1.00	39.96		N
ATOM	957	CA	SER	C	119	−5.765	50.456	11.697	1.00	55.76		C
ATOM	958	C	SER	C	119	−5.145	49.241	12.384	1.00	58.97		C
ATOM	959	O	SER	C	119	−5.879	48.417	12.940	1.00	56.42		O
ATOM	960	CB	SER	C	119	−6.956	50.024	10.833	1.00	47.59		C
ATOM	961	OG	SER	C	119	−6.537	49.473	9.592	1.00	60.90		O
ATOM	962	N	ALA	C	120	−3.821	49.092	12.325	1.00	53.37		N
ATOM	963	CA	ALA	C	120	−3.157	47.942	12.923	1.00	49.27		C
ATOM	964	C	ALA	C	120	−3.115	48.063	14.439	1.00	53.61		C
ATOM	965	O	ALA	C	120	−3.088	49.160	15.007	1.00	51.80		O
ATOM	966	CB	ALA	C	120	−1.736	47.799	12.376	1.00	54.97		C
ATOM	967	N	SER	C	121	−3.101	46.918	15.104	1.00	50.81	GZ00	N
ATOM	968	CA	SER	C	121	−2.922	46.921	16.546	1.00	62.62	GZ00	C
ATOM	969	C	SER	C	121	−1.817	45.945	16.925	1.00	55.18	GZ00	C
ATOM	970	O	SER	C	121	−1.492	45.015	16.175	1.00	50.22	GZ00	O
ATOM	971	CB	SER	C	121	−4.226	46.571	17.271	1.00	60.87	GZ00	C
ATOM	972	OG	SER	C	121	−4.902	45.539	16.576	1.00	67.02	GZ00	O
ATOM	973	N	THR	C	122	−1.276	46.170	18.123	1.00	43.63	GZ00	N
ATOM	974	CA	THR	C	122	−0.125	45.444	18.640	1.00	49.19	GZ00	C
ATOM	975	C	THR	C	122	−0.197	43.955	18.342	1.00	48.67	GZ00	C
ATOM	976	O	THR	C	122	−1.207	43.300	18.591	1.00	54.63	GZ00	O
ATOM	977	CB	THR	C	122	−0.014	45.661	20.147	1.00	51.65	GZ00	C
ATOM	978	OG1	THR	C	122	0.017	47.074	20.426	1.00	49.30	GZ00	O
ATOM	979	CG2	THR	C	122	1.260	44.988	20.690	1.00	49.88	GZ00	C
ATOM	980	N	LYS	C	123	0.890	43.430	17.795	1.00	50.80	GZ00	N
ATOM	981	CA	LYS	C	123	0.976	42.015	17.485	1.00	49.10	GZ00	C
ATOM	982	C	LYS	C	123	2.446	41.622	17.506	1.00	56.41	GZ00	C
ATOM	983	O	LYS	C	123	3.290	42.358	16.985	1.00	49.74	GZ00	O
ATOM	984	CB	LYS	C	123	0.338	41.693	16.133	1.00	44.99	GZ00	C
ATOM	985	CG	LYS	C	123	0.499	40.238	15.807	1.00	44.28	GZ00	C
ATOM	986	CD	LYS	C	123	−0.078	39.820	14.484	1.00	49.15	GZ00	C
ATOM	987	CE	LYS	C	123	0.361	38.368	14.217	1.00	62.00	GZ00	C
ATOM	988	NZ	LYS	C	123	−0.182	37.795	12.951	1.00	72.41	GZ00	N1+
ATOM	989	N	GLY	C	124	2.752	40.507	18.178	1.00	53.97	GZ00	N
ATOM	990	CA	GLY	C	124	4.094	39.983	18.217	1.00	39.15	GZ00	C
ATOM	991	C	GLY	C	124	4.382	39.194	16.962	1.00	43.80	GZ00	C
ATOM	992	O	GLY	C	124	3.474	38.686	16.297	1.00	46.60	GZ00	O
ATOM	993	N	PRO	C	125	5.658	39.060	16.625	1.00	47.07	GZ00	N
ATOM	994	CA	PRO	C	125	6.043	38.419	15.362	1.00	48.03	GZ00	C
ATOM	995	C	PRO	C	125	6.129	36.902	15.443	1.00	43.83	GZ00	C
ATOM	996	O	PRO	C	125	6.341	36.326	16.503	1.00	45.86	GZ00	O
ATOM	997	CB	PRO	C	125	7.440	38.999	15.095	1.00	45.07	GZ00	C
ATOM	998	CG	PRO	C	125	7.989	39.254	16.464	1.00	48.96	GZ00	C
ATOM	999	CD	PRO	C	125	6.800	39.689	17.314	1.00	46.04	GZ00	C
ATOM	1000	N	SER	C	126	5.963	36.270	14.280	1.00	42.83	GZ00	N
ATOM	1001	CA	SER	C	126	6.393	34.900	14.053	1.00	46.91	GZ00	C
ATOM	1002	C	SER	C	126	7.817	34.900	13.498	1.00	49.79	GZ00	C
ATOM	1003	O	SER	C	126	8.157	35.713	12.635	1.00	45.82	GZ00	O
ATOM	1004	CB	SER	C	126	5.461	34.192	13.071	1.00	50.64	GZ00	C
ATOM	1005	OG	SER	C	126	4.145	34.158	13.572	1.00	58.04	GZ00	O
ATOM	1006	N	VAL	C	127	8.645	33.980	13.986	1.00	49.68	GZ00	N
ATOM	1007	CA	VAL	C	127	10.059	33.915	13.624	1.00	45.00	GZ00	C
ATOM	1008	C	VAL	C	127	10.335	32.584	12.950	1.00	42.10	GZ00	C
ATOM	1009	O	VAL	C	127	10.021	31.528	13.504	1.00	57.42	GZ00	O
ATOM	1010	CB	VAL	C	127	10.958	34.110	14.855	1.00	44.31	GZ00	C
ATOM	1011	CG1	VAL	C	127	12.431	34.119	14.456	1.00	47.62	GZ00	C
ATOM	1012	CG2	VAL	C	127	10.577	35.406	15.554	1.00	41.45	GZ00	C
ATOM	1013	N	PHE	C	128	10.912	32.635	11.758	1.00	43.32	GZ00	N
ATOM	1014	CA	PHE	C	128	11.244	31.451	10.983	1.00	44.87	GZ00	C
ATOM	1015	C	PHE	C	128	12.729	31.447	10.629	1.00	50.79	GZ00	C
ATOM	1016	O	PHE	C	128	13.327	32.511	10.435	1.00	47.46	GZ00	O
ATOM	1017	CB	PHE	C	128	10.425	31.399	9.694	1.00	48.10	GZ00	C
ATOM	1018	CG	PHE	C	128	8.942	31.384	9.922	1.00	58.19	GZ00	C
ATOM	1019	CD1	PHE	C	128	8.272	30.200	10.176	1.00	58.46	GZ00	C
ATOM	1020	CD2	PHE	C	128	8.220	32.566	9.912	1.00	56.25	GZ00	C
ATOM	1021	CE1	PHE	C	128	6.912	30.198	10.387	1.00	58.84	GZ00	C
ATOM	1022	CE2	PHE	C	128	6.855	32.568	10.128	1.00	55.91	GZ00	C
ATOM	1023	CZ	PHE	C	128	6.205	31.387	10.358	1.00	55.09	GZ00	C
ATOM	1024	N	PRO	C	129	13.360	30.275	10.560	1.00	52.29	GZ00	N
ATOM	1025	CA	PRO	C	129	14.779	30.230	10.200	1.00	40.71	GZ00	C
ATOM	1026	C	PRO	C	129	14.975	30.363	8.705	1.00	44.60	GZ00	C
ATOM	1027	O	PRO	C	129	14.205	29.819	7.907	1.00	48.43	GZ00	O
ATOM	1028	CB	PRO	C	129	15.218	28.840	10.681	1.00	53.19	GZ00	C
ATOM	1029	CG	PRO	C	129	13.998	28.000	10.486	1.00	46.32	GZ00	C
ATOM	1030	CD	PRO	C	129	12.829	28.925	10.840	1.00	50.96	GZ00	C
ATOM	1031	N	LEU	C	130	16.017	31.101	8.330	1.00	39.68	GZ00	N
ATOM	1032	CA	LEU	C	130	16.463	31.190	6.947	1.00	38.79	GZ00	C
ATOM	1033	C	LEU	C	130	17.725	30.330	6.838	1.00	45.86	GZ00	C
ATOM	1034	O	LEU	C	130	18.834	30.778	7.150	1.00	44.51	GZ00	O
ATOM	1035	CB	LEU	C	130	16.699	32.647	6.568	1.00	41.81	GZ00	C
ATOM	1036	CG	LEU	C	130	15.436	33.491	6.795	1.00	45.70	GZ00	C
ATOM	1037	CD1	LEU	C	130	15.639	34.968	6.444	1.00	40.24	GZ00	C
ATOM	1038	CD2	LEU	C	130	14.275	32.910	6.003	1.00	44.72	GZ00	C
ATOM	1039	N	ALA	C	131	17.552	29.096	6.402	1.00	46.13	GZ00	N
ATOM	1040	CA	ALA	C	131	18.618	28.113	6.528	1.00	43.66	GZ00	C
ATOM	1041	C	ALA	C	131	19.672	28.301	5.441	1.00	44.63	GZ00	C
ATOM	1042	O	ALA	C	131	19.339	28.524	4.278	1.00	46.42	GZ00	O
ATOM	1043	CB	ALA	C	131	18.060	26.703	6.457	1.00	36.60	GZ00	C
ATOM	1044	N	PRO	C	132	20.943	28.159	5.792	1.00	50.91	GZ00	N
ATOM	1045	CA	PRO	C	132	22.009	28.205	4.784	1.00	52.92	GZ00	C
ATOM	1046	C	PRO	C	132	22.027	26.951	3.921	1.00	63.10	GZ00	C
ATOM	1047	O	PRO	C	132	21.557	25.876	4.315	1.00	65.83	GZ00	O
ATOM	1048	CB	PRO	C	132	23.279	28.301	5.631	1.00	51.34	GZ00	C
ATOM	1049	CG	PRO	C	132	22.910	27.548	6.901	1.00	47.48	GZ00	C
ATOM	1050	CD	PRO	C	132	21.454	27.876	7.145	1.00	49.36	GZ00	C
ATOM	1051	N	SER	C	133	22.606	27.103	2.724	1.00	65.77	GZ00	N
ATOM	1052	CA	SER	C	133	22.642	26.041	1.718	1.00	75.34	GZ00	C
ATOM	1053	C	SER	C	133	23.713	26.317	0.668	1.00	79.20	GZ00	C
ATOM	1054	O	SER	C	133	24.893	26.462	0.990	1.00	81.66	GZ00	O
ATOM	1055	CB	SER	C	133	21.272	25.900	1.043	1.00	74.63	GZ00	C
ATOM	1056	OG	SER	C	133	20.727	27.170	0.711	1.00	72.62	GZ00	O
ATOM	1057	N	SER	C	134	23.317	26.372	−0.599	1.00	91.08	GZ00	N
ATOM	1058	CA	SER	C	134	24.136	27.032	−1.612	1.00	84.25	GZ00	C
ATOM	1059	C	SER	C	134	23.720	28.503	−1.692	1.00	85.59	GZ00	C
ATOM	1060	O	SER	C	134	23.292	29.031	−2.718	1.00	89.34	GZ00	O
ATOM	1061	CB	SER	C	134	24.022	26.312	−2.950	1.00	90.76	GZ00	C
ATOM	1062	OG	SER	C	134	24.604	25.016	−2.867	1.00	71.01	GZ00	O
ATOM	1063	N	SER	C	136	23.766	29.125	−0.514	1.00	87.58	GZ00	N
ATOM	1064	CA	SER	C	136	23.877	30.568	−0.336	1.00	76.32	GZ00	C
ATOM	1065	C	SER	C	136	25.274	30.904	0.199	1.00	70.77	GZ00	C
ATOM	1066	O	SER	C	136	25.441	31.713	1.121	1.00	56.45	GZ00	O
ATOM	1067	CB	SER	C	136	22.777	31.098	0.588	1.00	64.27	GZ00	C
ATOM	1068	OG	SER	C	136	22.863	30.567	1.905	1.00	55.15	GZ00	O
ATOM	1069	N	THR	C	137	26.294	30.248	−0.363	1.00	68.34	GZ00	N
ATOM	1070	CA	THR	C	137	27.686	30.490	−0.008	1.00	69.91	GZ00	C
ATOM	1071	C	THR	C	137	28.416	31.190	−1.157	1.00	67.19	GZ00	C
ATOM	1072	O	THR	C	137	28.180	30.891	−2.332	1.00	69.81	GZ00	O
ATOM	1073	CB	THR	C	137	28.407	29.183	0.387	1.00	64.52	GZ00	C
ATOM	1074	OG1	THR	C	137	29.096	28.626	−0.739	1.00	77.04	GZ00	O
ATOM	1075	CG2	THR	C	137	27.427	28.167	0.946	1.00	58.14	GZ00	C
ATOM	1076	N	SER	C	138	29.289	32.144	−0.810	1.00	68.23	GZ00	N
ATOM	1077	CA	SER	C	138	30.030	32.950	−1.784	1.00	66.23	GZ00	C
ATOM	1078	C	SER	C	138	31.526	32.891	−1.454	1.00	65.41	GZ00	C
ATOM	1079	O	SER	C	138	32.054	33.661	−0.629	1.00	62.93	GZ00	O
ATOM	1080	CB	SER	C	138	29.508	34.383	−1.828	1.00	70.26	GZ00	C
ATOM	1081	OG	SER	C	138	29.183	34.732	−3.162	1.00	77.29	GZ00	O
ATOM	1082	N	GLY	C	139	32.210	31.988	−2.153	1.00	65.74	GZ00	N
ATOM	1083	CA	GLY	C	139	33.577	31.673	−1.822	1.00	55.52	GZ00	C
ATOM	1084	C	GLY	C	139	33.581	30.952	−0.495	1.00	52.92	GZ00	C
ATOM	1085	O	GLY	C	139	32.963	29.889	−0.339	1.00	56.98	GZ00	O
ATOM	1086	N	GLY	C	140	34.241	31.550	0.483	1.00	39.11	GZ00	N
ATOM	1087	CA	GLY	C	140	34.394	30.917	1.767	1.00	37.84	GZ00	C
ATOM	1088	C	GLY	C	140	33.435	31.476	2.782	1.00	35.31	GZ00	C
ATOM	1089	O	GLY	C	140	33.686	31.410	3.987	1.00	35.90	GZ00	O
ATOM	1090	N	THR	C	141	32.312	31.990	2.314	1.00	30.60	GZ00	N
ATOM	1091	CA	THR	C	141	31.371	32.678	3.180	1.00	35.07	GZ00	C
ATOM	1092	C	THR	C	141	29.975	32.121	2.959	1.00	45.03	GZ00	C
ATOM	1093	O	THR	C	141	29.638	31.698	1.858	1.00	45.95	GZ00	O
ATOM	1094	CB	THR	C	141	31.469	34.196	2.898	1.00	34.50	GZ00	C
ATOM	1095	OG1	THR	C	141	31.995	34.851	4.055	1.00	45.09	GZ00	O
ATOM	1096	CG2	THR	C	141	30.182	34.807	2.446	1.00	40.84	GZ00	C
ATOM	1097	N	ALA	C	142	29.186	32.058	4.026	1.00	40.91	GZ00	N
ATOM	1098	CA	ALA	C	142	27.833	31.528	3.943	1.00	37.80	GZ00	C
ATOM	1099	C	ALA	C	142	26.893	32.457	4.683	1.00	34.33	GZ00	C
ATOM	1100	O	ALA	C	142	27.251	33.006	5.730	1.00	37.65	GZ00	O
ATOM	1101	CB	ALA	C	142	27.729	30.125	4.539	1.00	37.82	GZ00	C
ATOM	1102	N	ALA	C	143	25.685	32.608	4.148	1.00	31.94	GZ00	N
ATOM	1103	CA	ALA	C	143	24.649	33.451	4.731	1.00	31.30	GZ00	C
ATOM	1104	C	ALA	C	143	23.527	32.602	5.324	1.00	38.60	GZ00	C
ATOM	1105	O	ALA	C	143	23.079	31.624	4.715	1.00	36.49	GZ00	O
ATOM	1106	CB	ALA	C	143	24.062	34.401	3.689	1.00	33.71	GZ00	C
ATOM	1107	N	LEU	C	144	23.099	32.976	6.529	1.00	37.05	GZ00	N
ATOM	1108	CA	LEU	C	144	21.975	32.361	7.208	1.00	40.29	GZ00	C
ATOM	1109	C	LEU	C	144	21.227	33.458	7.957	1.00	40.87	GZ00	C
ATOM	1110	O	LEU	C	144	21.800	34.504	8.281	1.00	41.49	GZ00	O
ATOM	1111	CB	LEU	C	144	22.463	31.247	8.144	1.00	42.35	GZ00	C
ATOM	1112	CG	LEU	C	144	23.403	31.747	9.239	1.00	47.05	GZ00	C
ATOM	1113	CD1	LEU	C	144	22.647	31.926	10.545	1.00	49.65	GZ00	C
ATOM	1114	CD2	LEU	C	144	24.583	30.834	9.410	1.00	40.72	GZ00	C
ATOM	1115	N	GLY	C	145	19.949	33.219	8.252	1.00	37.19	GZ00	N
ATOM	1116	CA	GLY	C	145	19.181	34.289	8.851	1.00	39.70	GZ00	C
ATOM	1117	C	GLY	C	145	17.884	33.886	9.522	1.00	40.16	GZ00	C
ATOM	1118	O	GLY	C	145	17.574	32.702	9.685	1.00	44.79	GZ00	O
ATOM	1119	N	CYS	C	146	17.133	34.916	9.910	1.00	38.48	GZ00	N
ATOM	1120	CA	CYS	C	146	15.879	34.810	10.641	1.00	40.61	GZ00	C
ATOM	1121	C	CYS	C	146	14.846	35.719	9.998	1.00	48.21	GZ00	C
ATOM	1122	O	CYS	C	146	15.099	36.916	9.820	1.00	41.15	GZ00	O
ATOM	1123	CB	CYS	C	146	16.058	35.212	12.114	1.00	36.30	GZ00	C
ATOM	1124	SG	CYS	C	146	16.447	33.783	13.156	1.00	70.07	GZ00	S
ATOM	1125	N	LEU	C	147	13.679	35.163	9.688	1.00	47.77	GZ00	N
ATOM	1126	CA	LEU	C	147	12.549	35.928	9.168	1.00	37.79	GZ00	C
ATOM	1127	C	LEU	C	147	11.641	36.320	10.333	1.00	45.95	GZ00	C
ATOM	1128	O	LEU	C	147	11.217	35.458	11.112	1.00	45.78	GZ00	O
ATOM	1129	CB	LEU	C	147	11.786	35.101	8.140	1.00	39.44	GZ00	C
ATOM	1130	CG	LEU	C	147	10.457	35.637	7.600	1.00	42.29	GZ00	C
ATOM	1131	CD1	LEU	C	147	10.605	37.010	6.924	1.00	35.22	GZ00	C
ATOM	1132	CD2	LEU	C	147	9.902	34.623	6.626	1.00	41.37	GZ00	C
ATOM	1133	N	VAL	C	148	11.392	37.614	10.493	1.00	36.60	GZ00	N
ATOM	1134	CA	VAL	C	148	10.604	38.136	11.607	1.00	39.69	GZ00	C
ATOM	1135	C	VAL	C	148	9.309	38.707	11.027	1.00	47.33	GZ00	C
ATOM	1136	O	VAL	C	148	9.266	39.872	10.617	1.00	45.03	GZ00	O
ATOM	1137	CB	VAL	C	148	11.375	39.192	12.409	1.00	42.14	GZ00	C
ATOM	1138	CG1	VAL	C	148	10.549	39.661	13.557	1.00	34.51	GZ00	C
ATOM	1139	CG2	VAL	C	148	12.701	38.631	12.933	1.00	38.14	GZ00	C
ATOM	1140	N	LYS	C	149	8.226	37.923	11.045	1.00	47.26	GZ00	N
ATOM	1141	CA	LYS	C	149	7.039	38.205	10.244	1.00	49.61	GZ00	C
ATOM	1142	C	LYS	C	149	5.887	38.797	11.059	1.00	48.25	GZ00	C
ATOM	1143	O	LYS	C	149	5.698	38.455	12.228	1.00	50.60	GZ00	O
ATOM	1144	CB	LYS	C	149	6.563	36.933	9.547	1.00	49.65	GZ00	C
ATOM	1145	CG	LYS	C	149	6.317	37.131	8.074	1.00	60.63	GZ00	C
ATOM	1146	CD	LYS	C	149	5.120	36.330	7.579	1.00	59.80	GZ00	C
ATOM	1147	CE	LYS	C	149	5.405	34.849	7.597	1.00	63.78	GZ00	C
ATOM	1148	NZ	LYS	C	149	4.321	34.077	6.887	1.00	62.06	GZ00	N1+
ATOM	1149	N	ASP	C	150	5.154	39.729	10.430	1.00	52.54	GZ00	N
ATOM	1150	CA	ASP	C	150	3.795	40.160	10.809	1.00	43.96	GZ00	C
ATOM	1151	C	ASP	C	150	3.707	40.710	12.236	1.00	45.35	GZ00	C
ATOM	1152	O	ASP	C	150	2.955	40.200	13.068	1.00	47.95	GZ00	O
ATOM	1153	CB	ASP	C	150	2.782	39.021	10.633	1.00	43.67	GZ00	C
ATOM	1154	CG	ASP	C	150	2.587	38.624	9.190	1.00	49.50	GZ00	C
ATOM	1155	OD1	ASP	C	150	2.874	39.436	8.284	1.00	47.60	GZ00	O
ATOM	1156	OD2	ASP	C	150	2.133	37.486	8.957	1.00	63.54	GZ00	O1−
ATOM	1157	N	TYR	C	151	4.437	41.792	12.498	1.00	38.78	GZ00	N
ATOM	1158	CA	TYR	C	151	4.395	42.435	13.802	1.00	42.10	GZ00	C
ATOM	1159	C	TYR	C	151	4.012	43.911	13.689	1.00	41.99	GZ00	C
ATOM	1160	O	TYR	C	151	4.115	44.534	12.628	1.00	46.82	GZ00	O
ATOM	1161	CB	TYR	C	151	5.751	42.308	14.529	1.00	46.66	GZ00	C
ATOM	1162	CG	TYR	C	151	6.892	43.080	13.890	1.00	45.23	GZ00	C
ATOM	1163	CD1	TYR	C	151	7.665	42.517	12.871	1.00	43.89	GZ00	C
ATOM	1164	CD2	TYR	C	151	7.206	44.366	14.317	1.00	45.36	GZ00	C
ATOM	1165	CE1	TYR	C	151	8.726	43.223	12.280	1.00	43.44	GZ00	C
ATOM	1166	CE2	TYR	C	151	8.259	45.082	13.739	1.00	52.49	GZ00	C
ATOM	1167	CZ	TYR	C	151	9.018	44.504	12.721	1.00	50.42	GZ00	C
ATOM	1168	OH	TYR	C	151	10.045	45.224	12.149	1.00	41.96	GZ00	O
ATOM	1169	N	PHE	C	152	3.617	44.474	14.824	1.00	40.95	GZ00	N
ATOM	1170	CA	PHE	C	152	3.224	45.868	14.926	1.00	45.04	GZ00	C
ATOM	1171	C	PHE	C	152	3.209	46.273	16.388	1.00	42.56	GZ00	C
ATOM	1172	O	PHE	C	152	2.802	45.496	17.235	1.00	45.01	GZ00	O
ATOM	1173	CB	PHE	C	152	1.847	46.113	14.294	1.00	47.75	GZ00	C
ATOM	1174	CG	PHE	C	152	1.465	47.558	14.260	1.00	48.38	GZ00	C
ATOM	1175	CD1	PHE	C	152	0.824	48.148	15.339	1.00	48.32	GZ00	C
ATOM	1176	CD2	PHE	C	152	1.783	48.342	13.167	1.00	51.92	GZ00	C
ATOM	1177	CE1	PHE	C	152	0.510	49.493	15.322	1.00	46.78	GZ00	C
ATOM	1178	CE2	PHE	C	152	1.451	49.693	13.144	1.00	49.11	GZ00	C
ATOM	1179	CZ	PHE	C	152	0.824	50.262	14.228	1.00	41.05	GZ00	C
ATOM	1180	N	PRO	C	153	3.698	47.479	16.702	1.00	42.68	GZ00	N
ATOM	1181	CA	PRO	C	153	4.419	48.428	15.848	1.00	52.96	GZ00	C
ATOM	1182	C	PRO	C	153	5.930	48.163	15.829	1.00	52.60	GZ00	C
ATOM	1183	O	PRO	C	153	6.398	47.155	16.353	1.00	54.71	GZ00	O
ATOM	1184	CB	PRO	C	153	4.152	49.766	16.532	1.00	43.17	GZ00	C
ATOM	1185	CG	PRO	C	153	4.224	49.393	17.978	1.00	39.59	GZ00	C
ATOM	1186	CD	PRO	C	153	3.545	48.016	18.065	1.00	40.76	GZ00	C
ATOM	1187	N	GLU	C	154	6.682	49.068	15.220	1.00	50.80	GZ00	N
ATOM	1188	CA	GLU	C	154	8.130	49.012	15.287	1.00	47.84	GZ00	C
ATOM	1189	C	GLU	C	154	8.530	49.382	16.706	1.00	45.65	GZ00	C
ATOM	1190	O	GLU	C	154	7.755	49.990	17.417	1.00	48.79	GZ00	O
ATOM	1191	CB	GLU	C	154	8.749	49.958	14.264	1.00	45.04	GZ00	C
ATOM	1192	CG	GLU	C	154	8.425	49.586	12.831	1.00	49.34	GZ00	C
ATOM	1193	CD	GLU	C	154	9.635	49.012	12.119	1.00	59.99	GZ00	C
ATOM	1194	OE1	GLU	C	154	10.114	49.663	11.168	1.00	58.68	GZ00	O
ATOM	1195	OE2	GLU	C	154	10.120	47.929	12.535	1.00	57.95	GZ00	O1−
ATOM	1196	N	PRO	C	155	9.737	49.006	17.137	1.00	50.54	GZ00	N
ATOM	1197	CA	PRO	C	155	10.755	48.195	16.472	1.00	44.50	GZ00	C
ATOM	1198	C	PRO	C	155	10.803	46.753	16.983	1.00	53.89	GZ00	C
ATOM	1199	O	PRO	C	155	10.174	46.436	17.999	1.00	55.35	GZ00	O
ATOM	1200	CB	PRO	C	155	12.031	48.921	16.845	1.00	44.74	GZ00	C
ATOM	1201	CG	PRO	C	155	11.773	49.333	18.257	1.00	44.99	GZ00	C
ATOM	1202	CD	PRO	C	155	10.279	49.641	18.350	1.00	39.64	GZ00	C
ATOM	1203	N	VAL	C	156	11.530	45.887	16.278	1.00	45.82	GZ00	N
ATOM	1204	CA	VAL	C	156	12.054	44.666	16.870	1.00	55.31	GZ00	C
ATOM	1205	C	VAL	C	156	13.562	44.814	16.945	1.00	52.03	GZ00	C
ATOM	1206	O	VAL	C	156	14.183	45.530	16.153	1.00	55.45	GZ00	O
ATOM	1207	CB	VAL	C	156	11.698	43.375	16.105	1.00	52.00	GZ00	C
ATOM	1208	CG1	VAL	C	156	10.204	43.139	16.092	1.00	51.44	GZ00	C
ATOM	1209	CG2	VAL	C	156	12.231	43.446	14.719	1.00	48.82	GZ00	C
ATOM	1210	N	THR	C	157	14.153	44.146	17.919	1.00	53.96	GZ00	N
ATOM	1211	CA	THR	C	157	15.596	44.007	17.989	1.00	54.98	GZ00	C
ATOM	1212	C	THR	C	157	15.949	42.554	17.732	1.00	54.62	GZ00	C
ATOM	1213	O	THR	C	157	15.221	41.644	18.142	1.00	54.87	GZ00	O
ATOM	1214	CB	THR	C	157	16.140	44.458	19.341	1.00	45.77	GZ00	C
ATOM	1215	OG1	THR	C	157	15.663	43.570	20.361	1.00	57.07	GZ00	O
ATOM	1216	CG2	THR	C	157	15.691	45.877	19.627	1.00	51.52	GZ00	C
ATOM	1217	N	VAL	C	158	17.042	42.345	17.015	1.00	51.30	GZ00	N
ATOM	1218	CA	VAL	C	158	17.521	41.010	16.706	1.00	47.26	GZ00	C
ATOM	1219	C	VAL	C	158	18.988	40.957	17.085	1.00	50.93	GZ00	C
ATOM	1220	O	VAL	C	158	19.767	41.833	16.692	1.00	49.49	GZ00	O
ATOM	1221	CB	VAL	C	158	17.343	40.660	15.219	1.00	46.28	GZ00	C
ATOM	1222	CG1	VAL	C	158	17.733	39.213	14.986	1.00	46.68	GZ00	C
ATOM	1223	CG2	VAL	C	158	15.911	40.951	14.752	1.00	43.16	GZ00	C
ATOM	1224	N	SER	C	159	19.361	39.943	17.850	1.00	51.31	GZ00	N
ATOM	1225	CA	SER	C	159	20.756	39.667	18.134	1.00	44.21	GZ00	C
ATOM	1226	C	SER	C	159	21.001	38.215	17.769	1.00	45.69	GZ00	C
ATOM	1227	O	SER	C	159	20.063	37.437	17.578	1.00	44.40	GZ00	O
ATOM	1228	CB	SER	C	159	21.126	39.946	19.605	1.00	39.33	GZ00	C
ATOM	1229	OG	SER	C	159	20.384	39.132	20.511	1.00	48.22	GZ00	O
ATOM	1230	N	TRP	C	160	22.270	37.863	17.648	1.00	44.65	GZ00	N
ATOM	1231	CA	TRP	C	160	22.671	36.505	17.332	1.00	38.87	GZ00	C
ATOM	1232	C	TRP	C	160	23.533	35.984	18.468	1.00	43.64	GZ00	C
ATOM	1233	O	TRP	C	160	24.351	36.729	19.025	1.00	42.33	GZ00	O
ATOM	1234	CB	TRP	C	160	23.420	36.436	15.998	1.00	36.78	GZ00	C
ATOM	1235	CG	TRP	C	160	22.520	36.662	14.845	1.00	41.44	GZ00	C
ATOM	1236	CD1	TRP	C	160	22.178	37.861	14.294	1.00	39.79	GZ00	C
ATOM	1237	CD2	TRP	C	160	21.786	35.664	14.123	1.00	40.51	GZ00	C
ATOM	1238	NE1	TRP	C	160	21.304	37.671	13.245	1.00	37.10	GZ00	N
ATOM	1239	CE2	TRP	C	160	21.038	36.335	13.125	1.00	36.83	GZ00	C
ATOM	1240	CE3	TRP	C	160	21.695	34.270	14.216	1.00	38.13	GZ00	C
ATOM	1241	CZ2	TRP	C	160	20.209	35.662	12.228	1.00	37.10	GZ00	C
ATOM	1242	CZ3	TRP	C	160	20.878	33.596	13.314	1.00	42.58	GZ00	C
ATOM	1243	CH2	TRP	C	160	20.142	34.294	12.336	1.00	43.28	GZ00	C
ATOM	1244	N	ASN	C	161	23.291	34.718	18.825	1.00	41.18	GZ00	N
ATOM	1245	CA	ASN	C	161	23.956	34.018	19.929	1.00	45.75	GZ00	C
ATOM	1246	C	ASN	C	161	24.057	34.898	21.169	1.00	45.89	GZ00	C
ATOM	1247	O	ASN	C	161	25.123	35.079	21.763	1.00	49.59	GZ00	O
ATOM	1248	CB	ASN	C	161	25.315	33.479	19.496	1.00	36.85	GZ00	C
ATOM	1249	CG	ASN	C	161	25.181	32.440	18.399	1.00	44.50	GZ00	C
ATOM	1250	OD1	ASN	C	161	24.067	32.010	18.062	1.00	46.14	GZ00	O
ATOM	1251	ND2	ASN	C	161	26.306	31.997	17.865	1.00	43.54	GZ00	N
ATOM	1252	N	SER	C	162	22.918	35.503	21.508	1.00	46.88	GZ00	N
ATOM	1253	CA	SER	C	162	22.740	36.290	22.727	1.00	43.45	GZ00	C
ATOM	1254	C	SER	C	162	23.687	37.476	22.784	1.00	47.59	GZ00	C
ATOM	1255	O	SER	C	162	24.110	37.883	23.866	1.00	49.00	GZ00	O
ATOM	1256	CB	SER	C	162	22.879	35.412	23.972	1.00	38.83	GZ00	C
ATOM	1257	OG	SER	C	162	22.029	34.280	23.821	1.00	48.75	GZ00	O
ATOM	1258	N	GLY	C	163	24.028	38.040	21.622	1.00	48.38	GZ00	N
ATOM	1259	CA	GLY	C	163	24.887	39.205	21.551	1.00	40.94	GZ00	C
ATOM	1260	C	GLY	C	163	26.359	38.927	21.292	1.00	53.03	GZ00	C
ATOM	1261	O	GLY	C	163	27.105	39.878	20.999	1.00	49.49	GZ00	O
ATOM	1262	N	ALA	C	164	26.804	37.665	21.374	1.00	39.35	GZ00	N
ATOM	1263	CA	ALA	C	164	28.227	37.381	21.179	1.00	50.46	GZ00	C
ATOM	1264	C	ALA	C	164	28.658	37.609	19.732	1.00	52.21	GZ00	C
ATOM	1265	O	ALA	C	164	29.776	38.077	19.475	1.00	52.82	GZ00	O
ATOM	1266	CB	ALA	C	164	28.544	35.947	21.599	1.00	41.14	GZ00	C
ATOM	1267	N	LEU	C	165	27.793	37.267	18.780	1.00	42.69	GZ00	N
ATOM	1268	CA	LEU	C	165	28.085	37.349	17.355	1.00	43.42	GZ00	C
ATOM	1269	C	LEU	C	165	27.513	38.653	16.821	1.00	44.45	GZ00	C
ATOM	1270	O	LEU	C	165	26.292	38.824	16.778	1.00	55.89	GZ00	O
ATOM	1271	CB	LEU	C	165	27.476	36.152	16.631	1.00	43.81	GZ00	C
ATOM	1272	CG	LEU	C	165	27.622	36.030	15.125	1.00	44.99	GZ00	C
ATOM	1273	CD1	LEU	C	165	29.090	36.095	14.649	1.00	39.41	GZ00	C
ATOM	1274	CD2	LEU	C	165	26.958	34.734	14.708	1.00	42.07	GZ00	C
ATOM	1275	N	THR	C	166	28.389	39.563	16.411	1.00	43.67	GZ00	N
ATOM	1276	CA	THR	C	166	28.013	40.872	15.890	1.00	50.96	GZ00	C
ATOM	1277	C	THR	C	166	28.621	41.169	14.521	1.00	48.02	GZ00	C
ATOM	1278	O	THR	C	166	27.950	41.770	13.676	1.00	46.23	GZ00	O
ATOM	1279	CB	THR	C	166	28.415	41.954	16.912	1.00	52.37	GZ00	C
ATOM	1280	OG1	THR	C	166	29.835	41.950	17.073	1.00	48.81	GZ00	O
ATOM	1281	CG2	THR	C	166	27.770	41.663	18.271	1.00	45.85	GZ00	C
ATOM	1282	N	SER	C	167	29.856	40.736	14.268	1.00	44.72	GZ00	N
ATOM	1283	CA	SER	C	167	30.445	40.880	12.941	1.00	46.25	GZ00	C
ATOM	1284	C	SER	C	167	29.673	40.045	11.937	1.00	42.05	GZ00	C
ATOM	1285	O	SER	C	167	29.319	38.894	12.201	1.00	43.05	GZ00	O
ATOM	1286	CB	SER	C	167	31.909	40.437	12.933	1.00	39.29	GZ00	C
ATOM	1287	OG	SER	C	167	32.675	41.320	13.706	1.00	49.43	GZ00	O
ATOM	1288	N	GLY	C	168	29.424	40.629	10.779	1.00	39.63	GZ00	N
ATOM	1289	CA	GLY	C	168	28.689	39.955	9.740	1.00	37.44	GZ00	C
ATOM	1290	C	GLY	C	168	27.189	39.958	9.919	1.00	39.53	GZ00	C
ATOM	1291	O	GLY	C	168	26.500	39.304	9.131	1.00	41.74	GZ00	O
ATOM	1292	N	VAL	C	169	26.653	40.702	10.893	1.00	37.21	GZ00	N
ATOM	1293	CA	VAL	C	169	25.219	40.711	11.158	1.00	39.62	GZ00	C
ATOM	1294	C	VAL	C	169	24.583	41.858	10.391	1.00	34.91	GZ00	C
ATOM	1295	O	VAL	C	169	24.991	43.010	10.529	1.00	35.65	GZ00	O
ATOM	1296	CB	VAL	C	169	24.921	40.858	12.660	1.00	42.01	GZ00	C
ATOM	1297	CG1	VAL	C	169	23.404	41.063	12.867	1.00	36.86	GZ00	C
ATOM	1298	CG2	VAL	C	169	25.410	39.673	13.434	1.00	42.36	GZ00	C
ATOM	1299	N	HIS	C	170	23.545	41.564	9.630	1.00	37.60	GZ00	N
ATOM	1300	CA	HIS	C	170	22.842	42.603	8.889	1.00	37.31	GZ00	C
ATOM	1301	C	HIS	C	170	21.345	42.438	9.134	1.00	37.74	GZ00	C
ATOM	1302	O	HIS	C	170	20.704	41.559	8.554	1.00	38.41	GZ00	O
ATOM	1303	CB	HIS	C	170	23.180	42.538	7.406	1.00	34.76	GZ00	C
ATOM	1304	CG	HIS	C	170	22.719	43.735	6.634	1.00	43.07	GZ00	C
ATOM	1305	ND1	HIS	C	170	22.966	43.897	5.287	1.00	43.71	GZ00	N
ATOM	1306	CD2	HIS	C	170	22.022	44.830	7.023	1.00	40.56	GZ00	C
ATOM	1307	CE1	HIS	C	170	22.453	45.045	4.883	1.00	45.93	GZ00	C
ATOM	1308	NE2	HIS	C	170	21.866	45.626	5.915	1.00	45.52	GZ00	N
ATOM	1309	N	THR	C	171	20.787	43.270	10.006	1.00	40.13	GZ00	N
ATOM	1310	CA	THR	C	171	19.342	43.337	10.182	1.00	39.22	GZ00	C
ATOM	1311	C	THR	C	171	18.800	44.400	9.230	1.00	39.29	GZ00	C
ATOM	1312	O	THR	C	171	19.079	45.581	9.404	1.00	36.69	GZ00	O
ATOM	1313	CB	THR	C	171	18.984	43.680	11.629	1.00	39.31	GZ00	C
ATOM	1314	OG1	THR	C	171	19.473	42.647	12.494	1.00	41.01	GZ00	O
ATOM	1315	CG2	THR	C	171	17.445	43.812	11.801	1.00	33.43	GZ00	C
ATOM	1316	N	PHE	C	172	17.989	43.982	8.262	1.00	38.72	GZ00	N
ATOM	1317	CA	PHE	C	172	17.457	44.839	7.215	1.00	38.37	GZ00	C
ATOM	1318	C	PHE	C	172	16.263	45.638	7.728	1.00	39.77	GZ00	C
ATOM	1319	O	PHE	C	172	15.478	45.140	8.537	1.00	41.83	GZ00	O
ATOM	1320	CB	PHE	C	172	16.990	44.017	6.013	1.00	35.77	GZ00	C
ATOM	1321	CG	PHE	C	172	18.092	43.449	5.195	1.00	34.43	GZ00	C
ATOM	1322	CD1	PHE	C	172	18.884	42.416	5.679	1.00	40.25	GZ00	C
ATOM	1323	CD2	PHE	C	172	18.354	43.957	3.936	1.00	40.94	GZ00	C
ATOM	1324	CE1	PHE	C	172	19.914	41.886	4.906	1.00	37.45	GZ00	C
ATOM	1325	CE2	PHE	C	172	19.389	43.434	3.162	1.00	43.89	GZ00	C
ATOM	1326	CZ	PHE	C	172	20.164	42.395	3.650	1.00	36.64	GZ00	C
ATOM	1327	N	PRO	C	173	16.092	46.871	7.252	1.00	37.95	GZ00	N
ATOM	1328	CA	PRO	C	173	14.883	47.639	7.596	1.00	33.97	GZ00	C
ATOM	1329	C	PRO	C	173	13.616	46.905	7.173	1.00	35.10	GZ00	C
ATOM	1330	O	PRO	C	173	13.585	46.195	6.163	1.00	33.25	GZ00	O
ATOM	1331	CB	PRO	C	173	15.064	48.945	6.817	1.00	35.19	GZ00	C
ATOM	1332	CG	PRO	C	173	16.573	49.046	6.616	1.00	34.04	GZ00	C
ATOM	1333	CD	PRO	C	173	17.049	47.638	6.441	1.00	32.78	GZ00	C
ATOM	1334	N	ALA	C	174	12.550	47.109	7.945	1.00	39.15	GZ00	N
ATOM	1335	CA	ALA	C	174	11.316	46.339	7.783	1.00	39.81	GZ00	C
ATOM	1336	C	ALA	C	174	10.533	46.750	6.532	1.00	35.98	GZ00	C
ATOM	1337	O	ALA	C	174	10.677	47.856	6.028	1.00	39.58	GZ00	O
ATOM	1338	CB	ALA	C	174	10.432	46.527	9.013	1.00	43.39	GZ00	C
ATOM	1339	N	VAL	C	175	9.686	45.824	6.013	1.00	38.79	GZ00	N
ATOM	1340	CA	VAL	C	175	8.639	46.209	5.066	1.00	39.33	GZ00	C
ATOM	1341	C	VAL	C	175	7.400	46.592	5.844	1.00	44.21	GZ00	C
ATOM	1342	O	VAL	C	175	7.056	45.957	6.847	1.00	43.28	GZ00	O
ATOM	1343	CB	VAL	C	175	8.256	45.087	4.084	1.00	50.56	GZ00	C
ATOM	1344	CG1	VAL	C	175	8.851	45.303	2.713	1.00	51.62	GZ00	C
ATOM	1345	CG2	VAL	C	175	8.510	43.718	4.667	1.00	44.82	GZ00	C
ATOM	1346	N	LEU	C	176	6.686	47.587	5.342	1.00	46.20	GZ00	N
ATOM	1347	CA	LEU	C	176	5.329	47.863	5.785	1.00	41.81	GZ00	C
ATOM	1348	C	LEU	C	176	4.400	47.199	4.775	1.00	42.53	GZ00	C
ATOM	1349	O	LEU	C	176	4.405	47.554	3.595	1.00	55.35	GZ00	O
ATOM	1350	CB	LEU	C	176	5.082	49.361	5.889	1.00	43.16	GZ00	C
ATOM	1351	CG	LEU	C	176	3.653	49.738	6.270	1.00	46.81	GZ00	C
ATOM	1352	CD1	LEU	C	176	3.258	48.982	7.523	1.00	39.25	GZ00	C
ATOM	1353	CD2	LEU	C	176	3.565	51.241	6.509	1.00	41.80	GZ00	C
ATOM	1354	N	GLN	C	177	3.666	46.189	5.219	1.00	44.53	GZ00	N
ATOM	1355	CA	GLN	C	177	2.809	45.403	4.345	1.00	50.59	GZ00	C
ATOM	1356	C	GLN	C	177	1.442	46.069	4.173	1.00	49.14	GZ00	C
ATOM	1357	O	GLN	C	177	0.999	46.856	5.018	1.00	43.05	GZ00	O
ATOM	1358	CB	GLN	C	177	2.634	43.990	4.909	1.00	46.96	GZ00	C
ATOM	1359	CG	GLN	C	177	3.923	43.188	5.105	1.00	49.24	GZ00	C
ATOM	1360	CD	GLN	C	177	3.666	41.894	5.863	1.00	56.86	GZ00	C
ATOM	1361	OE1	GLN	C	177	3.214	40.898	5.285	1.00	62.22	GZ00	O
ATOM	1362	NE2	GLN	C	177	3.939	41.905	7.170	1.00	48.26	GZ00	N
ATOM	1363	N	SER	C	178	0.751	45.698	3.084	1.00	45.38	GZ00	N
ATOM	1364	CA	SER	C	178	−0.624	46.166	2.867	1.00	48.86	GZ00	C
ATOM	1365	C	SER	C	178	−1.544	45.854	4.039	1.00	46.49	GZ00	C
ATOM	1366	O	SER	C	178	−2.528	46.562	4.260	1.00	57.16	GZ00	O
ATOM	1367	CB	SER	C	178	−1.216	45.531	1.617	1.00	50.40	GZ00	C
ATOM	1368	OG	SER	C	178	−0.204	45.003	0.795	1.00	71.70	GZ00	O
ATOM	1369	N	SER	C	179	−1.258	44.793	4.786	1.00	50.74	GZ00	N
ATOM	1370	CA	SER	C	179	−1.988	44.477	6.007	1.00	43.18	GZ00	C
ATOM	1371	C	SER	C	179	−1.776	45.503	7.110	1.00	49.34	GZ00	C
ATOM	1372	O	SER	C	179	−2.482	45.454	8.121	1.00	48.58	GZ00	O
ATOM	1373	CB	SER	C	179	−1.546	43.111	6.513	1.00	44.27	GZ00	C
ATOM	1374	OG	SER	C	179	−0.258	43.204	7.095	1.00	48.97	GZ00	O
ATOM	1375	N	GLY	C	180	−0.798	46.398	6.970	1.00	46.74	GZ00	N
ATOM	1376	CA	GLY	C	180	−0.440	47.281	8.059	1.00	45.92	GZ00	C
ATOM	1377	C	GLY	C	180	0.566	46.707	9.037	1.00	50.25	GZ00	C
ATOM	1378	O	GLY	C	180	0.916	47.389	10.012	1.00	43.25	GZ00	O
ATOM	1379	N	LEU	C	181	1.039	45.481	8.813	1.00	44.89	GZ00	N
ATOM	1380	CA	LEU	C	181	2.003	44.836	9.695	1.00	49.99	GZ00	C
ATOM	1381	C	LEU	C	181	3.408	44.908	9.101	1.00	47.59	GZ00	C
ATOM	1382	O	LEU	C	181	3.594	45.023	7.887	1.00	47.03	GZ00	O
ATOM	1383	CB	LEU	C	181	1.621	43.373	9.938	1.00	43.97	GZ00	C
ATOM	1384	CG	LEU	C	181	0.269	43.159	10.616	1.00	50.80	GZ00	C
ATOM	1385	CD1	LEU	C	181	−0.047	41.676	10.719	1.00	43.98	GZ00	C
ATOM	1386	CD2	LEU	C	181	0.246	43.830	11.981	1.00	46.56	GZ00	C
ATOM	1387	N	TYR	C	182	4.404	44.833	9.973	1.00	45.32	GZ00	N
ATOM	1388	CA	TYR	C	182	5.793	44.866	9.536	1.00	45.62	GZ00	C
ATOM	1389	C	TYR	C	182	6.381	43.465	9.437	1.00	44.85	GZ00	C
ATOM	1390	O	TYR	C	182	5.955	42.536	10.124	1.00	51.18	GZ00	O
ATOM	1391	CB	TYR	C	182	6.645	45.701	10.484	1.00	44.25	GZ00	C
ATOM	1392	CG	TYR	C	182	6.265	47.162	10.529	1.00	49.19	GZ00	C
ATOM	1393	CD1	TYR	C	182	6.805	48.072	9.628	1.00	49.61	GZ00	C
ATOM	1394	CD2	TYR	C	182	5.368	47.633	11.474	1.00	51.64	GZ00	C
ATOM	1395	CE1	TYR	C	182	6.474	49.408	9.678	1.00	43.85	GZ00	C
ATOM	1396	CE2	TYR	C	182	5.029	48.974	11.530	1.00	55.94	GZ00	C
ATOM	1397	CZ	TYR	C	182	5.587	49.853	10.626	1.00	50.36	GZ00	C
ATOM	1398	OH	TYR	C	182	5.243	51.177	10.679	1.00	43.75	GZ00	O
ATOM	1399	N	SER	C	183	7.374	43.326	8.569	1.00	46.44	GZ00	N
ATOM	1400	CA	SER	C	183	8.231	42.152	8.534	1.00	42.34	GZ00	C
ATOM	1401	C	SER	C	183	9.673	42.600	8.304	1.00	42.61	GZ00	C
ATOM	1402	O	SER	C	183	9.927	43.635	7.681	1.00	42.07	GZ00	O
ATOM	1403	CB	SER	C	183	7.799	41.173	7.452	1.00	40.89	GZ00	C
ATOM	1404	OG	SER	C	183	6.531	40.617	7.751	1.00	50.66	GZ00	O
ATOM	1405	N	LEU	C	184	10.622	41.838	8.842	1.00	42.23	GZ00	N
ATOM	1406	CA	LEU	C	184	12.018	42.081	8.515	1.00	39.25	GZ00	C
ATOM	1407	C	LEU	C	184	12.794	40.772	8.518	1.00	43.48	GZ00	C
ATOM	1408	O	LEU	C	184	12.337	39.746	9.029	1.00	40.77	GZ00	O
ATOM	1409	CB	LEU	C	184	12.650	43.095	9.473	1.00	35.18	GZ00	C
ATOM	1410	CG	LEU	C	184	12.809	42.808	10.965	1.00	45.00	GZ00	C
ATOM	1411	CD1	LEU	C	184	13.869	41.700	11.303	1.00	40.29	GZ00	C
ATOM	1412	CD2	LEU	C	184	13.218	44.117	11.588	1.00	33.99	GZ00	C
ATOM	1413	N	SER	C	185	14.012	40.842	7.986	1.00	44.24	GZ00	N
ATOM	1414	CA	SER	C	185	14.963	39.747	8.041	1.00	35.64	GZ00	C
ATOM	1415	C	SER	C	185	16.258	40.228	8.669	1.00	41.38	GZ00	C
ATOM	1416	O	SER	C	185	16.650	41.392	8.526	1.00	39.54	GZ00	O
ATOM	1417	CB	SER	C	185	15.260	39.197	6.661	1.00	36.15	GZ00	C
ATOM	1418	OG	SER	C	185	14.075	38.752	6.055	1.00	40.64	GZ00	O
ATOM	1419	N	SER	C	186	16.927	39.308	9.349	1.00	38.32	GZ00	N
ATOM	1420	CA	SER	C	186	18.265	39.524	9.871	1.00	36.92	GZ00	C
ATOM	1421	C	SER	C	186	19.108	38.382	9.349	1.00	40.04	GZ00	C
ATOM	1422	O	SER	C	186	18.687	37.226	9.434	1.00	43.87	GZ00	O
ATOM	1423	CB	SER	C	186	18.273	39.558	11.396	1.00	38.94	GZ00	C
ATOM	1424	OG	SER	C	186	19.589	39.675	11.902	1.00	39.68	GZ00	O
ATOM	1425	N	VAL	C	187	20.267	38.698	8.773	1.00	38.05	GZ00	N
ATOM	1426	CA	VAL	C	187	21.164	37.675	8.245	1.00	39.23	GZ00	C
ATOM	1427	C	VAL	C	187	22.543	37.869	8.849	1.00	38.02	GZ00	C
ATOM	1428	O	VAL	C	187	22.977	38.990	9.130	1.00	40.44	GZ00	O
ATOM	1429	CB	VAL	C	187	21.291	37.714	6.708	1.00	42.17	GZ00	C
ATOM	1430	CG1	VAL	C	187	19.984	37.334	6.048	1.00	51.50	GZ00	C
ATOM	1431	CG2	VAL	C	187	21.733	39.100	6.265	1.00	42.55	GZ00	C
ATOM	1432	N	VAL	C	188	23.252	36.770	9.018	1.00	36.36	GZ00	N
ATOM	1433	CA	VAL	C	188	24.640	36.836	9.426	1.00	36.04	GZ00	C
ATOM	1434	C	VAL	C	188	25.458	36.076	8.397	1.00	29.41	GZ00	C
ATOM	1435	O	VAL	C	188	25.037	35.025	7.901	1.00	36.76	GZ00	O
ATOM	1436	CB	VAL	C	188	24.848	36.314	10.861	1.00	42.84	GZ00	C
ATOM	1437	CG1	VAL	C	188	24.200	34.977	11.043	1.00	38.37	GZ00	C
ATOM	1438	CG2	VAL	C	188	26.343	36.272	11.210	1.00	41.22	GZ00	C
ATOM	1439	N	THR	C	189	26.558	36.673	8.000	1.00	28.33	GZ00	N
ATOM	1440	CA	THR	C	189	27.541	36.056	7.132	1.00	32.84	GZ00	C
ATOM	1441	C	THR	C	189	28.628	35.434	8.001	1.00	34.03	GZ00	C
ATOM	1442	O	THR	C	189	29.180	36.100	8.883	1.00	35.30	GZ00	O
ATOM	1443	CB	THR	C	189	28.159	37.112	6.215	1.00	32.93	GZ00	C
ATOM	1444	OG1	THR	C	189	27.144	37.724	5.438	1.00	45.99	GZ00	O
ATOM	1445	CG2	THR	C	189	29.182	36.491	5.293	1.00	42.71	GZ00	C
ATOM	1446	N	VAL	C	190	28.939	34.171	7.745	1.00	34.62	GZ00	N
ATOM	1447	CA	VAL	C	190	29.911	33.429	8.544	1.00	31.43	GZ00	C
ATOM	1448	C	VAL	C	190	30.828	32.676	7.590	1.00	33.62	GZ00	C
ATOM	1449	O	VAL	C	190	30.489	32.452	6.412	1.00	32.38	GZ00	O
ATOM	1450	CB	VAL	C	190	29.217	32.438	9.514	1.00	32.44	GZ00	C
ATOM	1451	CG1	VAL	C	190	28.249	33.160	10.466	1.00	30.52	GZ00	C
ATOM	1452	CG2	VAL	C	190	28.516	31.364	8.716	1.00	32.19	GZ00	C
ATOM	1453	N	PRO	C	191	31.989	32.240	8.078	1.00	30.12	GZ00	N
ATOM	1454	CA	PRO	C	191	32.826	31.359	7.271	1.00	32.76	GZ00	C
ATOM	1455	C	PRO	C	191	32.058	30.080	6.963	1.00	30.65	GZ00	C
ATOM	1456	O	PRO	C	191	31.363	29.531	7.820	1.00	33.10	GZ00	O
ATOM	1457	CB	PRO	C	191	34.045	31.120	8.172	1.00	32.26	GZ00	C
ATOM	1458	CG	PRO	C	191	34.060	32.297	9.081	1.00	34.77	GZ00	C
ATOM	1459	CD	PRO	C	191	32.645	32.579	9.350	1.00	27.68	GZ00	C
ATOM	1460	N	SER	C	192	32.149	29.634	5.711	1.00	29.53	GZ00	N
ATOM	1461	CA	SER	C	192	31.350	28.487	5.287	1.00	39.33	GZ00	C
ATOM	1462	C	SER	C	192	31.675	27.230	6.099	1.00	36.23	GZ00	C
ATOM	1463	O	SER	C	192	30.769	26.485	6.472	1.00	42.93	GZ00	O
ATOM	1464	CB	SER	C	192	31.541	28.240	3.789	1.00	38.81	GZ00	C
ATOM	1465	OG	SER	C	192	32.874	27.909	3.459	1.00	43.23	GZ00	O
ATOM	1466	N	SER	C	193	32.938	27.035	6.471	1.00	34.82	GZ00	N
ATOM	1467	CA	SER	C	193	33.323	25.884	7.287	1.00	34.53	GZ00	C
ATOM	1468	C	SER	C	193	32.696	25.922	8.671	1.00	34.09	GZ00	C
ATOM	1469	O	SER	C	193	32.757	24.928	9.386	1.00	39.08	GZ00	O
ATOM	1470	CB	SER	C	193	34.853	25.776	7.406	1.00	30.12	GZ00	C
ATOM	1471	OG	SER	C	193	35.392	26.892	8.093	1.00	36.36	GZ00	O
ATOM	1472	N	SER	C	194	32.163	27.056	9.102	1.00	38.37	GZ00	N
ATOM	1473	CA	SER	C	194	31.530	27.087	10.411	1.00	33.39	GZ00	C
ATOM	1474	C	SER	C	194	30.113	26.516	10.401	1.00	42.74	GZ00	C
ATOM	1475	O	SER	C	194	29.523	26.338	11.474	1.00	39.11	GZ00	O
ATOM	1476	CB	SER	C	194	31.499	28.525	10.943	1.00	36.98	GZ00	C
ATOM	1477	OG	SER	C	194	32.808	29.033	11.127	1.00	48.78	GZ00	O
ATOM	1478	N	LEU	C	195	29.544	26.221	9.235	1.00	39.64	GZ00	N
ATOM	1479	CA	LEU	C	195	28.171	25.716	9.219	1.00	49.46	GZ00	C
ATOM	1480	C	LEU	C	195	28.073	24.358	9.912	1.00	44.13	GZ00	C
ATOM	1481	O	LEU	C	195	27.079	24.064	10.584	1.00	58.41	GZ00	O
ATOM	1482	CB	LEU	C	195	27.658	25.619	7.783	1.00	39.54	GZ00	C
ATOM	1483	CG	LEU	C	195	27.446	26.952	7.097	1.00	40.14	GZ00	C
ATOM	1484	CD1	LEU	C	195	26.943	26.739	5.696	1.00	44.58	GZ00	C
ATOM	1485	CD2	LEU	C	195	26.470	27.772	7.904	1.00	40.80	GZ00	C
ATOM	1486	N	GLY	C	196	29.081	23.506	9.744	1.00	51.36	GZ00	N
ATOM	1487	CA	GLY	C	196	29.046	22.221	10.420	1.00	65.18	GZ00	C
ATOM	1488	C	GLY	C	196	29.407	22.268	11.889	1.00	66.41	GZ00	C
ATOM	1489	O	GLY	C	196	29.013	21.375	12.644	1.00	61.49	GZ00	O
ATOM	1490	N	THR	C	197	30.128	23.300	12.314	1.00	62.25	GZ00	N
ATOM	1491	CA	THR	C	197	30.755	23.340	13.626	1.00	58.93	GZ00	C
ATOM	1492	C	THR	C	197	29.995	24.161	14.655	1.00	58.26	GZ00	C
ATOM	1493	O	THR	C	197	30.047	23.842	15.845	1.00	62.50	GZ00	O
ATOM	1494	CB	THR	C	197	32.165	23.899	13.486	1.00	60.74	GZ00	C
ATOM	1495	OG1	THR	C	197	32.802	23.224	12.405	1.00	62.30	GZ00	O
ATOM	1496	CG2	THR	C	197	32.961	23.642	14.759	1.00	74.83	GZ00	C
ATOM	1497	N	GLN	C	198	29.373	25.261	14.243	1.00	52.75	GZ00	N
ATOM	1498	CA	GLN	C	198	28.836	26.250	15.166	1.00	50.37	GZ00	C
ATOM	1499	C	GLN	C	198	27.314	26.260	15.176	1.00	47.44	GZ00	C
ATOM	1500	O	GLN	C	198	26.650	25.910	14.197	1.00	47.96	GZ00	O
ATOM	1501	CB	GLN	C	198	29.345	27.650	14.839	1.00	49.33	GZ00	C
ATOM	1502	CG	GLN	C	198	30.852	27.725	14.782	1.00	55.27	GZ00	C
ATOM	1503	CD	GLN	C	198	31.515	27.225	16.062	1.00	61.24	GZ00	C
ATOM	1504	OE1	GLN	C	198	32.566	26.585	16.007	1.00	51.30	GZ00	O
ATOM	1505	NE2	GLN	C	198	30.903	27.517	17.218	1.00	56.92	GZ00	N
ATOM	1506	N	THR	C	199	26.773	26.623	16.322	1.00	52.47	GZ00	N
ATOM	1507	CA	THR	C	199	25.343	26.782	16.481	1.00	55.26	GZ00	C
ATOM	1508	C	THR	C	199	25.008	28.268	16.402	1.00	49.37	GZ00	C
ATOM	1509	O	THR	C	199	25.618	29.094	17.092	1.00	42.11	GZ00	O
ATOM	1510	CB	THR	C	199	24.875	26.156	17.795	1.00	51.51	GZ00	C
ATOM	1511	OG1	THR	C	199	24.993	24.734	17.686	1.00	63.19	GZ00	O
ATOM	1512	CG2	THR	C	199	23.428	26.505	18.070	1.00	53.59	GZ00	C
ATOM	1513	N	TYR	C	200	24.078	28.610	15.518	1.00	48.90	GZ00	N
ATOM	1514	CA	TYR	C	200	23.662	29.990	15.315	1.00	48.61	GZ00	C
ATOM	1515	C	TYR	C	200	22.209	30.127	15.721	1.00	46.13	GZ00	C
ATOM	1516	O	TYR	C	200	21.332	29.443	15.173	1.00	44.41	GZ00	O
ATOM	1517	CB	TYR	C	200	23.885	30.425	13.871	1.00	40.49	GZ00	C
ATOM	1518	CG	TYR	C	200	25.348	30.403	13.527	1.00	43.98	GZ00	C
ATOM	1519	CD1	TYR	C	200	26.196	31.359	14.053	1.00	42.42	GZ00	C
ATOM	1520	CD2	TYR	C	200	25.891	29.415	12.718	1.00	41.47	GZ00	C
ATOM	1521	CE1	TYR	C	200	27.536	31.356	13.770	1.00	39.19	GZ00	C
ATOM	1522	CE2	TYR	C	200	27.254	29.408	12.425	1.00	45.38	GZ00	C
ATOM	1523	CZ	TYR	C	200	28.062	30.394	12.954	1.00	39.23	GZ00	C
ATOM	1524	OH	TYR	C	200	29.417	30.433	12.699	1.00	45.19	GZ00	O
ATOM	1525	N	ILE	C	201	21.975	30.996	16.697	1.00	42.87	GZ00	N
ATOM	1526	CA	ILE	C	201	20.663	31.253	17.264	1.00	42.84	GZ00	C
ATOM	1527	C	ILE	C	201	20.414	32.743	17.188	1.00	44.10	GZ00	C
ATOM	1528	O	ILE	C	201	21.240	33.530	17.663	1.00	46.46	GZ00	O
ATOM	1529	CB	ILE	C	201	20.581	30.788	18.727	1.00	50.09	GZ00	C
ATOM	1530	CG1	ILE	C	201	20.743	29.262	18.814	1.00	45.99	GZ00	C
ATOM	1531	CG2	ILE	C	201	19.298	31.312	19.375	1.00	42.60	GZ00	C
ATOM	1532	CD1	ILE	C	201	20.953	28.790	20.208	1.00	32.65	GZ00	C
ATOM	1533	N	CYS	C	202	19.279	33.131	16.604	1.00	42.47	GZ00	N
ATOM	1534	CA	CYS	C	202	18.862	34.523	16.601	1.00	43.27	GZ00	C
ATOM	1535	C	CYS	C	202	17.860	34.776	17.723	1.00	49.37	GZ00	C
ATOM	1536	O	CYS	C	202	17.021	33.922	18.040	1.00	48.50	GZ00	O
ATOM	1537	CB	CYS	C	202	18.262	34.923	15.250	1.00	47.82	GZ00	C
ATOM	1538	SG	CYS	C	202	16.539	34.525	15.045	1.00	59.08	GZ00	S
ATOM	1539	N	ASN	C	203	17.976	35.945	18.341	1.00	44.56	GZ00	N
ATOM	1540	CA	ASN	C	203	17.167	36.321	19.492	1.00	39.69	GZ00	C
ATOM	1541	C	ASN	C	203	16.329	37.519	19.079	1.00	46.86	GZ00	C
ATOM	1542	O	ASN	C	203	16.862	38.616	18.876	1.00	43.01	GZ00	O
ATOM	1543	CB	ASN	C	203	18.043	36.660	20.698	1.00	40.17	GZ00	C
ATOM	1544	CG	ASN	C	203	19.277	35.769	20.785	1.00	50.91	GZ00	C
ATOM	1545	OD1	ASN	C	203	20.407	36.239	20.626	1.00	44.43	GZ00	O
ATOM	1546	ND2	ASN	C	203	19.057	34.467	20.968	1.00	40.98	GZ00	N
ATOM	1547	N	VAL	C	204	15.027	37.320	18.972	1.00	44.56	GZ00	N
ATOM	1548	CA	VAL	C	204	14.126	38.360	18.515	1.00	46.34	GZ00	C
ATOM	1549	C	VAL	C	204	13.377	38.894	19.715	1.00	43.52	GZ00	C
ATOM	1550	O	VAL	C	204	12.839	38.122	20.516	1.00	51.43	GZ00	O
ATOM	1551	CB	VAL	C	204	13.166	37.826	17.447	1.00	50.83	GZ00	C
ATOM	1552	CG1	VAL	C	204	12.204	38.932	17.006	1.00	40.92	GZ00	C
ATOM	1553	CG2	VAL	C	204	13.984	37.271	16.291	1.00	38.78	GZ00	C
ATOM	1554	N	ASN	C	205	13.361	40.208	19.858	1.00	40.86	GZ00	N
ATOM	1555	CA	ASN	C	205	12.687	40.856	20.970	1.00	54.57	GZ00	C
ATOM	1556	C	ASN	C	205	11.772	41.947	20.431	1.00	58.30	GZ00	C
ATOM	1557	O	ASN	C	205	12.237	42.886	19.776	1.00	55.70	GZ00	O
ATOM	1558	CB	ASN	C	205	13.691	41.445	21.965	1.00	49.16	GZ00	C
ATOM	1559	CG	ASN	C	205	13.009	42.013	23.204	1.00	69.12	GZ00	C
ATOM	1560	OD1	ASN	C	205	11.837	41.702	23.489	1.00	63.20	GZ00	O
ATOM	1561	ND2	ASN	C	205	13.716	42.884	23.921	1.00	72.08	GZ00	N
ATOM	1562	N	HIS	C	206	10.482	41.839	20.732	1.00	55.60	GZ00	N
ATOM	1563	CA	HIS	C	206	9.489	42.834	20.326	1.00	56.54	GZ00	C
ATOM	1564	C	HIS	C	206	8.843	43.347	21.611	1.00	58.64	GZ00	C
ATOM	1565	O	HIS	C	206	7.857	42.788	22.098	1.00	54.70	GZ00	O
ATOM	1566	CB	HIS	C	206	8.472	42.249	19.356	1.00	51.09	GZ00	C
ATOM	1567	CG	HIS	C	206	7.482	43.251	18.851	1.00	60.00	GZ00	C
ATOM	1568	ND1	HIS	C	206	6.150	42.954	18.660	1.00	56.09	GZ00	N
ATOM	1569	CD2	HIS	C	206	7.633	44.548	18.494	1.00	60.16	GZ00	C
ATOM	1570	CE1	HIS	C	206	5.525	44.026	18.209	1.00	55.91	GZ00	C
ATOM	1571	NE2	HIS	C	206	6.402	45.007	18.100	1.00	50.50	GZ00	N
ATOM	1572	N	LYS	C	207	9.435	44.398	22.179	1.00	59.62	GZ00	N
ATOM	1573	CA	LYS	C	207	8.977	44.892	23.475	1.00	60.73	GZ00	C
ATOM	1574	C	LYS	C	207	7.519	45.338	23.493	1.00	69.23	GZ00	C
ATOM	1575	O	LYS	C	207	6.848	45.083	24.509	1.00	66.50	GZ00	O
ATOM	1576	CB	LYS	C	207	9.906	46.014	23.956	1.00	58.40	GZ00	C
ATOM	1577	CG	LYS	C	207	11.292	45.481	24.321	1.00	69.34	GZ00	C
ATOM	1578	CD	LYS	C	207	12.257	46.543	24.809	1.00	77.26	GZ00	C
ATOM	1579	CE	LYS	C	207	13.596	45.890	25.148	1.00	81.04	GZ00	C
ATOM	1580	NZ	LYS	C	207	14.641	46.873	25.530	1.00	87.24	GZ00	N1+
ATOM	1581	N	PRO	C	208	6.956	45.959	22.441	1.00	69.40	GZ00	N
ATOM	1582	CA	PRO	C	208	5.540	46.372	22.538	1.00	59.57	GZ00	C
ATOM	1583	C	PRO	C	208	4.585	45.244	22.898	1.00	64.04	GZ00	C
ATOM	1584	O	PRO	C	208	3.640	45.466	23.666	1.00	69.66	GZ00	O
ATOM	1585	CB	PRO	C	208	5.257	46.942	21.145	1.00	53.38	GZ00	C
ATOM	1586	CG	PRO	C	208	6.582	47.479	20.704	1.00	65.93	GZ00	C
ATOM	1587	CD	PRO	C	208	7.608	46.524	21.241	1.00	55.91	GZ00	C
ATOM	1588	N	SER	C	209	4.814	44.034	22.401	1.00	60.28	GZ00	N
ATOM	1589	CA	SER	C	209	4.019	42.880	22.786	1.00	57.00	GZ00	C
ATOM	1590	C	SER	C	209	4.762	41.960	23.758	1.00	67.68	GZ00	C
ATOM	1591	O	SER	C	209	4.284	40.848	24.024	1.00	64.38	GZ00	O
ATOM	1592	CB	SER	C	209	3.586	42.091	21.546	1.00	56.00	GZ00	C
ATOM	1593	OG	SER	C	209	4.691	41.469	20.915	1.00	63.30	GZ00	O
ATOM	1594	N	ASN	C	210	5.918	42.392	24.271	1.00	68.38	GZ00	N
ATOM	1595	CA	ASN	C	210	6.846	41.563	25.049	1.00	66.63	GZ00	C
ATOM	1596	C	ASN	C	210	6.898	40.139	24.505	1.00	64.18	GZ00	C
ATOM	1597	O	ASN	C	210	6.538	39.164	25.164	1.00	67.42	GZ00	O
ATOM	1598	CB	ASN	C	210	6.528	41.574	26.543	1.00	74.01	GZ00	C
ATOM	1599	CG	ASN	C	210	5.055	41.657	26.828	1.00	83.26	GZ00	C
ATOM	1600	OD1	ASN	C	210	4.483	42.750	26.885	1.00	89.02	GZ00	O
ATOM	1601	ND2	ASN	C	210	4.420	40.502	26.997	1.00	83.49	GZ00	N
ATOM	1602	N	THR	C	211	7.358	40.045	23.268	1.00	61.55	GZ00	N
ATOM	1603	CA	THR	C	211	7.633	38.772	22.633	1.00	57.57	GZ00	C
ATOM	1604	C	THR	C	211	9.143	38.608	22.609	1.00	60.01	GZ00	C
ATOM	1605	O	THR	C	211	9.862	39.532	22.214	1.00	65.19	GZ00	O
ATOM	1606	CB	THR	C	211	7.089	38.734	21.209	1.00	54.23	GZ00	C
ATOM	1607	OG1	THR	C	211	5.691	39.013	21.227	1.00	60.96	GZ00	O
ATOM	1608	CG2	THR	C	211	7.316	37.377	20.586	1.00	57.50	GZ00	C
ATOM	1609	N	LYS	C	212	9.620	37.460	23.084	1.00	60.21	GZ00	N
ATOM	1610	CA	LYS	C	212	11.018	37.076	22.951	1.00	52.01	GZ00	C
ATOM	1611	C	LYS	C	212	11.042	35.689	22.350	1.00	52.91	GZ00	C
ATOM	1612	O	LYS	C	212	10.456	34.760	22.906	1.00	57.94	GZ00	O
ATOM	1613	CB	LYS	C	212	11.753	37.110	24.290	1.00	47.41	GZ00	C
ATOM	1614	CG	LYS	C	212	11.691	38.475	24.978	1.00	57.15	GZ00	C
ATOM	1615	CD	LYS	C	212	12.644	38.565	26.174	1.00	66.23	GZ00	C
ATOM	1616	CE	LYS	C	212	12.433	39.861	26.969	1.00	79.81	GZ00	C
ATOM	1617	NZ	LYS	C	212	13.705	40.467	27.503	1.00	78.51	GZ00	N1+
ATOM	1618	N	VAL	C	213	11.710	35.555	21.215	1.00	55.55	GZ00	N
ATOM	1619	CA	VAL	C	213	11.839	34.287	20.520	1.00	49.66	GZ00	C
ATOM	1620	C	VAL	C	213	13.319	34.021	20.272	1.00	50.74	GZ00	C
ATOM	1621	O	VAL	C	213	14.050	34.906	19.810	1.00	48.29	GZ00	O
ATOM	1622	CB	VAL	C	213	11.051	34.291	19.199	1.00	51.80	GZ00	C
ATOM	1623	CG1	VAL	C	213	11.260	32.982	18.441	1.00	52.63	GZ00	C
ATOM	1624	CG2	VAL	C	213	9.583	34.508	19.477	1.00	52.72	GZ00	C
ATOM	1625	N	ASP	C	214	13.757	32.813	20.598	1.00	51.96	GZ00	N
ATOM	1626	CA	ASP	C	214	15.054	32.301	20.199	1.00	43.41	GZ00	C
ATOM	1627	C	ASP	C	214	14.791	31.231	19.160	1.00	52.09	GZ00	C
ATOM	1628	O	ASP	C	214	13.923	30.374	19.356	1.00	60.39	GZ00	O
ATOM	1629	CB	ASP	C	214	15.820	31.717	21.384	1.00	47.17	GZ00	C
ATOM	1630	CG	ASP	C	214	16.093	32.742	22.473	1.00	53.34	GZ00	C
ATOM	1631	OD1	ASP	C	214	16.343	33.921	22.145	1.00	53.82	GZ00	O
ATOM	1632	OD2	ASP	C	214	16.071	32.367	23.665	1.00	64.40	GZ00	O1−
ATOM	1633	N	LYS	C	215	15.527	31.282	18.060	1.00	49.22	GZ00	N
ATOM	1634	CA	LYS	C	215	15.322	30.324	16.993	1.00	46.64	GZ00	C
ATOM	1635	C	LYS	C	215	16.691	29.904	16.489	1.00	51.67	GZ00	C
ATOM	1636	O	LYS	C	215	17.531	30.748	16.165	1.00	50.73	GZ00	O
ATOM	1637	CB	LYS	C	215	14.459	30.916	15.877	1.00	41.93	GZ00	C
ATOM	1638	CG	LYS	C	215	14.213	29.983	14.699	1.00	58.37	GZ00	C
ATOM	1639	CD	LYS	C	215	13.161	28.894	14.993	1.00	57.43	GZ00	C
ATOM	1640	CE	LYS	C	215	11.848	29.473	15.498	1.00	54.91	GZ00	C
ATOM	1641	NZ	LYS	C	215	10.704	28.533	15.296	1.00	59.67	GZ00	N1+
ATOM	1642	N	LYS	C	216	16.916	28.597	16.475	1.00	48.55	GZ00	N
ATOM	1643	CA	LYS	C	216	18.160	28.025	16.004	1.00	44.55	GZ00	C
ATOM	1644	C	LYS	C	216	18.075	27.873	14.498	1.00	51.23	GZ00	C
ATOM	1645	O	LYS	C	216	17.073	27.377	13.973	1.00	48.07	GZ00	O
ATOM	1646	CB	LYS	C	216	18.384	26.667	16.671	1.00	53.16	GZ00	C
ATOM	1647	CG	LYS	C	216	19.666	25.939	16.297	1.00	58.06	GZ00	C
ATOM	1648	CD	LYS	C	216	19.698	24.568	16.972	1.00	68.72	GZ00	C
ATOM	1649	CE	LYS	C	216	21.064	23.901	16.884	1.00	76.90	GZ00	C
ATOM	1650	NZ	LYS	C	216	21.133	22.703	17.775	1.00	81.06	GZ00	N1+
ATOM	1651	N	VAL	C	217	19.122	28.296	13.802	1.00	42.74	GZ00	N
ATOM	1652	CA	VAL	C	217	19.158	28.228	12.355	1.00	45.91	GZ00	C
ATOM	1653	C	VAL	C	217	20.199	27.179	12.003	1.00	52.09	GZ00	C
ATOM	1654	O	VAL	C	217	21.399	27.371	12.243	1.00	50.43	GZ00	O
ATOM	1655	CB	VAL	C	217	19.472	29.594	11.727	1.00	47.85	GZ00	C
ATOM	1656	CG1	VAL	C	217	19.352	29.534	10.217	1.00	36.68	GZ00	C
ATOM	1657	CG2	VAL	C	217	18.552	30.667	12.314	1.00	38.98	GZ00	C
ATOM	1658	N	GLU	C	218	19.742	26.069	11.431	1.00	54.61	GZ00	N
ATOM	1659	CA	GLU	C	218	20.591	24.937	11.107	1.00	54.05	GZ00	C
ATOM	1660	C	GLU	C	218	20.622	24.755	9.603	1.00	49.13	GZ00	C
ATOM	1661	O	GLU	C	218	19.647	25.082	8.922	1.00	58.50	GZ00	O
ATOM	1662	CB	GLU	C	218	20.080	23.637	11.742	1.00	65.26	GZ00	C
ATOM	1663	CG	GLU	C	218	19.944	23.671	13.253	1.00	70.38	GZ00	C
ATOM	1664	CD	GLU	C	218	19.413	22.365	13.822	1.00	84.00	GZ00	C
ATOM	1665	OE1	GLU	C	218	18.889	21.534	13.040	1.00	82.26	GZ00	O
ATOM	1666	OE2	GLU	C	218	19.515	22.180	15.056	1.00	91.02	GZ00	O1−
ATOM	1667	N	PRO	C	219	21.716	24.232	9.056	1.00	57.01	GZ00	N
ATOM	1668	CA	PRO	C	219	21.755	23.952	7.612	1.00	53.03	GZ00	C
ATOM	1669	C	PRO	C	219	20.705	22.941	7.170	1.00	58.97	GZ00	C
ATOM	1670	O	PRO	C	219	19.991	22.384	8.008	1.00	62.86	GZ00	O
ATOM	1671	CB	PRO	C	219	23.185	23.443	7.393	1.00	49.20	GZ00	C
ATOM	1672	CG	PRO	C	219	23.796	23.307	8.761	1.00	47.12	GZ00	C
ATOM	1673	CD	PRO	C	219	23.051	24.186	9.671	1.00	55.30	GZ00	C
ATOM	1674	N	LYS	C	220	20.623	22.700	5.857	1.00	71.75	GZ00	N
ATOM	1675	CA	LYS	C	220	19.610	21.841	5.209	1.00	68.27	GZ00	C
ATOM	1676	C	LYS	C	220	18.226	22.491	5.306	1.00	73.79	GZ00	C
ATOM	1677	O	LYS	C	220	17.355	22.046	6.058	1.00	80.81	GZ00	O
ATOM	1678	CB	LYS	C	220	19.570	20.424	5.812	1.00	60.33	GZ00	C
ATOM	1679	CG	LYS	C	220	18.562	19.498	5.140	1.00	75.19	GZ00	C
ATOM	1680	CD	LYS	C	220	18.194	18.314	6.009	1.00	81.62	GZ00	C
ATOM	1681	CE	LYS	C	220	17.204	17.408	5.284	1.00	83.68	GZ00	C
ATOM	1682	NZ	LYS	C	220	15.922	18.107	4.974	1.00	81.30	GZ00	N1+
TER
ATOM	1683	N	GLN	D	1	3.622	57.068	−14.037	1.00	73.81		N
ATOM	1684	CA	GLN	D	1	2.256	57.519	−13.830	1.00	77.03		C
ATOM	1685	C	GLN	D	1	2.220	58.975	−13.340	1.00	71.19		C
ATOM	1686	O	GLN	D	1	1.170	59.618	−13.403	1.00	70.55		O
ATOM	1687	CB	GLN	D	1	1.535	56.594	−12.844	1.00	76.72		C
ATOM	1688	CG	GLN	D	1	0.016	56.704	−12.856	1.00	83.42		C
ATOM	1689	CD	GLN	D	1	−0.568	56.892	−11.458	1.00	94.69		C
ATOM	1690	OE1	GLN	D	1	0.127	56.720	−10.448	1.00	86.56		O
ATOM	1691	NE2	GLN	D	1	−1.851	57.255	−11.395	1.00	91.59		N
ATOM	1692	N	SER	D	2	3.352	59.504	−12.865	1.00	62.32		N
ATOM	1693	CA	SER	D	2	3.404	60.928	−12.539	1.00	62.06		C
ATOM	1694	C	SER	D	2	3.359	61.752	−13.826	1.00	54.47		C
ATOM	1695	O	SER	D	2	3.840	61.331	−14.885	1.00	54.37		O
ATOM	1696	CB	SER	D	2	4.637	61.269	−11.685	1.00	55.55		C
ATOM	1697	OG	SER	D	2	5.815	61.429	−12.445	1.00	44.68		O
ATOM	1698	N	VAL	D	3	2.765	62.942	−13.725	1.00	51.09		N
ATOM	1699	CA	VAL	D	3	2.399	63.693	−14.926	1.00	44.98		C
ATOM	1700	C	VAL	D	3	3.625	64.277	−15.623	1.00	44.14		C
ATOM	1701	O	VAL	D	3	3.682	64.317	−16.858	1.00	42.24		O
ATOM	1702	CB	VAL	D	3	1.355	64.762	−14.561	1.00	48.49		C
ATOM	1703	CG1	VAL	D	3	1.035	65.656	−15.762	1.00	33.38		C
ATOM	1704	CG2	VAL	D	3	0.095	64.072	−13.994	1.00	36.61		C
ATOM	1705	N	LEU	D	4	4.610	64.757	−14.867	1.00	40.88		N
ATOM	1706	CA	LEU	D	4	5.895	65.115	−15.451	1.00	38.31		C
ATOM	1707	C	LEU	D	4	6.842	63.946	−15.255	1.00	42.46		C
ATOM	1708	O	LEU	D	4	6.841	63.318	−14.195	1.00	41.68		O
ATOM	1709	CB	LEU	D	4	6.484	66.365	−14.808	1.00	36.49		C
ATOM	1710	CG	LEU	D	4	5.476	67.494	−14.624	1.00	34.13		C
ATOM	1711	CD1	LEU	D	4	6.074	68.656	−13.825	1.00	34.44		C
ATOM	1712	CD2	LEU	D	4	4.978	67.953	−15.972	1.00	29.23		C
ATOM	1713	N	THR	D	5	7.637	63.640	−16.273	1.00	39.33		N
ATOM	1714	CA	THR	D	5	8.541	62.503	−16.203	1.00	34.69		C
ATOM	1715	C	THR	D	5	9.987	62.990	−16.144	1.00	41.85		C
ATOM	1716	O	THR	D	5	10.420	63.814	−16.959	1.00	32.54		O
ATOM	1717	CB	THR	D	5	8.307	61.529	−17.363	1.00	40.41		C
ATOM	1718	OG1	THR	D	5	8.542	62.190	−18.596	1.00	58.56		O
ATOM	1719	CG2	THR	D	5	6.858	61.060	−17.366	1.00	35.80		C
ATOM	1720	N	GLN	D	6	10.703	62.522	−15.132	1.00	33.22		N
ATOM	1721	CA	GLN	D	6	12.100	62.739	−14.872	1.00	31.46		C
ATOM	1722	C	GLN	D	6	12.802	61.390	−14.902	1.00	35.85		C
ATOM	1723	O	GLN	D	6	12.187	60.381	−14.554	1.00	35.36		O
ATOM	1724	CB	GLN	D	6	12.302	63.370	−13.490	1.00	31.54		C
ATOM	1725	CG	GLN	D	6	11.670	64.731	−13.302	1.00	32.96		C
ATOM	1726	CD	GLN	D	6	11.827	65.238	−11.884	1.00	38.63		C
ATOM	1727	OE1	GLN	D	6	10.841	65.645	−11.248	1.00	36.32		O
ATOM	1728	NE2	GLN	D	6	13.073	65.220	−11.367	1.00	31.40		N
ATOM	1729	N	PRO	D	7	14.069	61.323	−15.306	1.00	39.24		N
ATOM	1730	CA	PRO	D	7	14.832	60.087	−15.078	1.00	33.07		C
ATOM	1731	C	PRO	D	7	14.881	59.791	−13.588	1.00	34.60		C
ATOM	1732	O	PRO	D	7	15.015	60.714	−12.764	1.00	32.93		O
ATOM	1733	CB	PRO	D	7	16.235	60.402	−15.652	1.00	31.22		C
ATOM	1734	CG	PRO	D	7	16.356	61.910	−15.589	1.00	34.93		C
ATOM	1735	CD	PRO	D	7	14.921	62.430	−15.806	1.00	35.72		C
ATOM	1736	N	PRO	D	8	14.755	58.518	−13.197	1.00	33.41		N
ATOM	1737	CA	PRO	D	8	14.682	58.200	−11.756	1.00	33.71		C
ATOM	1738	C	PRO	D	8	15.987	58.443	−11.027	1.00	36.29		C
ATOM	1739	O	PRO	D	8	15.966	58.847	−9.855	1.00	35.95		O
ATOM	1740	CB	PRO	D	8	14.299	56.705	−11.730	1.00	31.63		C
ATOM	1741	CG	PRO	D	8	14.777	56.181	−13.032	1.00	33.24		C
ATOM	1742	CD	PRO	D	8	14.568	57.333	−14.040	1.00	28.70		C
ATOM	1743	N	SER	D	9	17.128	58.252	−11.679	1.00	31.20		N
ATOM	1744	CA	SER	D	9	18.367	58.463	−10.945	1.00	41.37		C
ATOM	1745	C	SER	D	9	19.485	58.910	−11.869	1.00	41.68		C
ATOM	1746	O	SER	D	9	19.492	58.642	−13.075	1.00	39.62		O
ATOM	1747	CB	SER	D	9	18.788	57.197	−10.195	1.00	32.55		C
ATOM	1748	OG	SER	D	9	18.984	56.168	−11.129	1.00	46.27		O
ATOM	1749	N	VAL	D	10	20.465	59.553	−11.259	1.00	35.48		N
ATOM	1750	CA	VAL	D	10	21.529	60.199	−12.000	1.00	37.87		C
ATOM	1751	C	VAL	D	10	22.736	60.253	−11.082	1.00	34.78		C
ATOM	1752	O	VAL	D	10	22.605	60.523	−9.880	1.00	36.71		O
ATOM	1753	CB	VAL	D	10	21.041	61.588	−12.472	1.00	40.73		C
ATOM	1754	CG1	VAL	D	10	21.926	62.691	−11.971	1.00	40.07		C
ATOM	1755	CG2	VAL	D	10	20.845	61.613	−13.973	1.00	38.95		C
ATOM	1756	N	SER	D	11	23.915	59.963	−11.625	1.00	37.46		N
ATOM	1757	CA	SER	D	11	25.092	59.962	−10.762	1.00	35.14		C
ATOM	1758	C	SER	D	11	26.324	60.390	−11.542	1.00	31.82		C
ATOM	1759	O	SER	D	11	26.474	60.057	−12.715	1.00	37.48		O
ATOM	1760	CB	SER	D	11	25.311	58.580	−10.130	1.00	33.24		C
ATOM	1761	OG	SER	D	11	25.640	57.636	−11.125	1.00	37.23		O
ATOM	1762	N	ALA	D	12	27.196	61.139	−10.877	1.00	35.26		N
ATOM	1763	CA	ALA	D	12	28.433	61.620	−11.469	1.00	34.57		C
ATOM	1764	C	ALA	D	12	29.379	61.996	−10.338	1.00	39.68		C
ATOM	1765	O	ALA	D	12	28.955	62.218	−9.199	1.00	31.45		O
ATOM	1766	CB	ALA	D	12	28.200	62.814	−12.409	1.00	31.29		C
ATOM	1767	N	ALA	D	13	30.673	62.071	−10.679	1.00	36.93		N
ATOM	1768	CA	ALA	D	13	31.748	62.366	−9.733	1.00	40.49		C
ATOM	1769	C	ALA	D	13	31.847	63.860	−9.433	1.00	40.25		C
ATOM	1770	O	ALA	D	13	31.411	64.695	−10.236	1.00	39.24		O
ATOM	1771	CB	ALA	D	13	33.081	61.875	−10.291	1.00	30.80		C
ATOM	1772	N	PRO	D	14	32.434	64.225	−8.288	1.00	33.52		N
ATOM	1773	CA	PRO	D	14	32.647	65.646	−7.994	1.00	38.76		C
ATOM	1774	C	PRO	D	14	33.382	66.324	−9.141	1.00	44.78		C
ATOM	1775	O	PRO	D	14	34.233	65.718	−9.798	1.00	36.43		O
ATOM	1776	CB	PRO	D	14	33.485	65.629	−6.711	1.00	35.31		C
ATOM	1777	CG	PRO	D	14	33.152	64.283	−6.060	1.00	30.30		C
ATOM	1778	CD	PRO	D	14	32.928	63.345	−7.208	1.00	32.96		C
ATOM	1779	N	GLY	D	15	33.008	67.579	−9.410	1.00	45.92		N
ATOM	1780	CA	GLY	D	15	33.585	68.342	−10.484	1.00	34.84		C
ATOM	1781	C	GLY	D	15	32.932	68.138	−11.829	1.00	41.92		C
ATOM	1782	O	GLY	D	15	33.143	68.956	−12.728	1.00	49.13		O
ATOM	1783	N	GLN	D	16	32.143	67.083	−12.001	1.00	37.37		N
ATOM	1784	CA	GLN	D	16	31.533	66.844	−13.302	1.00	48.89		C
ATOM	1785	C	GLN	D	16	30.220	67.627	−13.500	1.00	47.03		C
ATOM	1786	O	GLN	D	16	29.744	68.367	−12.628	1.00	39.51		O
ATOM	1787	CB	GLN	D	16	31.306	65.355	−13.502	1.00	50.09		C
ATOM	1788	CG	GLN	D	16	32.570	64.589	−13.809	1.00	57.03		C
ATOM	1789	CD	GLN	D	16	32.260	63.311	−14.566	1.00	75.65		C
ATOM	1790	OE1	GLN	D	16	31.830	62.302	−13.979	1.00	62.08		O
ATOM	1791	NE2	GLN	D	16	32.445	63.353	−15.886	1.00	86.71		N
ATOM	1792	N	LYS	D	17	29.674	67.481	−14.711	1.00	50.37		N
ATOM	1793	CA	LYS	D	17	28.424	68.054	−15.189	1.00	47.34		C
ATOM	1794	C	LYS	D	17	27.325	67.004	−15.183	1.00	51.01		C
ATOM	1795	O	LYS	D	17	27.566	65.822	−15.440	1.00	57.21		O
ATOM	1796	CB	LYS	D	17	28.537	68.558	−16.635	1.00	48.76		C
ATOM	1797	CG	LYS	D	17	29.325	69.812	−16.889	1.00	66.24		C
ATOM	1798	CD	LYS	D	17	29.537	69.967	−18.408	1.00	76.78		C
ATOM	1799	CE	LYS	D	17	30.502	71.109	−18.742	1.00	85.45		C
ATOM	1800	NZ	LYS	D	17	30.739	71.204	−20.209	1.00	85.79		N
ATOM	1801	N	AVAL	D	18	26.098	67.456	−14.947	0.60	46.54		N
ATOM	1802	CA	AVAL	D	18	24.936	66.572	−14.935	0.60	45.04		C
ATOM	1803	C	AVAL	D	18	23.728	67.369	−15.412	0.60	42.17		C
ATOM	1804	O	AVAL	D	18	23.622	68.572	−15.150	0.60	42.21		O
ATOM	1805	CB	AVAL	D	18	24.745	65.964	−13.527	0.60	43.33		C
ATOM	1806	CG1	AVAL	D	18	23.328	66.101	−13.049	0.60	41.29		C
ATOM	1807	CG2	AVAL	D	18	25.187	64.524	−13.516	0.60	41.57		C
ATOM	1808	N	BVAL	D	18	26.101	67.445	−14.920	0.40	46.52		N
ATOM	1809	CA	BVAL	D	18	24.961	66.551	−15.030	0.40	45.04		C
ATOM	1810	C	BVAL	D	18	23.744	67.363	−15.441	0.40	42.19		C
ATOM	1811	O	BVAL	D	18	23.643	68.561	−15.158	0.40	42.16		O
ATOM	1812	CB	BVAL	D	18	24.729	65.769	−13.718	0.40	43.17		C
ATOM	1813	CG1	BVAL	D	18	24.057	66.644	−12.663	0.40	39.96		C
ATOM	1814	CG2	BVAL	D	18	23.942	64.530	−14.005	0.40	42.54		C
ATOM	1815	N	THR	D	19	22.831	66.698	−16.143	1.00	46.67		N
ATOM	1816	CA	THR	D	19	21.594	67.285	−16.650	1.00	42.21		C
ATOM	1817	C	THR	D	19	20.412	66.449	−16.178	1.00	42.60		C
ATOM	1818	O	THR	D	19	20.469	65.212	−16.217	1.00	40.66		O
ATOM	1819	CB	THR	D	19	21.646	67.356	−18.189	1.00	36.82		C
ATOM	1820	OG1	THR	D	19	21.854	68.714	−18.572	1.00	49.09		O
ATOM	1821	CG2	THR	D	19	20.396	66.796	−18.859	1.00	40.02		C
ATOM	1822	N	ILE	D	20	19.343	67.117	−15.733	1.00	35.88		N
ATOM	1823	CA	ILE	D	20	18.132	66.439	−15.267	1.00	33.46		C
ATOM	1824	C	ILE	D	20	16.954	66.997	−16.042	1.00	38.36		C
ATOM	1825	O	ILE	D	20	16.680	68.200	−15.976	1.00	36.03		O
ATOM	1826	CB	ILE	D	20	17.907	66.602	−13.753	1.00	38.27		C
ATOM	1827	CG1	ILE	D	20	19.043	65.927	−12.976	1.00	32.31		C
ATOM	1828	CG2	ILE	D	20	16.555	65.993	−13.341	1.00	34.30		C
ATOM	1829	CD1	ILE	D	20	19.010	66.199	−11.490	1.00	28.88		C
ATOM	1830	N	SER	D	21	16.253	66.127	−16.764	1.00	31.98		N
ATOM	1831	CA	SER	D	21	15.188	66.575	−17.643	1.00	36.18		C
ATOM	1832	C	SER	D	21	13.814	66.346	−17.011	1.00	40.44		C
ATOM	1833	O	SER	D	21	13.639	65.541	−16.094	1.00	35.10		O
ATOM	1834	CB	SER	D	21	15.267	65.862	−18.988	1.00	35.20		C
ATOM	1835	OG	SER	D	21	15.097	64.461	−18.840	1.00	43.09		O
ATOM	1836	N	CYS	D	22	12.829	67.052	−17.552	1.00	32.32		N
ATOM	1837	CA	CYS	D	22	11.476	67.044	−17.012	1.00	36.57		C
ATOM	1838	C	CYS	D	22	10.549	67.317	−18.192	1.00	36.72		C
ATOM	1839	O	CYS	D	22	10.444	68.454	−18.656	1.00	33.99		O
ATOM	1840	CB	CYS	D	22	11.339	68.103	−15.933	1.00	34.58		C
ATOM	1841	SG	CYS	D	22	9.650	68.451	−15.371	1.00	54.36		S
ATOM	1842	N	SER	D	23	9.915	66.282	−18.703	1.00	34.27		N
ATOM	1843	CA	SER	D	23	9.059	66.460	−19.859	1.00	42.72		C
ATOM	1844	C	SER	D	23	7.582	66.345	−19.454	1.00	41.50		C
ATOM	1845	O	SER	D	23	7.209	65.545	−18.582	1.00	29.92		O
ATOM	1846	CB	SER	D	23	9.450	65.476	−20.954	1.00	34.92		C
ATOM	1847	OG	SER	D	23	8.893	64.230	−20.677	1.00	50.39		O
ATOM	1848	N	GLY	D	24	6.765	67.218	−20.037	1.00	36.33		N
ATOM	1849	CA	GLY	D	24	5.336	67.237	−19.809	1.00	38.73		C
ATOM	1850	C	GLY	D	24	4.600	67.510	−21.103	1.00	39.14		C
ATOM	1851	O	GLY	D	24	4.942	66.945	−22.139	1.00	42.42		O
ATOM	1852	N	SER	D	25	3.620	68.406	−21.078	1.00	36.67		N
ATOM	1853	CA	SER	D	25	2.743	68.598	−22.221	1.00	39.25		C
ATOM	1854	C	SER	D	25	2.382	70.072	−22.346	1.00	38.01		C
ATOM	1855	O	SER	D	25	2.754	70.902	−21.506	1.00	33.82		O
ATOM	1856	CB	SER	D	25	1.496	67.732	−22.067	1.00	41.16		C
ATOM	1857	OG	SER	D	25	0.709	68.227	−20.994	1.00	50.29		O
ATOM	1858	N	SER	D	26	1.657	70.404	−23.420	1.00	31.89		N
ATOM	1859	CA	SER	D	26	1.329	71.809	−23.656	1.00	36.67		C
ATOM	1860	C	SER	D	26	0.486	72.395	−22.527	1.00	38.14		C
ATOM	1861	O	SER	D	26	0.548	73.600	−22.271	1.00	38.11		O
ATOM	1862	CB	SER	D	26	0.624	71.976	−25.002	1.00	31.63		C
ATOM	1863	OG	SER	D	26	−0.356	70.980	−25.146	1.00	53.99		O
ATOM	1864	N	SER	D	27	−0.279	71.575	−21.818	1.00	33.81		N
ATOM	1865	CA	SER	D	27	−1.109	72.150	−20.773	1.00	37.80		C
ATOM	1866	C	SER	D	27	−0.387	72.281	−19.431	1.00	40.08		C
ATOM	1867	O	SER	D	27	−0.954	72.862	−18.498	1.00	36.37		O
ATOM	1868	CB	SER	D	27	−2.393	71.336	−20.608	1.00	31.40		C
ATOM	1869	OG	SER	D	27	−2.088	70.014	−20.236	1.00	50.96		O
ATOM	1870	N	ASN	D	28	0.839	71.765	−19.295	1.00	34.89		N
ATOM	1871	CA	ASN	D	28	1.555	72.073	−18.068	1.00	33.57		C
ATOM	1872	C	ASN	D	28	2.831	72.854	−18.389	1.00	34.78		C
ATOM	1873	O	ASN	D	28	2.800	74.091	−18.405	1.00	36.75		O
ATOM	1874	CB	ASN	D	28	1.817	70.808	−17.214	1.00	34.30		C
ATOM	1875	CG	ASN	D	28	2.277	69.580	−18.027	1.00	34.72		C
ATOM	1876	OD1	ASN	D	28	3.345	69.568	−18.641	1.00	33.73		O
ATOM	1877	ND2	ASN	D	28	1.500	68.515	−17.949	1.00	35.11		N
ATOM	1878	N	ILE	D	29	3.952	72.171	−18.633	1.00	33.54		N
ATOM	1879	CA	ILE	D	29	5.218	72.866	−18.877	1.00	34.11		C
ATOM	1880	C	ILE	D	29	5.107	73.810	−20.072	1.00	36.11		C
ATOM	1881	O	ILE	D	29	5.691	74.897	−20.082	1.00	33.26		O
ATOM	1882	CB	ILE	D	29	6.350	71.840	−19.063	1.00	33.30		C
ATOM	1883	CG1	ILE	D	29	6.604	71.107	−17.741	1.00	32.39		C
ATOM	1884	CG2	ILE	D	29	7.621	72.520	−19.555	1.00	25.88		C
ATOM	1885	CD1	ILE	D	29	7.724	70.138	−17.806	1.00	36.95		C
ATOM	1886	N	GLY	D	30	4.368	73.412	−21.103	1.00	38.51		N
ATOM	1887	CA	GLY	D	30	4.274	74.237	−22.289	1.00	30.45		C
ATOM	1888	C	GLY	D	30	3.608	75.580	−22.062	1.00	38.50		C
ATOM	1889	O	GLY	D	30	3.763	76.475	−22.889	1.00	40.64		O
ATOM	1890	N	ASN	D	31	2.836	75.744	−20.987	1.00	37.18		N
ATOM	1891	CA	ASN	D	31	2.178	77.031	−20.815	1.00	37.16		C
ATOM	1892	C	ASN	D	31	2.192	77.595	−19.395	1.00	36.18		C
ATOM	1893	O	ASN	D	31	1.488	78.576	−19.137	1.00	42.11		O
ATOM	1894	CB	ASN	D	31	0.731	76.942	−21.340	1.00	41.60		C
ATOM	1895	CG	ASN	D	31	0.681	77.025	−22.867	1.00	53.09		C
ATOM	1896	OD1	ASN	D	31	0.759	78.110	−23.442	1.00	63.01		O
ATOM	1897	ND2	ASN	D	31	0.591	75.877	−23.525	1.00	45.20		N
ATOM	1898	N	ASN	D	32	2.985	77.059	−18.471	1.00	38.29		N
ATOM	1899	CA	ASN	D	32	3.026	77.622	−17.128	1.00	35.50		C
ATOM	1900	C	ASN	D	32	4.467	77.757	−16.662	1.00	33.99		C
ATOM	1901	O	ASN	D	32	5.394	77.247	−17.291	1.00	37.19		O
ATOM	1902	CB	ASN	D	32	2.192	76.787	−16.158	1.00	29.83		C
ATOM	1903	CG	ASN	D	32	0.731	76.754	−16.548	1.00	35.04		C
ATOM	1904	OD1	ASN	D	32	0.003	77.720	−16.321	1.00	41.43		O
ATOM	1905	ND2	ASN	D	32	0.299	75.657	−17.166	1.00	38.66		N
ATOM	1906	N	TYR	D	33	4.647	78.497	−15.572	1.00	30.88		N
ATOM	1907	CA	TYR	D	33	5.973	78.725	−15.020	1.00	31.61		C
ATOM	1908	C	TYR	D	33	6.529	77.443	−14.422	1.00	39.01		C
ATOM	1909	O	TYR	D	33	5.815	76.704	−13.751	1.00	35.01		O
ATOM	1910	CB	TYR	D	33	5.925	79.804	−13.951	1.00	27.05		C
ATOM	1911	CG	TYR	D	33	5.492	81.136	−14.476	1.00	32.55		C
ATOM	1912	CD1	TYR	D	33	6.214	81.780	−15.478	1.00	29.14		C
ATOM	1913	CD2	TYR	D	33	4.358	81.770	−13.965	1.00	38.90		C
ATOM	1914	CE1	TYR	D	33	5.805	83.036	−15.967	1.00	36.47		C
ATOM	1915	CE2	TYR	D	33	3.948	83.013	−14.438	1.00	33.42		C
ATOM	1916	CZ	TYR	D	33	4.671	83.642	−15.438	1.00	37.47		C
ATOM	1917	OH	TYR	D	33	4.246	84.866	−15.903	1.00	36.22		O
ATOM	1918	N	VAL	D	34	7.821	77.195	−14.623	1.00	33.97		N
ATOM	1919	CA	VAL	D	34	8.440	75.966	−14.138	1.00	32.04		C
ATOM	1920	C	VAL	D	34	9.272	76.250	−12.896	1.00	31.06		C
ATOM	1921	O	VAL	D	34	9.986	77.254	−12.832	1.00	32.29		O
ATOM	1922	CB	VAL	D	34	9.292	75.308	−15.236	1.00	33.98		C
ATOM	1923	CG1	VAL	D	34	10.002	74.100	−14.684	1.00	30.92		C
ATOM	1924	CG2	VAL	D	34	8.407	74.884	−16.397	1.00	34.56		C
ATOM	1925	N	SER	D	35	9.166	75.373	−11.896	1.00	31.29		N
ATOM	1926	CA	SER	D	35	9.991	75.425	−10.697	1.00	30.60		C
ATOM	1927	C	SER	D	35	10.791	74.134	−10.560	1.00	35.34		C
ATOM	1928	O	SER	D	35	10.367	73.068	−11.017	1.00	31.50		O
ATOM	1929	CB	SER	D	35	9.166	75.614	−9.423	1.00	26.83		C
ATOM	1930	OG	SER	D	35	8.548	76.889	−9.407	1.00	31.37		O
ATOM	1931	N	TRP	D	36	11.967	74.248	−9.938	1.00	31.19		N
ATOM	1932	CA	TRP	D	36	12.774	73.104	−9.559	1.00	30.26		C
ATOM	1933	C	TRP	D	36	12.996	73.142	−8.060	1.00	29.04		C
ATOM	1934	O	TRP	D	36	13.286	74.196	−7.491	1.00	29.53		O
ATOM	1935	CB	TRP	D	36	14.112	73.084	−10.274	1.00	25.90		C
ATOM	1936	CG	TRP	D	36	14.009	72.705	−11.713	1.00	32.87		C
ATOM	1937	CD1	TRP	D	36	13.867	73.552	−12.773	1.00	33.05		C
ATOM	1938	CD2	TRP	D	36	14.049	71.383	−12.259	1.00	32.92		C
ATOM	1939	NE1	TRP	D	36	13.812	72.835	−13.947	1.00	33.23		N
ATOM	1940	CE2	TRP	D	36	13.941	71.505	−13.660	1.00	29.67		C
ATOM	1941	CE3	TRP	D	36	14.187	70.108	−11.701	1.00	32.52		C
ATOM	1942	CZ2	TRP	D	36	13.946	70.401	−14.512	1.00	32.64		C
ATOM	1943	CZ3	TRP	D	36	14.185	69.012	−12.546	1.00	30.06		C
ATOM	1944	CH2	TRP	D	36	14.058	69.166	−13.936	1.00	35.04		C
ATOM	1945	N	TYR	D	37	12.874	71.982	−7.429	1.00	31.89		N
ATOM	1946	CA	TYR	D	37	13.051	71.848	−5.995	1.00	29.68		C
ATOM	1947	C	TYR	D	37	14.168	70.859	−5.693	1.00	36.72		C
ATOM	1948	O	TYR	D	37	14.324	69.839	−6.383	1.00	33.31		O
ATOM	1949	CB	TYR	D	37	11.735	71.417	−5.343	1.00	28.40		C
ATOM	1950	CG	TYR	D	37	10.598	72.378	−5.659	1.00	30.46		C
ATOM	1951	CD1	TYR	D	37	10.417	73.540	−4.921	1.00	27.52		C
ATOM	1952	CD2	TYR	D	37	9.723	72.130	−6.719	1.00	29.85		C
ATOM	1953	CE1	TYR	D	37	9.368	74.423	−5.219	1.00	32.37		C
ATOM	1954	CE2	TYR	D	37	8.691	72.993	−7.019	1.00	27.34		C
ATOM	1955	CZ	TYR	D	37	8.517	74.137	−6.271	1.00	30.55		C
ATOM	1956	OH	TYR	D	37	7.495	74.995	−6.595	1.00	35.11		O
ATOM	1957	N	GLN	D	38	14.938	71.174	−4.653	1.00	32.56		N
ATOM	1958	CA	GLN	D	38	16.019	70.332	−4.174	1.00	30.13		C
ATOM	1959	C	GLN	D	38	15.690	69.837	−2.770	1.00	33.68		C
ATOM	1960	O	GLN	D	38	15.362	70.635	−1.880	1.00	31.93		O
ATOM	1961	CB	GLN	D	38	17.349	71.102	−4.170	1.00	30.01		C
ATOM	1962	CG	GLN	D	38	18.527	70.323	−3.564	1.00	28.04		C
ATOM	1963	CD	GLN	D	38	19.729	71.214	−3.280	1.00	34.96		C
ATOM	1964	OE1	GLN	D	38	19.664	72.147	−2.473	1.00	32.51		O
ATOM	1965	NE2	GLN	D	38	20.828	70.944	−3.971	1.00	33.81		N
ATOM	1966	N	GLN	D	39	15.790	68.528	−2.572	1.00	32.31		N
ATOM	1967	CA	GLN	D	39	15.552	67.918	−1.266	1.00	38.47		C
ATOM	1968	C	GLN	D	39	16.805	67.162	−0.843	1.00	33.22		C
ATOM	1969	O	GLN	D	39	17.057	66.051	−1.324	1.00	33.95		O
ATOM	1970	CB	GLN	D	39	14.336	67.001	−1.294	1.00	32.82		C
ATOM	1971	CG	GLN	D	39	13.941	66.543	0.090	1.00	38.29		C
ATOM	1972	CD	GLN	D	39	12.621	65.809	0.118	1.00	34.34		C
ATOM	1973	OE1	GLN	D	39	12.221	65.165	−0.862	1.00	38.36		O
ATOM	1974	NE2	GLN	D	39	11.909	65.942	1.236	1.00	30.94		N
ATOM	1975	N	LEU	D	40	17.612	67.779	0.023	1.00	37.41		N
ATOM	1976	CA	LEU	D	40	18.766	67.069	0.571	1.00	41.50		C
ATOM	1977	C	LEU	D	40	18.281	65.913	1.450	1.00	44.75		C
ATOM	1978	O	LEU	D	40	17.202	65.988	2.051	1.00	39.49		O
ATOM	1979	CB	LEU	D	40	19.659	68.020	1.368	1.00	41.85		C
ATOM	1980	CG	LEU	D	40	20.144	69.262	0.592	1.00	42.10		C
ATOM	1981	CD1	LEU	D	40	20.614	70.363	1.515	1.00	38.12		C
ATOM	1982	CD2	LEU	D	40	21.236	68.903	−0.380	1.00	31.04		C
ATOM	1983	N	PRO	D	41	19.045	64.827	1.520	1.00	47.88		N
ATOM	1984	CA	PRO	D	41	18.568	63.625	2.225	1.00	42.38		C
ATOM	1985	C	PRO	D	41	18.152	63.935	3.656	1.00	45.34		C
ATOM	1986	O	PRO	D	41	18.876	64.603	4.404	1.00	46.53		O
ATOM	1987	CB	PRO	D	41	19.780	62.691	2.182	1.00	43.44		C
ATOM	1988	CG	PRO	D	41	20.639	63.217	1.062	1.00	46.87		C
ATOM	1989	CD	PRO	D	41	20.427	64.690	1.030	1.00	42.00		C
ATOM	1990	N	GLY	D	42	16.963	63.459	4.029	1.00	38.47		N
ATOM	1991	CA	GLY	D	42	16.400	63.729	5.346	1.00	39.47		C
ATOM	1992	C	GLY	D	42	15.980	65.164	5.648	1.00	51.21		C
ATOM	1993	O	GLY	D	42	15.801	65.501	6.822	1.00	48.36		O
ATOM	1994	N	THR	D	43	15.793	66.022	4.642	1.00	44.85		N
ATOM	1995	CA	THR	D	43	15.393	67.415	4.867	1.00	47.53		C
ATOM	1996	C	THR	D	43	14.123	67.747	4.090	1.00	39.84		C
ATOM	1997	O	THR	D	43	13.599	66.944	3.315	1.00	42.92		O
ATOM	1998	CB	THR	D	43	16.503	68.414	4.475	1.00	45.75		C
ATOM	1999	OG1	THR	D	43	16.602	68.488	3.045	1.00	36.10		O
ATOM	2000	CG2	THR	D	43	17.857	67.992	5.056	1.00	41.52		C
ATOM	2001	N	ALA	D	44	13.619	68.952	4.318	1.00	38.36		N
ATOM	2002	CA	ALA	D	44	12.484	69.426	3.553	1.00	38.31		C
ATOM	2003	C	ALA	D	44	12.916	69.799	2.137	1.00	39.83		C
ATOM	2004	O	ALA	D	44	14.100	70.032	1.878	1.00	37.35		O
ATOM	2005	CB	ALA	D	44	11.849	70.632	4.238	1.00	38.73		C
ATOM	2006	N	PRO	D	45	11.977	69.838	1.194	1.00	36.33		N
ATOM	2007	CA	PRO	D	45	12.277	70.462	−0.097	1.00	35.97		C
ATOM	2008	C	PRO	D	45	12.678	71.911	0.121	1.00	33.44		C
ATOM	2009	O	PRO	D	45	12.384	72.519	1.155	1.00	33.83		O
ATOM	2010	CB	PRO	D	45	10.948	70.365	−0.872	1.00	28.82		C
ATOM	2011	CG	PRO	D	45	10.265	69.198	−0.245	1.00	36.55		C
ATOM	2012	CD	PRO	D	45	10.615	69.281	1.225	1.00	34.97		C
ATOM	2013	N	LYS	D	46	13.362	72.460	−0.880	1.00	39.06		N
ATOM	2014	CA	LYS	D	46	13.782	73.855	−0.903	1.00	35.89		C
ATOM	2015	C	LYS	D	46	13.682	74.312	−2.350	1.00	36.30		C
ATOM	2016	O	LYS	D	46	13.953	73.521	−3.262	1.00	37.16		O
ATOM	2017	CB	LYS	D	46	15.212	73.986	−0.348	1.00	36.94		C
ATOM	2018	CG	LYS	D	46	15.919	75.292	−0.569	1.00	43.26		C
ATOM	2019	CD	LYS	D	46	17.430	75.058	−0.548	1.00	46.21		C
ATOM	2020	CE	LYS	D	46	18.178	76.121	0.262	1.00	53.10		C
ATOM	2021	NZ	LYS	D	46	19.663	75.960	0.110	1.00	59.22		N1+
ATOM	2022	N	LEU	D	47	13.270	75.565	−2.569	1.00	31.33		N
ATOM	2023	CA	LEU	D	47	13.200	76.086	−3.931	1.00	31.83		C
ATOM	2024	C	LEU	D	47	14.601	76.299	−4.513	1.00	35.29		C
ATOM	2025	O	LEU	D	47	15.454	76.963	−3.911	1.00	33.02		O
ATOM	2026	CB	LEU	D	47	12.417	77.388	−3.962	1.00	26.35		C
ATOM	2027	CG	LEU	D	47	12.230	78.066	−5.326	1.00	35.90		C
ATOM	2028	CD1	LEU	D	47	11.484	77.183	−6.337	1.00	30.55		C
ATOM	2029	CD2	LEU	D	47	11.508	79.411	−5.153	1.00	30.96		C
ATOM	2030	N	LEU	D	48	14.837	75.725	−5.687	1.00	34.87		N
ATOM	2031	CA	LEU	D	48	16.123	75.799	−6.374	1.00	37.46		C
ATOM	2032	C	LEU	D	48	16.107	76.811	−7.513	1.00	33.53		C
ATOM	2033	O	LEU	D	48	17.043	77.600	−7.660	1.00	38.96		O
ATOM	2034	CB	LEU	D	48	16.516	74.416	−6.926	1.00	27.18		C
ATOM	2035	CG	LEU	D	48	17.944	74.289	−7.452	1.00	28.56		C
ATOM	2036	CD1	LEU	D	48	18.892	74.353	−6.289	1.00	32.28		C
ATOM	2037	CD2	LEU	D	48	18.153	72.987	−8.196	1.00	32.35		C
ATOM	2038	N	LEU	D	49	15.063	76.766	−8.334	1.00	29.89		N
ATOM	2039	CA	LEU	D	49	14.871	77.609	−9.500	1.00	31.38		C
ATOM	2040	C	LEU	D	49	13.383	77.885	−9.629	1.00	35.27		C
ATOM	2041	O	LEU	D	49	12.563	76.964	−9.504	1.00	32.72		O
ATOM	2042	CB	LEU	D	49	15.360	76.932	−10.789	1.00	28.28		C
ATOM	2043	CG	LEU	D	49	16.848	76.621	−10.937	1.00	40.25		C
ATOM	2044	CD1	LEU	D	49	17.100	75.739	−12.173	1.00	34.47		C
ATOM	2045	CD2	LEU	D	49	17.642	77.943	−10.996	1.00	32.52		C
ATOM	2046	N	TYR	D	50	13.031	79.136	−9.909	1.00	28.76		N
ATOM	2047	CA	TYR	D	50	11.656	79.423	−10.287	1.00	31.24		C
ATOM	2048	C	TYR	D	50	11.659	80.149	−11.622	1.00	31.13		C
ATOM	2049	O	TYR	D	50	12.697	80.634	−12.077	1.00	32.85		O
ATOM	2050	CB	TYR	D	50	10.923	80.211	−9.196	1.00	30.09		C
ATOM	2051	CG	TYR	D	50	11.519	81.554	−8.869	1.00	27.45		C
ATOM	2052	CD1	TYR	D	50	12.726	81.672	−8.163	1.00	31.73		C
ATOM	2053	CD2	TYR	D	50	10.859	82.708	−9.238	1.00	29.79		C
ATOM	2054	CE1	TYR	D	50	13.253	82.920	−7.843	1.00	34.25		C
ATOM	2055	CE2	TYR	D	50	11.366	83.964	−8.921	1.00	36.09		C
ATOM	2056	CZ	TYR	D	50	12.546	84.072	−8.229	1.00	36.80		C
ATOM	2057	OH	TYR	D	50	12.995	85.340	−7.954	1.00	34.65		O
ATOM	2058	N	ASP	D	51	10.487	80.198	−12.260	1.00	33.46		N
ATOM	2059	CA	ASP	D	51	10.371	80.678	−13.638	1.00	34.13		C
ATOM	2060	C	ASP	D	51	11.474	80.078	−14.517	1.00	35.70		C
ATOM	2061	O	ASP	D	51	12.269	80.788	−15.139	1.00	32.50		O
ATOM	2062	CB	ASP	D	51	10.410	82.199	−13.683	1.00	33.19		C
ATOM	2063	CG	ASP	D	51	10.091	82.738	−15.053	1.00	36.53		C
ATOM	2064	OD1	ASP	D	51	9.413	82.007	−15.813	1.00	37.05		O
ATOM	2065	OD2	ASP	D	51	10.507	83.882	−15.361	1.00	36.34		O1−
ATOM	2066	N	SER	D	52	11.565	78.745	−14.494	1.00	35.41		N
ATOM	2067	CA	SER	D	52	12.525	77.980	−15.295	1.00	35.10		C
ATOM	2068	C	SER	D	52	13.986	78.153	−14.884	1.00	34.26		C
ATOM	2069	O	SER	D	52	14.730	77.167	−14.836	1.00	34.09		O
ATOM	2070	CB	SER	D	52	12.393	78.333	−16.779	1.00	29.40		C
ATOM	2071	OG	SER	D	52	11.152	77.892	−17.275	1.00	42.15		O
ATOM	2072	N	ASN	D	53	14.437	79.386	−14.628	1.00	32.85		N
ATOM	2073	CA	ASN	D	53	15.878	79.558	−14.463	1.00	32.56		C
ATOM	2074	C	ASN	D	53	16.290	80.660	−13.495	1.00	34.70		C
ATOM	2075	O	ASN	D	53	17.467	81.027	−13.485	1.00	34.38		O
ATOM	2076	CB	ASN	D	53	16.536	79.814	−15.804	1.00	29.46		C
ATOM	2077	CG	ASN	D	53	16.066	81.113	−16.443	1.00	40.20		C
ATOM	2078	OD1	ASN	D	53	15.192	81.817	−15.918	1.00	32.59		O
ATOM	2079	ND2	ASN	D	53	16.652	81.440	−17.583	1.00	37.64		N
ATOM	2080	N	LYS	D	54	15.391	81.191	−12.677	1.00	36.81		N
ATOM	2081	CA	LYS	D	54	15.761	82.209	−11.713	1.00	29.79		C
ATOM	2082	C	LYS	D	54	16.163	81.540	−10.408	1.00	35.07		C
ATOM	2083	O	LYS	D	54	15.433	80.686	−9.887	1.00	34.40		O
ATOM	2084	CB	LYS	D	54	14.601	83.166	−11.469	1.00	34.19		C
ATOM	2085	CG	LYS	D	54	14.979	84.334	−10.607	1.00	39.09		C
ATOM	2086	CD	LYS	D	54	15.984	85.215	−11.319	1.00	36.81		C
ATOM	2087	CE	LYS	D	54	16.480	86.282	−10.370	1.00	39.74		C
ATOM	2088	NZ	LYS	D	54	17.279	87.308	−11.098	1.00	49.26		N1+
ATOM	2089	N	ARG	D	55	17.318	81.924	−9.890	1.00	38.57		N
ATOM	2090	C	ARG	D	55	17.333	82.285	−7.476	1.00	39.73		C
ATOM	2091	O	ARG	D	55	17.511	83.503	−7.533	1.00	41.35		O
ATOM	2092	CA	AARG	D	55	17.814	81.402	−8.621	0.50	38.68		C
ATOM	2093	CB	AARG	D	55	19.341	81.344	−8.605	0.50	37.77		C
ATOM	2094	CG	AARG	D	55	19.958	80.202	−9.404	0.50	40.11		C
ATOM	2095	CD	AARG	D	55	21.494	80.251	−9.387	0.50	40.35		C
ATOM	2096	NE	AARG	D	55	22.017	81.378	−10.159	0.50	39.90		N
ATOM	2097	CZ	AARG	D	55	22.738	82.377	−9.659	0.50	39.21		C
ATOM	2098	NH1	AARG	D	55	23.141	83.349	−10.459	0.50	39.24		N1+
ATOM	2099	NH2	AARG	D	55	23.060	82.406	−8.369	0.50	34.82		N
ATOM	2100	CA	BARG	D	55	17.803	81.399	−8.621	0.50	38.68		C
ATOM	2101	CB	BARG	D	55	19.324	81.321	−8.607	0.50	37.74		C
ATOM	2102	CG	BARG	D	55	19.902	80.435	−9.684	0.50	40.11		C
ATOM	2103	CD	BARG	D	55	21.390	80.690	−9.875	0.50	41.27		C
ATOM	2104	NE	BARG	D	55	21.881	80.029	−11.080	0.50	44.29		N
ATOM	2105	CZ	BARG	D	55	21.979	80.606	−12.275	0.50	41.10		C
ATOM	2106	NH1	BARG	D	55	21.632	81.878	−12.448	0.50	43.98		N1+
ATOM	2107	NH2	BARG	D	55	22.436	79.903	−13.299	0.50	37.99		N
ATOM	2108	N	PRO	D	56	16.709	81.722	−6.444	1.00	42.43		N
ATOM	2109	CA	PRO	D	56	16.550	82.476	−5.202	1.00	39.14		C
ATOM	2110	C	PRO	D	56	17.937	82.781	−4.673	1.00	39.14		C
ATOM	2111	O	PRO	D	56	18.921	82.132	−5.037	1.00	39.24		O
ATOM	2112	CB	PRO	D	56	15.800	81.513	−4.264	1.00	40.40		C
ATOM	2113	CG	PRO	D	56	15.350	80.384	−5.079	1.00	36.67		C
ATOM	2114	CD	PRO	D	56	16.195	80.347	−6.344	1.00	38.20		C
ATOM	2115	N	SER	D	57	18.025	83.787	−3.819	1.00	38.52		N
ATOM	2116	CA	SER	D	57	19.326	84.087	−3.245	1.00	45.88		C
ATOM	2117	C	SER	D	57	19.760	82.911	−2.381	1.00	44.76		C
ATOM	2118	O	SER	D	57	18.928	82.206	−1.807	1.00	46.46		O
ATOM	2119	CB	SER	D	57	19.282	85.384	−2.441	1.00	45.60		C
ATOM	2120	OG	SER	D	57	18.126	85.430	−1.652	1.00	61.35		O
ATOM	2121	N	GLY	D	58	21.056	82.630	−2.375	1.00	45.80		N
ATOM	2122	CA	GLY	D	58	21.558	81.468	−1.677	1.00	38.95		C
ATOM	2123	C	GLY	D	58	21.780	80.253	−2.549	1.00	45.79		C
ATOM	2124	O	GLY	D	58	22.406	79.290	−2.093	1.00	50.05		O
ATOM	2125	N	ILE	D	59	21.280	80.246	−3.777	1.00	44.59		N
ATOM	2126	CA	ILE	D	59	21.479	79.123	−4.684	1.00	37.66		C
ATOM	2127	C	ILE	D	59	22.682	79.446	−5.571	1.00	42.15		C
ATOM	2128	O	ILE	D	59	22.645	80.454	−6.294	1.00	41.34		O
ATOM	2129	CB	ILE	D	59	20.232	78.831	−5.528	1.00	40.49		C
ATOM	2130	CG1	ILE	D	59	19.045	78.500	−4.616	1.00	37.44		C
ATOM	2131	CG2	ILE	D	59	20.527	77.690	−6.542	1.00	36.08		C
ATOM	2132	CD1	ILE	D	59	19.273	77.277	−3.723	1.00	34.90		C
ATOM	2133	N	PRO	D	60	23.724	78.612	−5.571	1.00	38.05		N
ATOM	2134	CA	PRO	D	60	24.938	78.914	−6.342	1.00	42.90		C
ATOM	2135	C	PRO	D	60	24.666	78.936	−7.835	1.00	40.36		C
ATOM	2136	O	PRO	D	60	23.778	78.245	−8.333	1.00	40.44		O
ATOM	2137	CB	PRO	D	60	25.888	77.754	−5.990	1.00	43.52		C
ATOM	2138	CG	PRO	D	60	25.222	76.963	−4.934	1.00	44.09		C
ATOM	2139	CD	PRO	D	60	23.756	77.268	−4.984	1.00	41.65		C
ATOM	2140	N	ALA	D	61	25.495	79.695	−8.557	1.00	38.15		N
ATOM	2141	CA	ALA	D	61	25.351	79.835	−10.003	1.00	46.92		C
ATOM	2142	C	ALA	D	61	25.639	78.546	−10.780	1.00	41.95		C
ATOM	2143	O	ALA	D	61	25.376	78.501	−11.990	1.00	41.08		O
ATOM	2144	CB	ALA	D	61	26.268	80.955	−10.507	1.00	37.90		C
ATOM	2145	N	ARG	D	62	26.167	77.501	−10.144	1.00	40.02		N
ATOM	2146	CA	ARG	D	62	26.364	76.277	−10.909	1.00	39.12		C
ATOM	2147	C	ARG	D	62	25.061	75.511	−11.136	1.00	41.84		C
ATOM	2148	O	ARG	D	62	25.060	74.529	−11.894	1.00	38.44		O
ATOM	2149	CB	ARG	D	62	27.411	75.384	−10.240	1.00	40.13		C
ATOM	2150	CG	ARG	D	62	27.061	74.940	−8.830	1.00	51.16		C
ATOM	2151	CD	ARG	D	62	28.110	73.962	−8.276	1.00	54.07		C
ATOM	2152	NE	ARG	D	62	27.617	73.327	−7.065	1.00	42.44		N
ATOM	2153	CZ	ARG	D	62	27.632	73.937	−5.888	1.00	48.82		C
ATOM	2154	NH1	ARG	D	62	28.139	75.165	−5.790	1.00	55.75		N1+
ATOM	2155	NH2	ARG	D	62	27.145	73.336	−4.819	1.00	44.87		N
ATOM	2156	N	PHE	D	63	23.959	75.946	−10.518	1.00	35.81		N
ATOM	2157	CA	PHE	D	63	22.630	75.461	−10.857	1.00	36.89		C
ATOM	2158	C	PHE	D	63	22.032	76.381	−11.914	1.00	41.20		C
ATOM	2159	O	PHE	D	63	22.021	77.610	−11.749	1.00	39.30		O
ATOM	2160	CB	PHE	D	63	21.724	75.420	−9.622	1.00	36.15		C
ATOM	2161	CG	PHE	D	63	22.177	74.455	−8.550	1.00	35.88		C
ATOM	2162	CD1	PHE	D	63	23.020	74.870	−7.539	1.00	36.00		C
ATOM	2163	CD2	PHE	D	63	21.747	73.132	−8.556	1.00	38.64		C
ATOM	2164	CE1	PHE	D	63	23.443	73.983	−6.550	1.00	43.00		C
ATOM	2165	CE2	PHE	D	63	22.165	72.239	−7.572	1.00	37.52		C
ATOM	2166	CZ	PHE	D	63	23.013	72.664	−6.565	1.00	36.44		C
ATOM	2167	N	SER	D	64	21.548	75.795	−13.005	1.00	35.81		N
ATOM	2168	CA	SER	D	64	20.854	76.595	−14.008	1.00	37.12		C
ATOM	2169	C	SER	D	64	19.753	75.760	−14.648	1.00	38.07		C
ATOM	2170	O	SER	D	64	19.691	74.529	−14.505	1.00	38.30		O
ATOM	2171	CB	SER	D	64	21.812	77.151	−15.076	1.00	31.57		C
ATOM	2172	OG	SER	D	64	22.505	76.104	−15.730	1.00	44.67		O
ATOM	2173	N	GLY	D	65	18.868	76.454	−15.349	1.00	34.85		N
ATOM	2174	CA	GLY	D	65	17.712	75.817	−15.927	1.00	38.26		C
ATOM	2175	C	GLY	D	65	17.422	76.371	−17.302	1.00	40.50		C
ATOM	2176	O	GLY	D	65	17.829	77.479	−17.661	1.00	39.25		O
ATOM	2177	N	SER	D	66	16.706	75.570	−18.071	1.00	33.85		N
ATOM	2178	CA	SER	D	66	16.204	76.050	−19.344	1.00	35.96		C
ATOM	2179	C	SER	D	66	14.865	75.386	−19.584	1.00	39.56		C
ATOM	2180	O	SER	D	66	14.493	74.412	−18.914	1.00	36.55		O
ATOM	2181	CB	SER	D	66	17.164	75.765	−20.490	1.00	36.16		C
ATOM	2182	OG	SER	D	66	17.463	74.379	−20.517	1.00	43.70		O
ATOM	2183	N	LYS	D	67	14.132	75.959	−20.522	1.00	31.53		N
ATOM	2184	CA	LYS	D	67	12.820	75.482	−20.896	1.00	33.07		C
ATOM	2185	C	LYS	D	67	12.746	75.549	−22.407	1.00	38.33		C
ATOM	2186	O	LYS	D	67	13.238	76.494	−23.014	1.00	43.23		O
ATOM	2187	CB	LYS	D	67	11.690	76.313	−20.249	1.00	32.47		C
ATOM	2188	CG	LYS	D	67	10.269	75.914	−20.705	1.00	28.80		C
ATOM	2189	CD	LYS	D	67	9.194	76.736	−20.001	1.00	35.59		C
ATOM	2190	CE	LYS	D	67	7.890	76.733	−20.788	1.00	45.34		C
ATOM	2191	NZ	LYS	D	67	6.693	77.312	−20.018	1.00	45.74		N1+
ATOM	2192	N	SER	D	68	12.175	74.523	−23.008	1.00	40.72		N
ATOM	2193	CA	SER	D	68	11.983	74.502	−24.446	1.00	40.77		C
ATOM	2194	C	SER	D	68	10.705	73.722	−24.702	1.00	40.33		C
ATOM	2195	O	SER	D	68	10.665	72.518	−24.439	1.00	41.36		O
ATOM	2196	CB	SER	D	68	13.179	73.866	−25.139	1.00	44.26		C
ATOM	2197	OG	SER	D	68	12.935	73.761	−26.526	1.00	55.67		O
ATOM	2198	N	GLY	D	69	9.655	74.408	−25.145	1.00	37.35		N
ATOM	2199	CA	GLY	D	69	8.413	73.715	−25.466	1.00	34.14		C
ATOM	2200	C	GLY	D	69	7.800	73.055	−24.242	1.00	37.93		C
ATOM	2201	O	GLY	D	69	7.543	73.700	−23.220	1.00	34.02		O
ATOM	2202	N	THR	D	70	7.592	71.738	−24.310	1.00	38.48		N
ATOM	2203	CA	THR	D	70	6.956	71.011	−23.219	1.00	38.13		C
ATOM	2204	C	THR	D	70	7.967	70.318	−22.304	1.00	39.79		C
ATOM	2205	O	THR	D	70	7.590	69.416	−21.549	1.00	40.93		O
ATOM	2206	CB	THR	D	70	5.968	69.982	−23.771	1.00	37.94		C
ATOM	2207	OG1	THR	D	70	6.672	69.053	−24.608	1.00	38.51		O
ATOM	2208	CG2	THR	D	70	4.899	70.665	−24.571	1.00	27.17		C
ATOM	2209	N	SER	D	71	9.240	70.702	−22.357	1.00	32.96		N
ATOM	2210	CA	SER	D	71	10.202	70.129	−21.431	1.00	40.52		C
ATOM	2211	C	SER	D	71	11.091	71.219	−20.853	1.00	36.32		C
ATOM	2212	O	SER	D	71	11.231	72.312	−21.411	1.00	44.52		O
ATOM	2213	CB	SER	D	71	11.049	69.031	−22.089	1.00	48.49		C
ATOM	2214	OG	SER	D	71	11.991	69.599	−22.976	1.00	58.32		O
ATOM	2215	N	ALA	D	72	11.645	70.915	−19.686	1.00	31.74		N
ATOM	2216	CA	ALA	D	72	12.519	71.800	−18.942	1.00	32.67		C
ATOM	2217	C	ALA	D	72	13.688	70.976	−18.443	1.00	37.05		C
ATOM	2218	O	ALA	D	72	13.541	69.784	−18.161	1.00	35.94		O
ATOM	2219	CB	ALA	D	72	11.796	72.461	−17.758	1.00	29.67		C
ATOM	2220	N	THR	D	73	14.861	71.594	−18.349	1.00	33.25		N
ATOM	2221	CA	THR	D	73	15.969	70.834	−17.809	1.00	33.69		C
ATOM	2222	C	THR	D	73	16.765	71.667	−16.813	1.00	36.67		C
ATOM	2223	O	THR	D	73	16.912	72.886	−16.951	1.00	37.39		O
ATOM	2224	CB	THR	D	73	16.875	70.239	−18.916	1.00	40.87		C
ATOM	2225	OG1	THR	D	73	18.214	70.724	−18.799	1.00	48.32		O
ATOM	2226	CG2	THR	D	73	16.335	70.483	−20.289	1.00	31.17		C
ATOM	2227	N	LEU	D	74	17.224	70.979	−15.775	1.00	36.18		N
ATOM	2228	CA	LEU	D	74	18.084	71.536	−14.749	1.00	40.71		C
ATOM	2229	C	LEU	D	74	19.514	71.068	−15.005	1.00	39.16		C
ATOM	2230	O	LEU	D	74	19.747	69.887	−15.269	1.00	36.86		O
ATOM	2231	CB	LEU	D	74	17.597	71.088	−13.375	1.00	32.52		C
ATOM	2232	CG	LEU	D	74	18.632	71.088	−12.262	1.00	33.76		C
ATOM	2233	CD1	LEU	D	74	18.979	72.495	−11.837	1.00	34.80		C
ATOM	2234	CD2	LEU	D	74	18.078	70.285	−11.105	1.00	28.46		C
ATOM	2235	N	GLY	D	75	20.456	71.992	−14.964	1.00	39.23		N
ATOM	2236	CA	GLY	D	75	21.861	71.676	−15.155	1.00	34.28		C
ATOM	2237	C	GLY	D	75	22.643	71.975	−13.891	1.00	35.73		C
ATOM	2238	O	GLY	D	75	22.380	72.971	−13.212	1.00	31.27		O
ATOM	2239	N	ILE	D	76	23.572	71.083	−13.555	1.00	37.91		N
ATOM	2240	CA	ILE	D	76	24.460	71.270	−12.416	1.00	37.96		C
ATOM	2241	C	ILE	D	76	25.880	71.043	−12.900	1.00	44.61		C
ATOM	2242	O	ILE	D	76	26.245	69.912	−13.243	1.00	45.05		O
ATOM	2243	CB	ILE	D	76	24.132	70.324	−11.259	1.00	37.47		C
ATOM	2244	CG1	ILE	D	76	22.612	70.258	−11.056	1.00	38.58		C
ATOM	2245	CG2	ILE	D	76	24.842	70.801	−10.019	1.00	34.75		C
ATOM	2246	CD1	ILE	D	76	22.182	69.396	−9.926	1.00	35.25		C
ATOM	2247	N	THR	D	77	26.684	72.103	−12.916	1.00	41.92		N
ATOM	2248	CA	THR	D	77	28.105	72.001	−13.217	1.00	45.22		C
ATOM	2249	C	THR	D	77	28.911	71.995	−11.922	1.00	49.05		C
ATOM	2250	O	THR	D	77	28.433	72.413	−10.863	1.00	46.09		O
ATOM	2251	CB	THR	D	77	28.570	73.156	−14.111	1.00	45.74		C
ATOM	2252	OG1	THR	D	77	28.494	74.389	−13.383	1.00	45.10		O
ATOM	2253	CG2	THR	D	77	27.707	73.246	−15.356	1.00	41.50		C
ATOM	2254	N	GLY	D	78	30.136	71.474	−12.015	1.00	50.10		N
ATOM	2255	CA	GLY	D	78	31.054	71.450	−10.893	1.00	40.32		C
ATOM	2256	C	GLY	D	78	30.509	70.763	−9.660	1.00	47.60		C
ATOM	2257	O	GLY	D	78	30.599	71.321	−8.562	1.00	46.13		O
ATOM	2258	N	LEU	D	79	29.977	69.545	−9.822	1.00	44.28		N
ATOM	2259	CA	LEU	D	79	29.291	68.851	−8.735	1.00	41.62		C
ATOM	2260	C	LEU	D	79	30.097	68.875	−7.445	1.00	41.28		C
ATOM	2261	O	LEU	D	79	31.306	68.625	−7.445	1.00	43.99		O
ATOM	2262	CB	LEU	D	79	29.044	67.391	−9.108	1.00	44.54		C
ATOM	2263	CG	LEU	D	79	27.718	66.829	−9.591	1.00	41.80		C
ATOM	2264	CD1	LEU	D	79	26.548	67.743	−9.317	1.00	41.01		C
ATOM	2265	CD2	LEU	D	79	27.807	66.456	−11.048	1.00	48.29		C
ATOM	2266	N	GLN	D	80	29.407	69.147	−6.341	1.00	38.12		N
ATOM	2267	CA	GLN	D	80	29.955	69.025	−5.000	1.00	37.63		C
ATOM	2268	C	GLN	D	80	29.166	67.992	−4.207	1.00	39.83		C
ATOM	2269	O	GLN	D	80	27.975	67.771	−4.461	1.00	44.36		O
ATOM	2270	CB	GLN	D	80	29.925	70.349	−4.277	1.00	35.93		C
ATOM	2271	CG	GLN	D	80	30.598	71.424	−5.072	1.00	44.41		C
ATOM	2272	CD	GLN	D	80	30.602	72.746	−4.351	1.00	48.07		C
ATOM	2273	OE1	GLN	D	80	30.141	72.848	−3.211	1.00	51.38		O
ATOM	2274	NE2	GLN	D	80	31.108	73.778	−5.018	1.00	49.68		N
ATOM	2275	N	THR	D	81	29.838	67.362	−3.236	1.00	39.23		N
ATOM	2276	CA	THR	D	81	29.185	66.313	−2.459	1.00	43.43		C
ATOM	2277	C	THR	D	81	27.905	66.827	−1.825	1.00	38.49		C
ATOM	2278	O	THR	D	81	26.949	66.066	−1.660	1.00	43.22		O
ATOM	2279	CB	THR	D	81	30.122	65.740	−1.386	1.00	33.08		C
ATOM	2280	OG1	THR	D	81	30.589	66.796	−0.558	1.00	47.69		O
ATOM	2281	CG2	THR	D	81	31.307	65.035	−2.020	1.00	35.64		C
ATOM	2282	N	GLY	D	82	27.859	68.112	−1.498	1.00	35.25		N
ATOM	2283	CA	GLY	D	82	26.664	68.722	−0.952	1.00	40.04		C
ATOM	2284	C	GLY	D	82	25.510	68.895	−1.929	1.00	38.60		C
ATOM	2285	O	GLY	D	82	24.437	69.339	−1.510	1.00	35.12		O
ATOM	2286	N	ASP	D	83	25.694	68.543	−3.200	1.00	33.43		N
ATOM	2287	CA	ASP	D	83	24.619	68.564	−4.179	1.00	37.84		C
ATOM	2288	C	ASP	D	83	23.834	67.251	−4.245	1.00	43.45		C
ATOM	2289	O	ASP	D	83	22.814	67.191	−4.957	1.00	40.21		O
ATOM	2290	CB	ASP	D	83	25.181	68.882	−5.566	1.00	33.25		C
ATOM	2291	CG	ASP	D	83	25.971	70.173	−5.593	1.00	42.35		C
ATOM	2292	OD1	ASP	D	83	25.680	71.085	−4.788	1.00	36.88		O
ATOM	2293	OD2	ASP	D	83	26.882	70.284	−6.440	1.00	44.43		O1−
ATOM	2294	N	GLU	D	84	24.310	66.192	−3.577	1.00	37.08		N
ATOM	2295	CA	GLU	D	84	23.578	64.931	−3.529	1.00	38.14		C
ATOM	2296	C	GLU	D	84	22.192	65.159	−2.929	1.00	37.73		C
ATOM	2297	O	GLU	D	84	22.075	65.642	−1.800	1.00	36.95		O
ATOM	2298	CB	GLU	D	84	24.359	63.904	−2.708	1.00	33.68		C
ATOM	2299	CG	GLU	D	84	23.683	62.544	−2.653	1.00	41.33		C
ATOM	2300	CD	GLU	D	84	24.682	61.389	−2.458	1.00	46.09		C
ATOM	2301	OE1	GLU	D	84	24.374	60.429	−1.716	1.00	49.48		O
ATOM	2302	OE2	GLU	D	84	25.766	61.427	−3.078	1.00	45.22		O1−
ATOM	2303	N	ALA	D	85	21.146	64.836	−3.688	1.00	31.07		N
ATOM	2304	CA	ALA	D	85	19.786	65.206	−3.298	1.00	29.56		C
ATOM	2305	C	ALA	D	85	18.818	64.596	−4.293	1.00	32.77		C
ATOM	2306	O	ALA	D	85	19.218	64.022	−5.314	1.00	32.03		O
ATOM	2307	CB	ALA	D	85	19.590	66.729	−3.227	1.00	30.06		C
ATOM	2308	N	ASP	D	86	17.531	64.697	−3.959	1.00	30.95		N
ATOM	2309	CA	ASP	D	86	16.457	64.474	−4.921	1.00	30.44		C
ATOM	2310	C	ASP	D	86	16.015	65.817	−5.481	1.00	33.26		C
ATOM	2311	O	ASP	D	86	15.958	66.816	−4.752	1.00	29.91		O
ATOM	2312	CB	ASP	D	86	15.261	63.780	−4.283	1.00	36.23		C
ATOM	2313	CG	ASP	D	86	15.600	62.414	−3.757	1.00	39.79		C
ATOM	2314	OD1	ASP	D	86	16.287	61.640	−4.460	1.00	49.35		O
ATOM	2315	OD2	ASP	D	86	15.202	62.134	−2.620	1.00	52.11		O1−
ATOM	2316	N	TYR	D	87	15.723	65.834	−6.775	1.00	28.24		N
ATOM	2317	CA	TYR	D	87	15.349	67.045	−7.481	1.00	30.37		C
ATOM	2318	C	TYR	D	87	13.993	66.832	−8.116	1.00	30.53		C
ATOM	2319	O	TYR	D	87	13.736	65.781	−8.716	1.00	31.12		O
ATOM	2320	CB	TYR	D	87	16.407	67.425	−8.550	1.00	31.35		C
ATOM	2321	CG	TYR	D	87	17.707	67.860	−7.930	1.00	28.53		C
ATOM	2322	CD2	TYR	D	87	18.711	66.933	−7.628	1.00	29.65		C
ATOM	2323	CD1	TYR	D	87	17.919	69.192	−7.596	1.00	30.97		C
ATOM	2324	CE2	TYR	D	87	19.913	67.350	−7.040	1.00	36.12		C
ATOM	2325	CE1	TYR	D	87	19.110	69.620	−6.999	1.00	32.34		C
ATOM	2326	CZ	TYR	D	87	20.101	68.700	−6.728	1.00	36.00		C
ATOM	2327	OH	TYR	D	87	21.261	69.124	−6.123	1.00	36.35		O
ATOM	2328	N	TYR	D	88	13.130	67.833	−7.986	1.00	31.77		N
ATOM	2329	CA	TYR	D	88	11.763	67.756	−8.495	1.00	30.69		C
ATOM	2330	C	TYR	D	88	11.442	68.977	−9.350	1.00	33.16		C
ATOM	2331	O	TYR	D	88	11.697	70.123	−8.943	1.00	27.49		O
ATOM	2332	CB	TYR	D	88	10.755	67.662	−7.330	1.00	28.47		C
ATOM	2333	CG	TYR	D	88	10.863	66.418	−6.469	1.00	32.12		C
ATOM	2334	CD1	TYR	D	88	10.157	65.254	−6.797	1.00	33.44		C
ATOM	2335	CD2	TYR	D	88	11.639	66.407	−5.312	1.00	35.30		C
ATOM	2336	CE1	TYR	D	88	10.246	64.107	−6.011	1.00	33.26		C
ATOM	2337	CE2	TYR	D	88	11.735	65.256	−4.505	1.00	28.88		C
ATOM	2338	CZ	TYR	D	88	11.038	64.121	−4.860	1.00	35.12		C
ATOM	2339	OH	TYR	D	88	11.138	63.001	−4.067	1.00	41.20		O
ATOM	2340	N	CYS	D	89	10.860	68.743	−10.520	1.00	29.10		N
ATOM	2341	CA	CYS	D	89	10.217	69.855	−11.206	1.00	33.19		C
ATOM	2342	C	CYS	D	89	8.723	69.907	−10.850	1.00	37.48		C
ATOM	2343	O	CYS	D	89	8.110	68.906	−10.450	1.00	33.89		O
ATOM	2344	CB	CYS	D	89	10.397	69.751	−12.722	1.00	35.57		C
ATOM	2345	SG	CYS	D	89	9.788	68.160	−13.353	1.00	50.43		S
ATOM	2346	N	GLY	D	90	8.153	71.103	−10.985	1.00	35.51		N
ATOM	2347	CA	GLY	D	90	6.747	71.329	−10.696	1.00	31.51		C
ATOM	2348	C	GLY	D	90	6.184	72.474	−11.510	1.00	32.91		C
ATOM	2349	O	GLY	D	90	6.886	73.440	−11.821	1.00	37.81		O
ATOM	2350	N	THR	D	91	4.905	72.347	−11.876	1.00	29.44		N
ATOM	2351	CA	THR	D	91	4.112	73.391	−12.523	1.00	35.31		C
ATOM	2352	C	THR	D	91	2.648	73.192	−12.187	1.00	34.83		C
ATOM	2353	O	THR	D	91	2.252	72.229	−11.533	1.00	31.62		O
ATOM	2354	CB	THR	D	91	4.039	73.364	−14.063	1.00	36.67		C
ATOM	2355	OG1	THR	D	91	4.722	72.256	−14.635	1.00	42.40		O
ATOM	2356	CG2	THR	D	91	4.377	74.637	−14.683	1.00	25.98		C
ATOM	2357	N	TRP	D	92	1.845	74.047	−12.800	1.00	33.75		N
ATOM	2358	CA	TRP	D	92	0.422	73.882	−12.929	1.00	32.47		C
ATOM	2359	C	TRP	D	92	0.088	73.103	−14.202	1.00	34.81		C
ATOM	2360	O	TRP	D	92	0.757	73.209	−15.235	1.00	30.64		O
ATOM	2361	CB	TRP	D	92	−0.234	75.251	−12.956	1.00	33.91		C
ATOM	2362	CG	TRP	D	92	−1.719	75.251	−12.940	1.00	35.91		C
ATOM	2363	CD1	TRP	D	92	−2.553	75.591	−13.969	1.00	31.74		C
ATOM	2364	CD2	TRP	D	92	−2.557	74.949	−11.818	1.00	34.97		C
ATOM	2365	NE1	TRP	D	92	−3.860	75.519	−13.554	1.00	37.78		N
ATOM	2366	CE2	TRP	D	92	−3.893	75.127	−12.238	1.00	39.89		C
ATOM	2367	CE3	TRP	D	92	−2.308	74.567	−10.494	1.00	27.09		C
ATOM	2368	CZ2	TRP	D	92	−4.979	74.921	−11.380	1.00	36.03		C
ATOM	2369	CZ3	TRP	D	92	−3.384	74.357	−9.643	1.00	35.46		C
ATOM	2370	CH2	TRP	D	92	−4.706	74.542	−10.087	1.00	35.32		C
ATOM	2371	N	ASP	D	93	−0.943	72.296	−14.109	1.00	32.62		N
ATOM	2372	CA	ASP	D	93	−1.540	71.671	−15.277	1.00	38.27		C
ATOM	2373	C	ASP	D	93	−2.925	72.275	−15.476	1.00	37.51		C
ATOM	2374	O	ASP	D	93	−3.809	72.089	−14.634	1.00	39.63		O
ATOM	2375	CB	ASP	D	93	−1.609	70.162	−15.121	1.00	37.98		C
ATOM	2376	CG	ASP	D	93	−2.016	69.490	−16.396	1.00	37.56		C
ATOM	2377	OD1	ASP	D	93	−3.109	69.827	−16.919	1.00	38.96		O1−
ATOM	2378	OD2	ASP	D	93	−1.226	68.659	−16.884	1.00	37.13		O
ATOM	2379	N	SER	D	94	−3.094	73.010	−16.583	1.00	40.55		N
ATOM	2380	CA	SER	D	94	−4.324	73.756	−16.838	1.00	43.35		C
ATOM	2381	C	SER	D	94	−5.502	72.843	−17.132	1.00	41.15		C
ATOM	2382	O	SER	D	94	−6.643	73.204	−16.848	1.00	47.84		O
ATOM	2383	CB	SER	D	94	−4.124	74.716	−18.009	1.00	37.93		C
ATOM	2384	OG	SER	D	94	−3.093	75.653	−17.720	1.00	50.29		O
ATOM	2385	N	SER	D	95	−5.261	71.659	−17.656	1.00	39.23		N
ATOM	2386	CA	SER	D	95	−6.392	70.814	−17.991	1.00	45.37		C
ATOM	2387	C	SER	D	95	−6.795	69.916	−16.843	1.00	44.47		C
ATOM	2388	O	SER	D	95	−7.981	69.617	−16.704	1.00	52.00		O
ATOM	2389	CB	SER	D	95	−6.084	69.960	−19.223	1.00	44.25		C
ATOM	2390	OG	SER	D	95	−5.390	68.785	−18.856	1.00	58.75		O
ATOM	2391	N	LEU	D	96	−5.845	69.487	−16.012	1.00	43.88		N
ATOM	2392	CA	LEU	D	96	−6.173	68.775	−14.780	1.00	37.73		C
ATOM	2393	C	LEU	D	96	−6.491	69.723	−13.621	1.00	36.61		C
ATOM	2394	O	LEU	D	96	−6.885	69.255	−12.550	1.00	38.29		O
ATOM	2395	CB	LEU	D	96	−5.019	67.839	−14.391	1.00	41.42		C
ATOM	2396	CG	LEU	D	96	−4.577	66.750	−15.380	1.00	39.10		C
ATOM	2397	CD1	LEU	D	96	−3.261	66.160	−14.963	1.00	34.94		C
ATOM	2398	CD2	LEU	D	96	−5.612	65.640	−15.506	1.00	35.48		C
ATOM	2399	N	ASN	D	97	−6.353	71.034	−13.811	1.00	37.50		N
ATOM	2400	CA	ASN	D	97	−6.524	72.032	−12.750	1.00	39.48		C
ATOM	2401	C	ASN	D	97	−5.885	71.606	−11.418	1.00	35.80		C
ATOM	2402	O	ASN	D	97	−6.519	71.581	−10.367	1.00	35.42		O
ATOM	2403	CB	ASN	D	97	−8.002	72.403	−12.591	1.00	33.46		C
ATOM	2404	CG	ASN	D	97	−8.304	73.766	−13.211	1.00	59.81		C
ATOM	2405	OD1	ASN	D	97	−8.600	74.731	−12.490	1.00	63.64		O
ATOM	2406	ND2	ASN	D	97	−8.104	73.888	−14.535	1.00	48.78		N
ATOM	2407	N	THR	D	98	−4.584	71.319	−11.468	1.00	34.96		N
ATOM	2408	CA	THR	D	98	−3.880	70.883	−10.267	1.00	40.51		C
ATOM	2409	C	THR	D	98	−2.389	71.197	−10.382	1.00	33.13		C
ATOM	2410	O	THR	D	98	−1.843	71.349	−11.482	1.00	33.25		O
ATOM	2411	CB	THR	D	98	−4.095	69.378	−10.000	1.00	31.21		C
ATOM	2412	OG1	THR	D	98	−3.498	69.048	−8.749	1.00	36.06		O
ATOM	2413	CG2	THR	D	98	−3.428	68.531	−11.061	1.00	31.76		C
ATOM	2414	N	VAL	D	99	−1.730	71.290	−9.222	1.00	29.98		N
ATOM	2415	CA	VAL	D	99	−0.267	71.342	−9.211	1.00	34.24		C
ATOM	2416	C	VAL	D	99	0.296	69.972	−9.558	1.00	34.16		C
ATOM	2417	O	VAL	D	99	−0.215	68.936	−9.120	1.00	34.33		O
ATOM	2418	CB	VAL	D	99	0.278	71.796	−7.849	1.00	33.92		C
ATOM	2419	CG1	VAL	D	99	1.787	71.619	−7.819	1.00	30.13		C
ATOM	2420	CG2	VAL	D	99	−0.114	73.241	−7.535	1.00	28.38		C
ATOM	2421	N	VAL	D	100	1.375	69.952	−10.321	1.00	29.37		N
ATOM	2422	CA	VAL	D	100	1.871	68.706	−10.875	1.00	30.81		C
ATOM	2423	C	VAL	D	100	3.380	68.659	−10.653	1.00	33.23		C
ATOM	2424	O	VAL	D	100	4.072	69.662	−10.890	1.00	32.58		O
ATOM	2425	CB	VAL	D	100	1.442	68.618	−12.352	1.00	32.14		C
ATOM	2426	CG1	VAL	D	100	2.538	68.362	−13.255	1.00	38.21		C
ATOM	2427	CG2	VAL	D	100	0.327	67.591	−12.507	1.00	35.01		C
ATOM	2428	N	PHE	D	101	3.869	67.537	−10.090	1.00	32.44		N
ATOM	2429	CA	PHE	D	101	5.292	67.296	−9.826	1.00	28.74		C
ATOM	2430	C	PHE	D	101	5.824	66.191	−10.728	1.00	30.41		C
ATOM	2431	O	PHE	D	101	5.091	65.280	−11.116	1.00	36.07		O
ATOM	2432	CB	PHE	D	101	5.571	66.879	−8.367	1.00	29.14		C
ATOM	2433	CG	PHE	D	101	5.505	68.006	−7.372	1.00	29.14		C
ATOM	2434	CD1	PHE	D	101	6.472	68.991	−7.355	1.00	29.41		C
ATOM	2435	CD2	PHE	D	101	4.483	68.067	−6.438	1.00	29.40		C
ATOM	2436	CE1	PHE	D	101	6.421	70.041	−6.430	1.00	30.71		C
ATOM	2437	CE2	PHE	D	101	4.412	69.107	−5.519	1.00	31.48		C
ATOM	2438	CZ	PHE	D	101	5.388	70.100	−5.509	1.00	28.28		C
ATOM	2439	N	GLY	D	102	7.112	66.269	−11.069	1.00	35.21		N
ATOM	2440	CA	GLY	D	102	7.774	65.104	−11.621	1.00	30.07		C
ATOM	2441	C	GLY	D	102	7.949	64.054	−10.539	1.00	34.24		C
ATOM	2442	O	GLY	D	102	7.809	64.324	−9.342	1.00	32.05		O
ATOM	2443	N	GLY	D	103	8.282	62.833	−10.962	1.00	33.87		N
ATOM	2444	CA	GLY	D	103	8.500	61.756	−9.998	1.00	30.14		C
ATOM	2445	C	GLY	D	103	9.767	61.896	−9.164	1.00	33.06		C
ATOM	2446	O	GLY	D	103	9.929	61.153	−8.195	1.00	33.57		O
ATOM	2447	N	GLY	D	104	10.649	62.840	−9.500	1.00	34.22		N
ATOM	2448	CA	GLY	D	104	11.866	63.034	−8.746	1.00	30.60		C
ATOM	2449	C	GLY	D	104	13.056	62.330	−9.363	1.00	32.84		C
ATOM	2450	O	GLY	D	104	12.939	61.230	−9.914	1.00	37.98		O
ATOM	2451	N	THR	D	105	14.219	62.953	−9.267	1.00	33.92		N
ATOM	2452	CA	THR	D	105	15.460	62.372	−9.749	1.00	32.14		C
ATOM	2453	C	THR	D	105	16.422	62.308	−8.581	1.00	35.31		C
ATOM	2454	O	THR	D	105	16.683	63.335	−7.945	1.00	33.86		O
ATOM	2455	CB	THR	D	105	16.052	63.202	−10.878	1.00	35.69		C
ATOM	2456	OG1	THR	D	105	15.118	63.236	−11.966	1.00	33.00		O
ATOM	2457	CG2	THR	D	105	17.374	62.575	−11.328	1.00	32.50		C
ATOM	2458	N	LYS	D	106	16.895	61.095	−8.260	1.00	35.10		N
ATOM	2459	CA	LYS	D	106	17.920	60.928	−7.232	1.00	39.20		C
ATOM	2460	C	LYS	D	106	19.287	61.212	−7.857	1.00	35.77		C
ATOM	2461	O	LYS	D	106	19.709	60.517	−8.796	1.00	33.65		O
ATOM	2462	CB	LYS	D	106	17.875	59.523	−6.612	1.00	37.13		C
ATOM	2463	CG	LYS	D	106	18.991	59.257	−5.575	1.00	41.72		C
ATOM	2464	CD	LYS	D	106	18.843	57.864	−4.893	1.00	66.03		C
ATOM	2465	CE	LYS	D	106	20.060	57.472	−4.002	1.00	43.48		C
ATOM	2466	NZ	LYS	D	106	20.399	58.527	−2.969	1.00	59.67		N1+
ATOM	2467	N	LEU	D	107	19.955	62.253	−7.355	1.00	37.32		N
ATOM	2468	CA	LEU	D	107	21.313	62.606	−7.757	1.00	39.36		C
ATOM	2469	C	LEU	D	107	22.264	62.033	−6.720	1.00	37.65		C
ATOM	2470	O	LEU	D	107	22.211	62.419	−5.542	1.00	38.47		O
ATOM	2471	CB	LEU	D	107	21.518	64.129	−7.855	1.00	26.67		C
ATOM	2472	CG	LEU	D	107	22.784	64.731	−8.570	1.00	37.81		C
ATOM	2473	CD1	LEU	D	107	23.134	66.182	−8.167	1.00	38.40		C
ATOM	2474	CD2	LEU	D	107	24.043	63.923	−8.466	1.00	34.25		C
ATOM	2475	N	THR	D	108	23.176	61.171	−7.148	1.00	30.15		N
ATOM	2476	CA	THR	D	108	24.270	60.823	−6.255	1.00	39.12		C
ATOM	2477	C	THR	D	108	25.591	61.351	−6.810	1.00	33.08		C
ATOM	2478	O	THR	D	108	25.888	61.234	−8.004	1.00	36.87		O
ATOM	2479	CB	THR	D	108	24.311	59.316	−5.951	1.00	42.14		C
ATOM	2480	OG1	THR	D	108	25.514	58.733	−6.459	1.00	51.43		O
ATOM	2481	CG2	THR	D	108	23.075	58.603	−6.471	1.00	39.89		C
ATOM	2482	N	VAL	D	109	26.338	62.011	−5.950	1.00	28.89		N
ATOM	2483	CA	VAL	D	109	27.679	62.461	−6.272	1.00	36.64		C
ATOM	2484	C	VAL	D	109	28.632	61.337	−5.873	1.00	36.03		C
ATOM	2485	O	VAL	D	109	28.838	61.088	−4.686	1.00	34.38		O
ATOM	2486	CB	VAL	D	109	27.999	63.769	−5.547	1.00	39.07		C
ATOM	2487	CG1	VAL	D	109	29.402	64.264	−5.930	1.00	39.69		C
ATOM	2488	CG2	VAL	D	109	26.914	64.807	−5.871	1.00	39.03		C
ATOM	2489	N	LEU	D	110	29.179	60.637	−6.868	1.00	36.80		N
ATOM	2490	CA	LEU	D	110	29.935	59.407	−6.646	1.00	35.35		C
ATOM	2491	C	LEU	D	110	31.166	59.653	−5.794	1.00	38.39		C
ATOM	2492	O	LEU	D	110	32.109	60.294	−6.255	1.00	39.60		O
ATOM	2493	CB	LEU	D	110	30.358	58.813	−7.978	1.00	31.68		C
ATOM	2494	CG	LEU	D	110	29.190	58.470	−8.886	1.00	42.08		C
ATOM	2495	CD1	LEU	D	110	29.720	58.230	−10.264	1.00	33.32		C
ATOM	2496	CD2	LEU	D	110	28.489	57.239	−8.343	1.00	40.75		C
ATOM	2497	N	SER	D	111	31.182	59.144	−4.564	1.00	38.34		N
ATOM	2498	CA	SER	D	111	32.330	59.296	−3.680	1.00	44.10		C
ATOM	2499	C	SER	D	111	32.991	57.956	−3.361	1.00	43.27		C
ATOM	2500	O	SER	D	111	33.843	57.885	−2.476	1.00	38.62		O
ATOM	2501	CB	SER	D	111	31.917	60.001	−2.396	1.00	39.42		C
ATOM	2502	OG	SER	D	111	30.920	59.235	−1.763	1.00	48.72		O
ATOM	2503	N	GLN	D	112	32.606	56.901	−4.058	1.00	36.34		N
ATOM	2504	CA	GLN	D	112	33.300	55.623	−4.010	1.00	36.47		C
ATOM	2505	C	GLN	D	112	32.964	54.900	−5.300	1.00	39.73		C
ATOM	2506	O	GLN	D	112	32.074	55.336	−6.045	1.00	41.47		O
ATOM	2507	CB	GLN	D	112	32.884	54.798	−2.774	1.00	34.11		C
ATOM	2508	CG	GLN	D	112	31.427	54.370	−2.745	1.00	40.26		C
ATOM	2509	CD	GLN	D	112	31.098	53.480	−1.545	1.00	44.54		C
ATOM	2510	OE1	GLN	D	112	31.422	52.289	−1.542	1.00	49.63		O
ATOM	2511	NE2	GLN	D	112	30.446	54.054	−0.523	1.00	32.71		N
ATOM	2512	N	PRO	D	113	33.662	53.816	−5.614	1.00	35.83	GZ00	N
ATOM	2513	CA	PRO	D	113	33.350	53.105	−6.859	1.00	29.36	GZ00	C
ATOM	2514	C	PRO	D	113	31.937	52.559	−6.824	1.00	41.40	GZ00	C
ATOM	2515	O	PRO	D	113	31.391	52.249	−5.763	1.00	33.72	GZ00	O
ATOM	2516	CB	PRO	D	113	34.371	51.969	−6.897	1.00	29.06	GZ00	C
ATOM	2517	CG	PRO	D	113	35.545	52.491	−6.029	1.00	36.02	GZ00	C
ATOM	2518	CD	PRO	D	113	34.878	53.300	−4.948	1.00	37.13	GZ00	C
ATOM	2519	N	LYS	D	114	31.346	52.445	−8.007	1.00	41.30	GZ00	N
ATOM	2520	CA	LYS	D	114	30.050	51.806	−8.112	1.00	39.99	GZ00	C
ATOM	2521	C	LYS	D	114	30.168	50.332	−7.726	1.00	42.17	GZ00	C
ATOM	2522	O	LYS	D	114	31.189	49.691	−7.965	1.00	37.31	GZ00	O
ATOM	2523	CB	LYS	D	114	29.510	51.967	−9.527	1.00	38.27	GZ00	C
ATOM	2524	CG	LYS	D	114	29.198	53.426	−9.890	1.00	48.75	GZ00	C
ATOM	2525	CD	LYS	D	114	28.597	53.502	−11.284	1.00	54.69	GZ00	C
ATOM	2526	CE	LYS	D	114	27.812	54.779	−11.536	1.00	43.93	GZ00	C
ATOM	2527	NZ	LYS	D	114	26.918	54.529	−12.718	1.00	45.98	GZ00	N1+
ATOM	2528	N	ALA	D	115	29.108	49.806	−7.107	1.00	37.03	GZ00	N
ATOM	2529	CA	ALA	D	115	29.084	48.455	−6.562	1.00	31.87	GZ00	C
ATOM	2530	C	ALA	D	115	27.754	47.802	−6.906	1.00	41.28	GZ00	C
ATOM	2531	O	ALA	D	115	26.691	48.304	−6.514	1.00	37.09	GZ00	O
ATOM	2532	CB	ALA	D	115	29.280	48.470	−5.040	1.00	29.90	GZ00	C
ATOM	2533	N	ALA	D	116	27.816	46.676	−7.610	1.00	34.16	GZ00	N
ATOM	2534	CA	ALA	D	116	26.622	45.929	−7.933	1.00	37.15	GZ00	C
ATOM	2535	C	ALA	D	116	26.071	45.289	−6.658	1.00	37.53	GZ00	C
ATOM	2536	O	ALA	D	116	26.816	45.037	−5.715	1.00	41.85	GZ00	O
ATOM	2537	CB	ALA	D	116	26.937	44.870	−8.989	1.00	28.78	GZ00	C
ATOM	2538	N	PRO	D	117	24.772	45.028	−6.594	1.00	40.96	GZ00	N
ATOM	2539	CA	PRO	D	117	24.207	44.481	−5.355	1.00	39.65	GZ00	C
ATOM	2540	C	PRO	D	117	24.590	43.022	−5.180	1.00	40.39	GZ00	C
ATOM	2541	O	PRO	D	117	24.686	42.263	−6.149	1.00	43.42	GZ00	O
ATOM	2542	CB	PRO	D	117	22.699	44.620	−5.568	1.00	37.24	GZ00	C
ATOM	2543	CG	PRO	D	117	22.553	44.435	−7.049	1.00	32.78	GZ00	C
ATOM	2544	CD	PRO	D	117	23.761	45.109	−7.664	1.00	38.78	GZ00	C
ATOM	2545	N	SER	D	118	24.817	42.626	−3.934	1.00	40.21	GZ00	N
ATOM	2546	CA	SER	D	118	24.859	41.203	−3.626	1.00	43.65	GZ00	C
ATOM	2547	C	SER	D	118	23.460	40.793	−3.190	1.00	44.22	GZ00	C
ATOM	2548	O	SER	D	118	22.822	41.475	−2.371	1.00	39.75	GZ00	O
ATOM	2549	CB	SER	D	118	25.901	40.867	−2.559	1.00	37.70	GZ00	C
ATOM	2550	OG	SER	D	118	25.559	41.468	−1.335	1.00	51.03	GZ00	O
ATOM	2551	N	VAL	D	119	22.982	39.701	−3.774	1.00	39.65	GZ00	N
ATOM	2552	CA	VAL	D	119	21.609	39.244	−3.641	1.00	39.06	GZ00	C
ATOM	2553	C	VAL	D	119	21.647	37.843	−3.065	1.00	44.09	GZ00	C
ATOM	2554	O	VAL	D	119	22.315	36.966	−3.626	1.00	39.00	GZ00	O
ATOM	2555	CB	VAL	D	119	20.894	39.235	−5.007	1.00	40.58	GZ00	C
ATOM	2556	CG1	VAL	D	119	19.469	38.765	−4.865	1.00	33.51	GZ00	C
ATOM	2557	CG2	VAL	D	119	20.964	40.602	−5.658	1.00	38.29	GZ00	C
ATOM	2558	N	THR	D	120	20.928	37.620	−1.963	1.00	38.97	GZ00	N
ATOM	2559	CA	THR	D	120	20.719	36.256	−1.507	1.00	40.40	GZ00	C
ATOM	2560	C	THR	D	120	19.218	36.005	−1.360	1.00	41.57	GZ00	C
ATOM	2561	O	THR	D	120	18.487	36.826	−0.798	1.00	39.96	GZ00	O
ATOM	2562	CB	THR	D	120	21.524	35.939	−0.211	1.00	48.39	GZ00	C
ATOM	2563	OG1	THR	D	120	20.649	35.655	0.882	1.00	55.57	GZ00	O
ATOM	2564	CG2	THR	D	120	22.506	37.053	0.178	1.00	42.25	GZ00	C
ATOM	2565	N	LEU	D	121	18.761	34.879	−1.903	1.00	42.65	GZ00	N
ATOM	2566	CA	LEU	D	121	17.343	34.562	−2.031	1.00	44.51	GZ00	C
ATOM	2567	C	LEU	D	121	17.063	33.332	−1.184	1.00	42.61	GZ00	C
ATOM	2568	O	LEU	D	121	17.626	32.269	−1.444	1.00	39.39	GZ00	O
ATOM	2569	CB	LEU	D	121	16.993	34.281	−3.495	1.00	42.30	GZ00	C
ATOM	2570	CG	LEU	D	121	15.574	34.358	−4.059	1.00	45.15	GZ00	C
ATOM	2571	CD1	LEU	D	121	15.333	33.234	−5.034	1.00	45.85	GZ00	C
ATOM	2572	CD2	LEU	D	121	14.485	34.413	−2.986	1.00	44.86	GZ00	C
ATOM	2573	N	PHE	D	122	16.200	33.467	−0.209	1.00	37.70	GZ00	N
ATOM	2574	CA	PHE	D	122	15.865	32.293	0.587	1.00	43.33	GZ00	C
ATOM	2575	C	PHE	D	122	14.487	31.766	0.221	1.00	49.36	GZ00	C
ATOM	2576	O	PHE	D	122	13.539	32.551	0.069	1.00	41.30	GZ00	O
ATOM	2577	CB	PHE	D	122	15.850	32.606	2.079	1.00	39.48	GZ00	C
ATOM	2578	CG	PHE	D	122	17.181	32.910	2.660	1.00	38.94	GZ00	C
ATOM	2579	CD1	PHE	D	122	18.057	31.887	2.982	1.00	38.46	GZ00	C
ATOM	2580	CD2	PHE	D	122	17.533	34.229	2.949	1.00	36.53	GZ00	C
ATOM	2581	CE1	PHE	D	122	19.288	32.169	3.550	1.00	45.61	GZ00	C
ATOM	2582	CE2	PHE	D	122	18.740	34.526	3.528	1.00	38.72	GZ00	C
ATOM	2583	CZ	PHE	D	122	19.636	33.494	3.830	1.00	40.64	GZ00	C
ATOM	2584	N	PRO	D	123	14.347	30.448	0.130	1.00	50.41	GZ00	N
ATOM	2585	CA	PRO	D	123	13.024	29.850	−0.048	1.00	46.66	GZ00	C
ATOM	2586	C	PRO	D	123	12.262	29.853	1.266	1.00	47.32	GZ00	C
ATOM	2587	O	PRO	D	123	12.829	30.182	2.317	1.00	41.78	GZ00	O
ATOM	2588	CB	PRO	D	123	13.356	28.423	−0.505	1.00	53.34	GZ00	C
ATOM	2589	CG	PRO	D	123	14.625	28.122	0.208	1.00	54.44	GZ00	C
ATOM	2590	CD	PRO	D	123	15.402	29.428	0.251	1.00	49.34	GZ00	C
ATOM	2591	N	PRO	D	124	10.968	29.530	1.259	1.00	54.23	GZ00	N
ATOM	2592	CA	PRO	D	124	10.243	29.456	2.533	1.00	49.80	GZ00	C
ATOM	2593	C	PRO	D	124	10.766	28.290	3.353	1.00	47.27	GZ00	C
ATOM	2594	O	PRO	D	124	11.127	27.246	2.809	1.00	40.84	GZ00	O
ATOM	2595	CB	PRO	D	124	8.786	29.239	2.109	1.00	52.85	GZ00	C
ATOM	2596	CG	PRO	D	124	8.882	28.604	0.771	1.00	58.62	GZ00	C
ATOM	2597	CD	PRO	D	124	10.120	29.144	0.117	1.00	50.64	GZ00	C
ATOM	2598	N	SER	D	125	10.848	28.487	4.665	1.00	47.15	GZ00	N
ATOM	2599	CA	SER	D	125	11.315	27.415	5.533	1.00	46.19	GZ00	C
ATOM	2600	C	SER	D	125	10.226	26.360	5.725	1.00	55.91	GZ00	C
ATOM	2601	O	SER	D	125	9.024	26.627	5.602	1.00	48.89	GZ00	O
ATOM	2602	CB	SER	D	125	11.725	27.963	6.895	1.00	46.67	GZ00	C
ATOM	2603	OG	SER	D	125	10.587	28.428	7.610	1.00	43.78	GZ00	O
ATOM	2604	N	SER	D	126	10.661	25.150	6.076	1.00	53.45	GZ00	N
ATOM	2605	CA	SER	D	126	9.697	24.081	6.294	1.00	49.33	GZ00	C
ATOM	2606	C	SER	D	126	8.769	24.420	7.455	1.00	51.40	GZ00	C
ATOM	2607	O	SER	D	126	7.564	24.166	7.392	1.00	57.31	GZ00	O
ATOM	2608	CB	SER	D	126	10.432	22.769	6.528	1.00	46.88	GZ00	C
ATOM	2609	OG	SER	D	126	11.378	22.938	7.552	1.00	58.67	GZ00	O
ATOM	2610	N	GLU	D	127	9.303	25.045	8.500	1.00	46.78	GZ00	N
ATOM	2611	CA	GLU	D	127	8.464	25.457	9.621	1.00	50.81	GZ00	C
ATOM	2612	C	GLU	D	127	7.347	26.393	9.173	1.00	60.09	GZ00	C
ATOM	2613	O	GLU	D	127	6.256	26.382	9.759	1.00	61.69	GZ00	O
ATOM	2614	CB	GLU	D	127	9.329	26.118	10.686	1.00	53.57	GZ00	C
ATOM	2615	CG	GLU	D	127	10.626	25.340	10.894	1.00	62.62	GZ00	C
ATOM	2616	CD	GLU	D	127	11.443	25.816	12.072	1.00	72.05	GZ00	C
ATOM	2617	OE1	GLU	D	127	10.899	26.562	12.933	1.00	69.83	GZ00	O
ATOM	2618	OE2	GLU	D	127	12.635	25.426	12.129	1.00	72.47	GZ00	O1−
ATOM	2619	N	GLU	D	128	7.608	27.240	8.170	1.00	56.85	GZ00	N
ATOM	2620	CA	GLU	D	128	6.568	28.148	7.700	1.00	54.23	GZ00	C
ATOM	2621	C	GLU	D	128	5.590	27.441	6.774	1.00	52.82	GZ00	C
ATOM	2622	O	GLU	D	128	4.390	27.728	6.804	1.00	53.66	GZ00	O
ATOM	2623	CB	GLU	D	128	7.174	29.364	6.983	1.00	52.45	GZ00	C
ATOM	2624	CG	GLU	D	128	6.132	30.482	6.745	1.00	57.44	GZ00	C
ATOM	2625	CD	GLU	D	128	6.545	31.555	5.722	1.00	58.50	GZ00	C
ATOM	2626	OE1	GLU	D	128	5.856	32.590	5.684	1.00	54.07	GZ00	O
ATOM	2627	OE2	GLU	D	128	7.518	31.373	4.950	1.00	49.75	GZ00	O1−
ATOM	2628	N	LEU	D	129	6.095	26.539	5.927	1.00	52.50	GZ00	N
ATOM	2629	CA	LEU	D	129	5.226	25.707	5.104	1.00	51.40	GZ00	C
ATOM	2630	C	LEU	D	129	4.279	24.879	5.969	1.00	59.74	GZ00	C
ATOM	2631	O	LEU	D	129	3.106	24.702	5.623	1.00	63.72	GZ00	O
ATOM	2632	CB	LEU	D	129	6.078	24.807	4.214	1.00	51.65	GZ00	C
ATOM	2633	CG	LEU	D	129	6.868	25.538	3.131	1.00	52.87	GZ00	C
ATOM	2634	CD1	LEU	D	129	7.857	24.604	2.459	1.00	44.54	GZ00	C
ATOM	2635	CD2	LEU	D	129	5.917	26.140	2.101	1.00	49.64	GZ00	C
ATOM	2636	N	GLN	D	130	4.767	24.388	7.115	1.00	54.99	GZ00	N
ATOM	2637	CA	GLN	D	130	3.913	23.640	8.032	1.00	66.06	GZ00	C
ATOM	2638	C	GLN	D	130	2.760	24.489	8.552	1.00	64.20	GZ00	C
ATOM	2639	O	GLN	D	130	1.673	23.958	8.810	1.00	68.64	GZ00	O
ATOM	2640	CB	GLN	D	130	4.729	23.097	9.210	1.00	64.34	GZ00	C
ATOM	2641	CG	GLN	D	130	5.729	22.005	8.863	1.00	65.01	GZ00	C
ATOM	2642	CD	GLN	D	130	6.363	21.409	10.113	1.00	78.91	GZ00	C
ATOM	2643	OE1	GLN	D	130	5.663	21.103	11.083	1.00	88.40	GZ00	O
ATOM	2644	NE2	GLN	D	130	7.691	21.262	10.108	1.00	62.99	GZ00	N
ATOM	2645	N	ALA	D	131	2.972	25.794	8.729	1.00	53.92	GZ00	N
ATOM	2646	CA	ALA	D	131	1.903	26.700	9.129	1.00	51.41	GZ00	C
ATOM	2647	C	ALA	D	131	1.100	27.196	7.943	1.00	56.66	GZ00	C
ATOM	2648	O	ALA	D	131	0.366	28.184	8.075	1.00	63.18	GZ00	O
ATOM	2649	CB	ALA	D	131	2.459	27.889	9.915	1.00	45.31	GZ00	C
ATOM	2650	N	ASN	D	132	1.246	26.543	6.784	1.00	55.73	GZ00	N
ATOM	2651	CA	ASN	D	132	0.472	26.840	5.573	1.00	65.28	GZ00	C
ATOM	2652	C	ASN	D	132	0.645	28.283	5.100	1.00	66.61	GZ00	C
ATOM	2653	O	ASN	D	132	−0.264	28.869	4.507	1.00	68.44	GZ00	O
ATOM	2654	CB	ASN	D	132	−1.018	26.502	5.762	1.00	67.97	GZ00	C
ATOM	2655	CG	ASN	D	132	−1.347	25.065	5.335	1.00	88.31	GZ00	C
ATOM	2656	OD1	ASN	D	132	−1.487	24.776	4.134	1.00	78.43	GZ00	O
ATOM	2657	ND2	ASN	D	132	−1.448	24.155	6.318	1.00	80.50	GZ00	N
ATOM	2658	N	LYS	D	133	1.812	28.866	5.352	1.00	68.70	GZ00	N
ATOM	2659	CA	LYS	D	133	2.244	30.090	4.696	1.00	59.67	GZ00	C
ATOM	2660	C	LYS	D	133	3.522	29.799	3.923	1.00	57.71	GZ00	C
ATOM	2661	O	LYS	D	133	4.135	28.737	4.069	1.00	58.17	GZ00	O
ATOM	2662	CB	LYS	D	133	2.468	31.225	5.701	1.00	52.27	GZ00	C
ATOM	2663	CG	LYS	D	133	1.236	31.650	6.454	1.00	58.15	GZ00	C
ATOM	2664	CD	LYS	D	133	1.590	32.644	7.547	1.00	82.46	GZ00	C
ATOM	2665	CE	LYS	D	133	0.389	32.977	8.428	1.00	90.01	GZ00	C
ATOM	2666	NZ	LYS	D	133	−0.049	31.789	9.221	1.00	85.20	GZ00	N1+
ATOM	2667	N	ALA	D	134	3.923	30.754	3.087	1.00	59.30	GZ00	N
ATOM	2668	CA	ALA	D	134	5.167	30.615	2.328	1.00	57.19	GZ00	C
ATOM	2669	C	ALA	D	134	5.607	31.994	1.872	1.00	56.76	GZ00	C
ATOM	2670	O	ALA	D	134	4.842	32.692	1.196	1.00	55.80	GZ00	O
ATOM	2671	CB	ALA	D	134	4.985	29.678	1.129	1.00	53.33	GZ00	C
ATOM	2672	N	THR	D	135	6.826	32.399	2.238	1.00	51.12	GZ00	N
ATOM	2673	CA	THR	D	135	7.368	33.652	1.730	1.00	46.27	GZ00	C
ATOM	2674	C	THR	D	135	8.764	33.429	1.168	1.00	50.06	GZ00	C
ATOM	2675	O	THR	D	135	9.604	32.783	1.803	1.00	41.99	GZ00	O
ATOM	2676	CB	THR	D	135	7.422	34.735	2.803	1.00	43.17	GZ00	C
ATOM	2677	OG1	THR	D	135	8.619	34.572	3.555	1.00	70.40	GZ00	O
ATOM	2678	CG2	THR	D	135	6.270	34.632	3.735	1.00	40.85	GZ00	C
ATOM	2679	N	LEU	D	136	9.002	33.964	−0.025	1.00	49.86	GZ00	N
ATOM	2680	CA	LEU	D	136	10.344	34.047	−0.574	1.00	43.03	GZ00	C
ATOM	2681	C	LEU	D	136	10.956	35.371	−0.127	1.00	44.71	GZ00	C
ATOM	2682	O	LEU	D	136	10.274	36.400	−0.088	1.00	45.54	GZ00	O
ATOM	2683	CB	LEU	D	136	10.328	33.951	−2.101	1.00	48.82	GZ00	C
ATOM	2684	CG	LEU	D	136	9.744	32.685	−2.734	1.00	50.57	GZ00	C
ATOM	2685	CD1	LEU	D	136	9.722	32.777	−4.241	1.00	43.90	GZ00	C
ATOM	2686	CD2	LEU	D	136	10.592	31.534	−2.313	1.00	54.51	GZ00	C
ATOM	2687	N	VAL	D	137	12.231	35.329	0.251	1.00	38.61	GZ00	N
ATOM	2688	CA	VAL	D	137	12.914	36.459	0.867	1.00	39.76	GZ00	C
ATOM	2689	C	VAL	D	137	14.144	36.781	0.037	1.00	43.30	GZ00	C
ATOM	2690	O	VAL	D	137	15.046	35.946	−0.086	1.00	43.19	GZ00	O
ATOM	2691	CB	VAL	D	137	13.286	36.167	2.326	1.00	40.83	GZ00	C
ATOM	2692	CG1	VAL	D	137	13.930	37.386	2.954	1.00	40.34	GZ00	C
ATOM	2693	CG2	VAL	D	137	12.032	35.756	3.116	1.00	39.27	GZ00	C
ATOM	2694	N	CYS	D	138	14.161	37.969	−0.563	1.00	39.42	GZ00	N
ATOM	2695	CA	CYS	D	138	15.270	38.436	−1.392	1.00	38.06	GZ00	C
ATOM	2696	C	CYS	D	138	15.958	39.590	−0.669	1.00	42.98	GZ00	C
ATOM	2697	O	CYS	D	138	15.379	40.679	−0.549	1.00	42.34	GZ00	O
ATOM	2698	CB	CYS	D	138	14.764	38.869	−2.767	1.00	46.28	GZ00	C
ATOM	2699	SG	CYS	D	138	16.005	39.055	−4.058	1.00	46.59	GZ00	S
ATOM	2700	N	LEU	D	139	17.165	39.345	−0.149	1.00	35.86	GZ00	N
ATOM	2701	CA	LEU	D	139	17.953	40.386	0.503	1.00	34.94	GZ00	C
ATOM	2702	C	LEU	D	139	18.994	40.946	−0.456	1.00	40.09	GZ00	C
ATOM	2703	O	LEU	D	139	19.692	40.198	−1.153	1.00	38.00	GZ00	O
ATOM	2704	CB	LEU	D	139	18.641	39.914	1.784	1.00	38.60	GZ00	C
ATOM	2705	CG	LEU	D	139	17.851	39.429	2.994	1.00	42.05	GZ00	C
ATOM	2706	CD1	LEU	D	139	16.412	39.996	2.992	1.00	34.31	GZ00	C
ATOM	2707	CD2	LEU	D	139	17.888	37.954	3.110	1.00	41.56	GZ00	C
ATOM	2708	N	ILE	D	140	19.072	42.271	−0.498	1.00	36.85	GZ00	N
ATOM	2709	CA	ILE	D	140	19.852	42.991	−1.490	1.00	40.84	GZ00	C
ATOM	2710	C	ILE	D	140	20.717	43.982	−0.735	1.00	39.30	GZ00	C
ATOM	2711	O	ILE	D	140	20.196	44.821	0.012	1.00	36.82	GZ00	O
ATOM	2712	CB	ILE	D	140	18.946	43.703	−2.510	1.00	36.07	GZ00	C
ATOM	2713	CG1	ILE	D	140	17.852	42.738	−2.998	1.00	41.84	GZ00	C
ATOM	2714	CG2	ILE	D	140	19.749	44.191	−3.673	1.00	33.32	GZ00	C
ATOM	2715	CD1	ILE	D	140	16.606	43.414	−3.540	1.00	40.09	GZ00	C
ATOM	2716	N	SER	D	141	22.028	43.899	−0.928	1.00	33.24	GZ00	N
ATOM	2717	CA	SER	D	141	22.918	44.678	−0.083	1.00	40.45	GZ00	C
ATOM	2718	C	SER	D	141	24.146	45.120	−0.865	1.00	40.51	GZ00	C
ATOM	2719	O	SER	D	141	24.453	44.592	−1.948	1.00	33.29	GZ00	O
ATOM	2720	CB	SER	D	141	23.348	43.878	1.155	1.00	39.86	GZ00	C
ATOM	2721	OG	SER	D	141	23.964	42.664	0.748	1.00	40.92	GZ00	O
ATOM	2722	N	ASP	D	142	24.835	46.117	−0.288	1.00	34.55	GZ00	N
ATOM	2723	CA	ASP	D	142	26.137	46.573	−0.776	1.00	45.39	GZ00	C
ATOM	2724	C	ASP	D	142	26.059	47.148	−2.192	1.00	42.72	GZ00	C
ATOM	2725	O	ASP	D	142	26.985	46.983	−2.988	1.00	37.05	GZ00	O
ATOM	2726	CB	ASP	D	142	27.165	45.436	−0.742	1.00	42.27	GZ00	C
ATOM	2727	CG	ASP	D	142	27.636	45.114	0.650	1.00	45.03	GZ00	C
ATOM	2728	OD1	ASP	D	142	27.734	46.043	1.489	1.00	49.79	GZ00	O
ATOM	2729	OD2	ASP	D	142	27.890	43.921	0.902	1.00	52.25	GZ00	O1−
ATOM	2730	N	PHE	D	143	24.967	47.826	−2.529	1.00	33.33	GZ00	N
ATOM	2731	CA	PHE	D	143	24.908	48.407	−3.858	1.00	35.29	GZ00	C
ATOM	2732	C	PHE	D	143	25.067	49.921	−3.775	1.00	33.78	GZ00	C
ATOM	2733	O	PHE	D	143	24.717	50.556	−2.773	1.00	36.42	GZ00	O
ATOM	2734	CB	PHE	D	143	23.637	48.009	−4.617	1.00	34.97	GZ00	C
ATOM	2735	CG	PHE	D	143	22.340	48.333	−3.911	1.00	35.61	GZ00	C
ATOM	2736	CD1	PHE	D	143	21.712	49.549	−4.113	1.00	32.64	GZ00	C
ATOM	2737	CD2	PHE	D	143	21.709	47.379	−3.112	1.00	38.53	GZ00	C
ATOM	2738	CE1	PHE	D	143	20.485	49.834	−3.493	1.00	41.16	GZ00	C
ATOM	2739	CE2	PHE	D	143	20.494	47.658	−2.486	1.00	40.15	GZ00	C
ATOM	2740	CZ	PHE	D	143	19.880	48.890	−2.672	1.00	32.95	GZ00	C
ATOM	2741	N	TYR	D	144	25.665	50.471	−4.824	1.00	35.76	GZ00	N
ATOM	2742	CA	TYR	D	144	26.002	51.882	−4.906	1.00	37.17	GZ00	C
ATOM	2743	C	TYR	D	144	26.142	52.286	−6.363	1.00	41.07	GZ00	C
ATOM	2744	O	TYR	D	144	26.899	51.649	−7.096	1.00	40.05	GZ00	O
ATOM	2745	CB	TYR	D	144	27.305	52.176	−4.182	1.00	31.07	GZ00	C
ATOM	2746	CG	TYR	D	144	27.652	53.644	−4.148	1.00	33.84	GZ00	C
ATOM	2747	CD1	TYR	D	144	27.125	54.478	−3.168	1.00	34.22	GZ00	C
ATOM	2748	CD2	TYR	D	144	28.485	54.207	−5.107	1.00	34.49	GZ00	C
ATOM	2749	CE1	TYR	D	144	27.433	55.822	−3.129	1.00	36.40	GZ00	C
ATOM	2750	CE2	TYR	D	144	28.800	55.559	−5.076	1.00	35.36	GZ00	C
ATOM	2751	CZ	TYR	D	144	28.271	56.358	−4.082	1.00	35.95	GZ00	C
ATOM	2752	OH	TYR	D	144	28.578	57.699	−4.037	1.00	40.59	GZ00	O
ATOM	2753	N	PRO	D	145	25.442	53.357	−6.782	1.00	35.13	GZ00	N
ATOM	2754	CA	PRO	D	145	24.556	54.168	−5.930	1.00	41.08	GZ00	C
ATOM	2755	C	PRO	D	145	23.258	53.476	−5.465	1.00	39.60	GZ00	C
ATOM	2756	O	PRO	D	145	22.944	52.359	−5.874	1.00	35.16	GZ00	O
ATOM	2757	CB	PRO	D	145	24.231	55.395	−6.811	1.00	40.78	GZ00	C
ATOM	2758	CG	PRO	D	145	24.659	55.048	−8.190	1.00	39.08	GZ00	C
ATOM	2759	CD	PRO	D	145	25.708	53.989	−8.088	1.00	36.76	GZ00	C
ATOM	2760	N	GLY	D	146	22.514	54.161	−4.600	1.00	34.87	GZ00	N
ATOM	2761	CA	GLY	D	146	21.429	53.525	−3.892	1.00	34.83	GZ00	C
ATOM	2762	C	GLY	D	146	20.087	53.444	−4.593	1.00	36.93	GZ00	C
ATOM	2763	O	GLY	D	146	19.088	53.931	−4.062	1.00	34.26	GZ00	O
ATOM	2764	N	ALA	D	147	20.037	52.844	−5.777	1.00	32.90	GZ00	N
ATOM	2765	CA	ALA	D	147	18.750	52.609	−6.410	1.00	32.84	GZ00	C
ATOM	2766	C	ALA	D	147	18.802	51.314	−7.178	1.00	32.60	GZ00	C
ATOM	2767	O	ALA	D	147	19.792	51.008	−7.841	1.00	39.02	GZ00	O
ATOM	2768	CB	ALA	D	147	18.326	53.719	−7.365	1.00	29.65	GZ00	C
ATOM	2769	N	VAL	D	148	17.684	50.603	−7.141	1.00	33.58	GZ00	N
ATOM	2770	CA	VAL	D	148	17.588	49.253	−7.651	1.00	34.66	GZ00	C
ATOM	2771	C	VAL	D	148	16.121	49.045	−7.985	1.00	41.83	GZ00	C
ATOM	2772	O	VAL	D	148	15.247	49.684	−7.396	1.00	32.66	GZ00	O
ATOM	2773	CB	VAL	D	148	18.126	48.264	−6.582	1.00	38.73	GZ00	C
ATOM	2774	CG1	VAL	D	148	17.030	47.484	−5.915	1.00	37.24	GZ00	C
ATOM	2775	CG2	VAL	D	148	19.218	47.381	−7.146	1.00	41.31	GZ00	C
ATOM	2776	N	THR	D	149	15.845	48.198	−8.967	1.00	38.40	GZ00	N
ATOM	2777	CA	THR	D	149	14.472	47.753	−9.182	1.00	44.38	GZ00	C
ATOM	2778	C	THR	D	149	14.427	46.229	−9.138	1.00	46.22	GZ00	C
ATOM	2779	O	THR	D	149	15.385	45.556	−9.546	1.00	43.23	GZ00	O
ATOM	2780	CB	THR	D	149	13.899	48.266	−10.513	1.00	46.92	GZ00	C
ATOM	2781	OG1	THR	D	149	14.727	47.815	−11.599	1.00	50.51	GZ00	O
ATOM	2782	CG2	THR	D	149	13.810	49.796	−10.512	1.00	38.30	GZ00	C
ATOM	2783	N	VAL	D	150	13.311	45.686	−8.642	1.00	36.64	GZ00	N
ATOM	2784	CA	VAL	D	150	13.203	44.262	−8.355	1.00	39.12	GZ00	C
ATOM	2785	C	VAL	D	150	12.046	43.662	−9.128	1.00	38.75	GZ00	C
ATOM	2786	O	VAL	D	150	10.920	44.160	−9.054	1.00	46.61	GZ00	O
ATOM	2787	CB	VAL	D	150	13.032	43.987	−6.853	1.00	39.37	GZ00	C
ATOM	2788	CG1	VAL	D	150	12.929	42.488	−6.631	1.00	41.26	GZ00	C
ATOM	2789	CG2	VAL	D	150	14.213	44.522	−6.121	1.00	34.76	GZ00	C
ATOM	2790	N	ALA	D	151	12.333	42.596	−9.865	1.00	39.71	GZ00	N
ATOM	2791	CA	ALA	D	151	11.333	41.805	−10.560	1.00	44.18	GZ00	C
ATOM	2792	C	ALA	D	151	11.434	40.350	−10.127	1.00	50.02	GZ00	C
ATOM	2793	O	ALA	D	151	12.534	39.784	−10.032	1.00	47.26	GZ00	O
ATOM	2794	CB	ALA	D	151	11.494	41.895	−12.081	1.00	37.34	GZ00	C
ATOM	2795	N	TRP	D	152	10.276	39.748	−9.889	1.00	47.18	GZ00	N
ATOM	2796	CA	TRP	D	152	10.164	38.343	−9.544	1.00	47.04	GZ00	C
ATOM	2797	C	TRP	D	152	9.629	37.556	−10.731	1.00	49.55	GZ00	C
ATOM	2798	O	TRP	D	152	8.800	38.055	−11.498	1.00	59.75	GZ00	O
ATOM	2799	CB	TRP	D	152	9.248	38.155	−8.345	1.00	41.47	GZ00	C
ATOM	2800	CG	TRP	D	152	9.799	38.641	−7.051	1.00	45.78	GZ00	C
ATOM	2801	CD1	TRP	D	152	9.786	39.918	−6.579	1.00	49.07	GZ00	C
ATOM	2802	CD2	TRP	D	152	10.400	37.837	−6.026	1.00	43.34	GZ00	C
ATOM	2803	NE1	TRP	D	152	10.361	39.967	−5.325	1.00	46.95	GZ00	N
ATOM	2804	CE2	TRP	D	152	10.736	38.700	−4.961	1.00	46.03	GZ00	C
ATOM	2805	CE3	TRP	D	152	10.699	36.468	−5.914	1.00	44.86	GZ00	C
ATOM	2806	CZ2	TRP	D	152	11.364	38.245	−3.792	1.00	48.01	GZ00	C
ATOM	2807	CZ3	TRP	D	152	11.318	36.008	−4.748	1.00	46.08	GZ00	C
ATOM	2808	CH2	TRP	D	152	11.649	36.905	−3.702	1.00	46.48	GZ00	C
ATOM	2809	N	LYS	D	153	10.109	36.330	−10.882	1.00	54.87	GZ00	N
ATOM	2810	CA	LYS	D	153	9.649	35.434	−11.929	1.00	57.27	GZ00	C
ATOM	2811	C	LYS	D	153	9.247	34.090	−11.331	1.00	66.16	GZ00	C
ATOM	2812	O	LYS	D	153	9.884	33.591	−10.396	1.00	64.92	GZ00	O
ATOM	2813	CB	LYS	D	153	10.728	35.247	−12.999	1.00	61.27	GZ00	C
ATOM	2814	CG	LYS	D	153	10.832	36.442	−13.910	1.00	66.71	GZ00	C
ATOM	2815	CD	LYS	D	153	11.805	36.232	−15.044	1.00	71.68	GZ00	C
ATOM	2816	CE	LYS	D	153	11.839	37.483	−15.930	1.00	79.74	GZ00	C
ATOM	2817	NZ	LYS	D	153	12.960	37.469	−16.930	1.00	89.60	GZ00	N1+
ATOM	2818	N	ALA	D	154	8.145	33.543	−11.836	1.00	68.05	GZ00	N
ATOM	2819	CA	ALA	D	154	7.729	32.169	−11.568	1.00	66.27	GZ00	C
ATOM	2820	C	ALA	D	154	7.933	31.392	−12.864	1.00	70.66	GZ00	C
ATOM	2821	O	ALA	D	154	7.229	31.641	−13.848	1.00	74.13	GZ00	O
ATOM	2822	CB	ALA	D	154	6.280	32.108	−11.092	1.00	57.49	GZ00	C
ATOM	2823	N	ASP	D	155	8.892	30.464	−12.866	1.00	69.01	GZ00	N
ATOM	2824	CA	ASP	D	155	9.320	29.751	−14.079	1.00	76.96	GZ00	C
ATOM	2825	C	ASP	D	155	9.440	30.697	−15.267	1.00	78.16	GZ00	C
ATOM	2826	O	ASP	D	155	8.849	30.482	−16.327	1.00	86.27	GZ00	O
ATOM	2827	CB	ASP	D	155	8.342	28.625	−14.445	1.00	79.86	GZ00	C
ATOM	2828	CG	ASP	D	155	8.311	27.503	−13.442	1.00	77.78	GZ00	C
ATOM	2829	OD1	ASP	D	155	9.379	27.134	−12.919	1.00	80.60	GZ00	O1−
ATOM	2830	OD2	ASP	D	155	7.205	26.974	−13.197	1.00	86.69	GZ00	O
ATOM	2831	N	SER	D	156	10.188	31.777	−15.083	1.00	72.25	GZ00	N
ATOM	2832	CA	SER	D	156	10.451	32.741	−16.147	1.00	79.24	GZ00	C
ATOM	2833	C	SER	D	156	9.207	33.506	−16.599	1.00	70.74	GZ00	C
ATOM	2834	O	SER	D	156	9.242	34.141	−17.656	1.00	70.59	GZ00	O
ATOM	2835	CB	SER	D	156	11.103	32.085	−17.366	1.00	79.59	GZ00	C
ATOM	2836	OG	SER	D	156	10.117	31.458	−18.157	1.00	81.93	GZ00	O
ATOM	2837	N	SER	D	157	8.086	33.449	−15.840	1.00	66.95	GZ00	N
ATOM	2838	CA	SER	D	157	6.934	34.326	−16.090	1.00	65.14	GZ00	C
ATOM	2839	C	SER	D	157	6.878	35.425	−15.047	1.00	67.53	GZ00	C
ATOM	2840	O	SER	D	157	7.031	35.145	−13.848	1.00	64.92	GZ00	O
ATOM	2841	CB	SER	D	157	5.624	33.544	−16.060	1.00	63.23	GZ00	C
ATOM	2842	OG	SER	D	157	5.562	32.633	−17.136	1.00	75.81	GZ00	O
ATOM	2843	N	PRO	D	158	6.652	36.670	−15.446	1.00	66.82	GZ00	N
ATOM	2844	CA	PRO	D	158	6.585	37.756	−14.462	1.00	56.39	GZ00	C
ATOM	2845	C	PRO	D	158	5.538	37.504	−13.392	1.00	59.58	GZ00	C
ATOM	2846	O	PRO	D	158	4.450	36.989	−13.660	1.00	66.88	GZ00	O
ATOM	2847	CB	PRO	D	158	6.236	38.986	−15.308	1.00	52.59	GZ00	C
ATOM	2848	CG	PRO	D	158	5.845	38.451	−16.652	1.00	66.17	GZ00	C
ATOM	2849	CD	PRO	D	158	6.585	37.169	−16.824	1.00	63.85	GZ00	C
ATOM	2850	N	VAL	D	159	5.900	37.834	−12.160	1.00	59.53	GZ00	N
ATOM	2851	CA	VAL	D	159	5.012	37.741	−11.012	1.00	57.33	GZ00	C
ATOM	2852	C	VAL	D	159	4.480	39.133	−10.721	1.00	64.87	GZ00	C
ATOM	2853	O	VAL	D	159	5.261	40.073	−10.535	1.00	75.66	GZ00	O
ATOM	2854	CB	VAL	D	159	5.735	37.169	−9.785	1.00	58.46	GZ00	C
ATOM	2855	CG1	VAL	D	159	4.831	37.239	−8.567	1.00	61.48	GZ00	C
ATOM	2856	CG2	VAL	D	159	6.174	35.737	−10.050	1.00	55.69	GZ00	C
ATOM	2857	N	LYS	D	160	3.157	39.269	−10.654	1.00	74.88	GZ00	N
ATOM	2858	CA	LYS	D	160	2.552	40.558	−10.329	1.00	76.06	GZ00	C
ATOM	2859	C	LYS	D	160	2.274	40.696	−8.831	1.00	82.77	GZ00	C
ATOM	2860	O	LYS	D	160	2.850	41.565	−8.160	1.00	78.66	GZ00	O
ATOM	2861	CB	LYS	D	160	1.265	40.755	−11.142	1.00	83.14	GZ00	C
ATOM	2862	CG	LYS	D	160	1.460	41.529	−12.445	1.00	91.80	GZ00	C
ATOM	2863	CD	LYS	D	160	2.006	42.934	−12.175	1.00	100.07	GZ00	C
ATOM	2864	CE	LYS	D	160	1.058	43.758	−11.302	1.00	96.51	GZ00	C
ATOM	2865	NZ	LYS	D	160	1.729	44.973	−10.750	1.00	94.46	GZ00	N1+
ATOM	2866	N	ALA	D	161	1.410	39.836	−8.293	1.00	72.49	GZ00	N
ATOM	2867	CA	ALA	D	161	0.885	40.022	−6.947	1.00	69.27	GZ00	C
ATOM	2868	C	ALA	D	161	1.739	39.312	−5.903	1.00	63.52	GZ00	C
ATOM	2869	O	ALA	D	161	2.490	38.379	−6.201	1.00	56.61	GZ00	O
ATOM	2870	CB	ALA	D	161	−0.551	39.514	−6.859	1.00	71.61	GZ00	C
ATOM	2871	N	GLY	D	162	1.608	39.774	−4.659	1.00	50.21	GZ00	N
ATOM	2872	CA	GLY	D	162	2.313	39.191	−3.536	1.00	58.65	GZ00	C
ATOM	2873	C	GLY	D	162	3.711	39.714	−3.291	1.00	57.47	GZ00	C
ATOM	2874	O	GLY	D	162	4.417	39.167	−2.426	1.00	54.30	GZ00	O
ATOM	2875	N	VAL	D	163	4.135	40.745	−4.023	1.00	51.81	GZ00	N
ATOM	2876	CA	VAL	D	163	5.480	41.291	−3.929	1.00	45.48	GZ00	C
ATOM	2877	C	VAL	D	163	5.431	42.543	−3.074	1.00	47.42	GZ00	C
ATOM	2878	O	VAL	D	163	4.618	43.442	−3.316	1.00	44.17	GZ00	O
ATOM	2879	CB	VAL	D	163	6.060	41.604	−5.319	1.00	46.37	GZ00	C
ATOM	2880	CG1	VAL	D	163	7.423	42.278	−5.184	1.00	50.48	GZ00	C
ATOM	2881	CG2	VAL	D	163	6.183	40.338	−6.140	1.00	47.00	GZ00	C
ATOM	2882	N	GLU	D	164	6.301	42.609	−2.076	1.00	45.49	GZ00	N
ATOM	2883	CA	GLU	D	164	6.498	43.832	−1.326	1.00	39.71	GZ00	C
ATOM	2884	C	GLU	D	164	7.990	44.067	−1.169	1.00	48.75	GZ00	C
ATOM	2885	O	GLU	D	164	8.749	43.133	−0.864	1.00	44.83	GZ00	O
ATOM	2886	CB	GLU	D	164	5.764	43.793	0.009	1.00	46.37	GZ00	C
ATOM	2887	CG	GLU	D	164	4.308	44.218	−0.195	1.00	59.54	GZ00	C
ATOM	2888	CD	GLU	D	164	3.415	43.931	0.978	1.00	60.43	GZ00	C
ATOM	2889	OE1	GLU	D	164	3.928	43.465	2.015	1.00	70.95	GZ00	O
ATOM	2890	OE2	GLU	D	164	2.197	44.189	0.869	1.00	56.32	GZ00	O1−
ATOM	2891	N	THR	D	165	8.400	45.308	−1.434	1.00	43.26	GZ00	N
ATOM	2892	CA	THR	D	165	9.794	45.691	−1.572	1.00	34.34	GZ00	C
ATOM	2893	C	THR	D	165	10.043	46.955	−0.778	1.00	37.84	GZ00	C
ATOM	2894	O	THR	D	165	9.267	47.903	−0.883	1.00	43.88	GZ00	O
ATOM	2895	CB	THR	D	165	10.122	45.903	−3.040	1.00	37.47	GZ00	C
ATOM	2896	OG1	THR	D	165	9.909	44.671	−3.730	1.00	39.61	GZ00	O
ATOM	2897	CG2	THR	D	165	11.578	46.354	−3.240	1.00	38.05	GZ00	C
ATOM	2898	N	THR	D	166	11.131	46.982	−0.011	1.00	37.74	GZ00	N
ATOM	2899	CA	THR	D	166	11.464	48.177	0.757	1.00	47.21	GZ00	C
ATOM	2900	C	THR	D	166	12.099	49.231	−0.141	1.00	40.41	GZ00	C
ATOM	2901	O	THR	D	166	12.548	48.951	−1.256	1.00	41.42	GZ00	O
ATOM	2902	CB	THR	D	166	12.470	47.888	1.882	1.00	40.73	GZ00	C
ATOM	2903	OG1	THR	D	166	13.677	47.375	1.311	1.00	36.35	GZ00	O
ATOM	2904	CG2	THR	D	166	11.922	46.878	2.882	1.00	40.85	GZ00	C
ATOM	2905	N	THR	D	167	12.135	50.451	0.365	1.00	42.55	GZ00	N
ATOM	2906	CA	THR	D	167	12.976	51.467	−0.237	1.00	49.39	GZ00	C
ATOM	2907	C	THR	D	167	14.429	51.231	0.164	1.00	47.70	GZ00	C
ATOM	2908	O	THR	D	167	14.702	50.656	1.218	1.00	50.42	GZ00	O
ATOM	2909	CB	THR	D	167	12.564	52.846	0.231	1.00	42.03	GZ00	C
ATOM	2910	OG1	THR	D	167	12.784	52.916	1.640	1.00	55.83	GZ00	O
ATOM	2911	CG2	THR	D	167	11.133	53.079	−0.052	1.00	40.08	GZ00	C
ATOM	2912	N	PRO	D	168	15.383	51.666	−0.647	1.00	50.17	GZ00	N
ATOM	2913	CA	PRO	D	168	16.789	51.463	−0.271	1.00	46.73	GZ00	C
ATOM	2914	C	PRO	D	168	17.132	52.312	0.943	1.00	48.10	GZ00	C
ATOM	2915	O	PRO	D	168	16.592	53.405	1.140	1.00	47.07	GZ00	O
ATOM	2916	CB	PRO	D	168	17.572	51.906	−1.515	1.00	44.24	GZ00	C
ATOM	2917	CG	PRO	D	168	16.579	52.648	−2.378	1.00	51.68	GZ00	C
ATOM	2918	CD	PRO	D	168	15.216	52.134	−2.030	1.00	42.84	GZ00	C
ATOM	2919	N	SER	D	169	18.006	51.773	1.789	1.00	38.56	GZ00	N
ATOM	2920	CA	SER	D	169	18.460	52.490	2.976	1.00	44.06	GZ00	C
ATOM	2921	C	SER	D	169	19.974	52.364	3.091	1.00	40.12	GZ00	C
ATOM	2922	O	SER	D	169	20.562	51.347	2.703	1.00	42.12	GZ00	O
ATOM	2923	CB	SER	D	169	17.776	51.973	4.261	1.00	37.35	GZ00	C
ATOM	2924	OG	SER	D	169	18.098	50.608	4.455	1.00	51.17	GZ00	O
ATOM	2925	N	LYS	D	170	20.601	53.409	3.614	1.00	38.28	GZ00	N
ATOM	2926	CA	LYS	D	170	22.053	53.472	3.624	1.00	42.03	GZ00	C
ATOM	2927	C	LYS	D	170	22.610	52.541	4.691	1.00	41.78	GZ00	C
ATOM	2928	O	LYS	D	170	22.160	52.564	5.839	1.00	44.51	GZ00	O
ATOM	2929	CB	LYS	D	170	22.542	54.897	3.877	1.00	38.33	GZ00	C
ATOM	2930	CG	LYS	D	170	24.014	55.068	3.482	1.00	45.43	GZ00	C
ATOM	2931	CD	LYS	D	170	24.575	56.405	3.934	1.00	48.05	GZ00	C
ATOM	2932	CE	LYS	D	170	23.962	57.548	3.176	1.00	54.50	GZ00	C
ATOM	2933	NZ	LYS	D	170	24.635	58.806	3.569	1.00	69.11	GZ00	N1+
ATOM	2934	N	GLN	D	171	23.589	51.723	4.305	1.00	41.93	GZ00	N
ATOM	2935	CA	GLN	D	171	24.346	50.889	5.228	1.00	47.20	GZ00	C
ATOM	2936	C	GLN	D	171	25.483	51.692	5.858	1.00	45.26	GZ00	C
ATOM	2937	O	GLN	D	171	25.816	52.797	5.422	1.00	47.74	GZ00	O
ATOM	2938	CB	GLN	D	171	24.933	49.672	4.508	1.00	38.79	GZ00	C
ATOM	2939	CG	GLN	D	171	23.914	48.809	3.823	1.00	38.60	GZ00	C
ATOM	2940	CD	GLN	D	171	24.560	47.787	2.932	1.00	45.79	GZ00	C
ATOM	2941	OE1	GLN	D	171	23.900	46.859	2.433	1.00	43.80	GZ00	O
ATOM	2942	NE2	GLN	D	171	25.868	47.942	2.715	1.00	45.31	GZ00	N
ATOM	2943	N	SER	D	172	26.118	51.089	6.865	1.00	49.48	GZ00	N
ATOM	2944	CA	SER	D	172	27.258	51.724	7.529	1.00	45.76	GZ00	C
ATOM	2945	C	SER	D	172	28.391	52.012	6.557	1.00	43.14	GZ00	C
ATOM	2946	O	SER	D	172	29.073	53.033	6.675	1.00	51.69	GZ00	O
ATOM	2947	CB	SER	D	172	27.769	50.826	8.658	1.00	55.56	GZ00	C
ATOM	2948	OG	SER	D	172	26.906	50.898	9.777	1.00	71.74	GZ00	O
ATOM	2949	N	ASN	D	173	28.628	51.122	5.601	1.00	40.90	GZ00	N
ATOM	2950	CA	ASN	D	173	29.697	51.363	4.646	1.00	37.43	GZ00	C
ATOM	2951	C	ASN	D	173	29.304	52.349	3.542	1.00	44.12	GZ00	C
ATOM	2952	O	ASN	D	173	30.080	52.526	2.588	1.00	41.37	GZ00	O
ATOM	2953	CB	ASN	D	173	30.171	50.030	4.038	1.00	41.28	GZ00	C
ATOM	2954	CG	ASN	D	173	29.139	49.370	3.147	1.00	44.26	GZ00	C
ATOM	2955	OD1	ASN	D	173	28.038	49.887	2.944	1.00	43.64	GZ00	O
ATOM	2956	ND2	ASN	D	173	29.500	48.208	2.597	1.00	50.50	GZ00	N
ATOM	2957	N	ASN	D	174	28.142	52.999	3.669	1.00	41.55	GZ00	N
ATOM	2958	CA	ASN	D	174	27.608	54.005	2.759	1.00	44.88	GZ00	C
ATOM	2959	C	ASN	D	174	27.151	53.429	1.426	1.00	44.23	GZ00	C
ATOM	2960	O	ASN	D	174	26.811	54.200	0.525	1.00	39.27	GZ00	O
ATOM	2961	CB	ASN	D	174	28.610	55.139	2.484	1.00	42.38	GZ00	C
ATOM	2962	CG	ASN	D	174	28.741	56.082	3.653	1.00	45.60	GZ00	C
ATOM	2963	OD1	ASN	D	174	27.827	56.220	4.457	1.00	52.29	GZ00	O
ATOM	2964	ND2	ASN	D	174	29.895	56.706	3.775	1.00	48.22	GZ00	N
ATOM	2965	N	LYS	D	175	27.187	52.114	1.242	1.00	43.55	GZ00	N
ATOM	2966	CA	LYS	D	175	26.380	51.487	0.204	1.00	46.60	GZ00	C
ATOM	2967	C	LYS	D	175	24.958	51.250	0.748	1.00	40.26	GZ00	C
ATOM	2968	O	LYS	D	175	24.628	51.624	1.877	1.00	36.35	GZ00	O
ATOM	2969	CB	LYS	D	175	27.054	50.204	−0.272	1.00	43.68	GZ00	C
ATOM	2970	CG	LYS	D	175	28.501	50.379	−0.772	1.00	42.53	GZ00	C
ATOM	2971	CD	LYS	D	175	29.043	48.983	−1.135	1.00	47.00	GZ00	C
ATOM	2972	CE	LYS	D	175	30.522	48.940	−1.403	1.00	54.60	GZ00	C
ATOM	2973	NZ	LYS	D	175	30.884	47.568	−1.857	1.00	65.92	GZ00	N
ATOM	2974	N	TYR	D	176	24.091	50.623	−0.042	1.00	37.23	GZ00	N
ATOM	2975	CA	TYR	D	176	22.676	50.583	0.302	1.00	36.34	GZ00	C
ATOM	2976	C	TYR	D	176	22.145	49.158	0.349	1.00	42.73	GZ00	C
ATOM	2977	O	TYR	D	176	22.657	48.244	−0.314	1.00	36.34	GZ00	O
ATOM	2978	CB	TYR	D	176	21.844	51.409	−0.693	1.00	36.80	GZ00	C
ATOM	2979	CG	TYR	D	176	22.044	52.899	−0.563	1.00	36.36	GZ00	C
ATOM	2980	CD2	TYR	D	176	21.057	53.710	−0.021	1.00	37.31	GZ00	C
ATOM	2981	CD1	TYR	D	176	23.222	53.497	−0.996	1.00	41.41	GZ00	C
ATOM	2982	CE2	TYR	D	176	21.252	55.072	0.098	1.00	40.59	GZ00	C
ATOM	2983	CE1	TYR	D	176	23.423	54.857	−0.883	1.00	39.52	GZ00	C
ATOM	2984	CZ	TYR	D	176	22.440	55.639	−0.347	1.00	39.72	GZ00	C
ATOM	2985	OH	TYR	D	176	22.662	56.981	−0.238	1.00	49.13	GZ00	O
ATOM	2986	N	ALA	D	177	21.056	49.003	1.103	1.00	41.16	GZ00	N
ATOM	2987	CA	ALA	D	177	20.371	47.728	1.246	1.00	39.60	GZ00	C
ATOM	2988	C	ALA	D	177	18.886	47.901	0.957	1.00	37.33	GZ00	C
ATOM	2989	O	ALA	D	177	18.321	48.987	1.140	1.00	41.92	GZ00	O
ATOM	2990	CB	ALA	D	177	20.552	47.133	2.665	1.00	35.41	GZ00	C
ATOM	2991	N	ALA	D	178	18.271	46.809	0.488	1.00	36.97	GZ00	N
ATOM	2992	CA	ALA	D	178	16.829	46.711	0.308	1.00	39.14	GZ00	C
ATOM	2993	C	ALA	D	178	16.415	45.246	0.381	1.00	41.15	GZ00	C
ATOM	2994	O	ALA	D	178	17.230	44.339	0.192	1.00	38.19	GZ00	O
ATOM	2995	CB	ALA	D	178	16.380	47.324	−1.023	1.00	31.46	GZ00	C
ATOM	2996	N	SER	D	179	15.125	45.012	0.628	1.00	39.23	GZ00	N
ATOM	2997	CA	SER	D	179	14.626	43.644	0.607	1.00	42.89	GZ00	C
ATOM	2998	C	SER	D	179	13.279	43.569	−0.100	1.00	42.30	GZ00	C
ATOM	2999	O	SER	D	179	12.526	44.543	−0.157	1.00	39.32	GZ00	O
ATOM	3000	CB	SER	D	179	14.561	43.043	2.026	1.00	37.57	GZ00	C
ATOM	3001	OG	SER	D	179	14.059	43.953	2.960	1.00	39.68	GZ00	O
ATOM	3002	N	SER	D	180	13.012	42.399	−0.673	1.00	39.99	GZ00	N
ATOM	3003	CA	SER	D	180	11.786	42.133	−1.407	1.00	45.51	GZ00	C
ATOM	3004	C	SER	D	180	11.212	40.781	−0.972	1.00	51.71	GZ00	C
ATOM	3005	O	SER	D	180	11.932	39.774	−0.921	1.00	43.37	GZ00	O
ATOM	3006	CB	SER	D	180	12.062	42.153	−2.911	1.00	42.12	GZ00	C
ATOM	3007	OG	SER	D	180	10.869	42.076	−3.655	1.00	40.91	GZ00	O
ATOM	3008	N	TYR	D	181	9.914	40.756	−0.686	1.00	44.23	GZ00	N
ATOM	3009	CA	TYR	D	181	9.237	39.561	−0.206	1.00	45.60	GZ00	C
ATOM	3010	C	TYR	D	181	8.159	39.158	−1.203	1.00	48.02	GZ00	C
ATOM	3011	O	TYR	D	181	7.369	40.001	−1.637	1.00	44.19	GZ00	O
ATOM	3012	CB	TYR	D	181	8.612	39.804	1.164	1.00	39.73	GZ00	C
ATOM	3013	CG	TYR	D	181	9.601	40.149	2.246	1.00	42.39	GZ00	C
ATOM	3014	CD2	TYR	D	181	10.094	39.167	3.100	1.00	35.39	GZ00	C
ATOM	3015	CD1	TYR	D	181	10.050	41.464	2.416	1.00	38.95	GZ00	C
ATOM	3016	CE2	TYR	D	181	11.005	39.477	4.098	1.00	38.77	GZ00	C
ATOM	3017	CE1	TYR	D	181	10.958	41.786	3.414	1.00	42.49	GZ00	C
ATOM	3018	CZ	TYR	D	181	11.437	40.785	4.254	1.00	40.93	GZ00	C
ATOM	3019	OH	TYR	D	181	12.335	41.092	5.250	1.00	36.93	GZ00	O
ATOM	3020	N	LEU	D	182	8.137	37.878	−1.576	1.00	39.63	GZ00	N
ATOM	3021	CA	LEU	D	182	7.075	37.312	−2.399	1.00	48.32	GZ00	C
ATOM	3022	C	LEU	D	182	6.258	36.347	−1.533	1.00	49.68	GZ00	C
ATOM	3023	O	LEU	D	182	6.774	35.321	−1.072	1.00	44.59	GZ00	O
ATOM	3024	CB	LEU	D	182	7.672	36.616	−3.621	1.00	45.93	GZ00	C
ATOM	3025	CG	LEU	D	182	6.711	35.859	−4.540	1.00	54.86	GZ00	C
ATOM	3026	CD1	LEU	D	182	5.643	36.822	−5.050	1.00	49.90	GZ00	C
ATOM	3027	CD2	LEU	D	182	7.467	35.191	−5.703	1.00	43.02	GZ00	C
ATOM	3028	N	SER	D	183	4.992	36.680	−1.295	1.00	52.23	GZ00	N
ATOM	3029	CA	SER	D	183	4.099	35.806	−0.538	1.00	47.98	GZ00	C
ATOM	3030	C	SER	D	183	3.397	34.840	−1.481	1.00	47.04	GZ00	C
ATOM	3031	O	SER	D	183	2.956	35.225	−2.564	1.00	52.72	GZ00	O
ATOM	3032	CB	SER	D	183	3.072	36.608	0.251	1.00	45.88	GZ00	C
ATOM	3033	OG	SER	D	183	3.720	37.533	1.102	1.00	53.76	GZ00	O
ATOM	3034	N	LEU	D	184	3.356	33.574	−1.088	1.00	51.61	GZ00	N
ATOM	3035	CA	LEU	D	184	2.741	32.523	−1.874	1.00	51.65	GZ00	C
ATOM	3036	C	LEU	D	184	1.951	31.621	−0.944	1.00	60.30	GZ00	C
ATOM	3037	O	LEU	D	184	2.089	31.679	0.284	1.00	57.40	GZ00	O
ATOM	3038	CB	LEU	D	184	3.777	31.687	−2.623	1.00	53.86	GZ00	C
ATOM	3039	CG	LEU	D	184	4.672	32.341	−3.654	1.00	51.77	GZ00	C
ATOM	3040	CD1	LEU	D	184	5.638	31.317	−4.213	1.00	50.48	GZ00	C
ATOM	3041	CD2	LEU	D	184	3.803	32.927	−4.738	1.00	58.87	GZ00	C
ATOM	3042	N	THR	D	185	1.097	30.745	−1.569	1.00	63.83	GZ00	N
ATOM	3043	CA	THR	D	185	0.577	29.598	−0.843	1.00	63.50	GZ00	C
ATOM	3044	C	THR	D	185	1.550	28.438	−0.977	1.00	60.27	GZ00	C
ATOM	3045	O	THR	D	185	2.270	28.332	−1.982	1.00	54.12	GZ00	O
ATOM	3046	CB	THR	D	185	−0.782	29.160	−1.397	1.00	58.04	GZ00	C
ATOM	3047	OG1	THR	D	185	−0.611	28.645	−2.727	1.00	62.01	GZ00	O
ATOM	3048	CG2	THR	D	185	−1.765	30.324	−1.417	1.00	49.17	GZ00	C
ATOM	3049	N	PRO	D	186	1.567	27.545	0.008	1.00	56.65	GZ00	N
ATOM	3050	CA	PRO	D	186	2.337	26.307	−0.160	1.00	61.35	GZ00	C
ATOM	3051	C	PRO	D	186	2.054	25.617	−1.484	1.00	70.92	GZ00	C
ATOM	3052	O	PRO	D	186	2.972	25.043	−2.089	1.00	71.62	GZ00	O
ATOM	3053	CB	PRO	D	186	1.893	25.474	1.047	1.00	64.94	GZ00	C
ATOM	3054	CG	PRO	D	186	1.565	26.502	2.095	1.00	56.23	GZ00	C
ATOM	3055	CD	PRO	D	186	0.970	27.657	1.353	1.00	57.72	GZ00	C
ATOM	3056	N	GLU	D	187	0.815	25.725	−1.981	1.00	72.13	GZ00	N
ATOM	3057	CA	GLU	D	187	0.440	25.117	−3.255	1.00	73.38	GZ00	C
ATOM	3058	C	GLU	D	187	1.182	25.782	−4.408	1.00	71.22	GZ00	C
ATOM	3059	O	GLU	D	187	1.817	25.105	−5.229	1.00	67.47	GZ00	O
ATOM	3060	CB	GLU	D	187	−1.074	25.235	−3.473	1.00	72.72	GZ00	C
ATOM	3061	CG	GLU	D	187	−1.909	25.465	−2.206	1.00	73.60	GZ00	C
ATOM	3062	CD	GLU	D	187	−1.655	24.438	−1.114	1.00	91.17	GZ00	C
ATOM	3063	OE1	GLU	D	187	−1.492	23.239	−1.442	1.00	95.11	GZ00	O
ATOM	3064	OE2	GLU	D	187	−1.608	24.842	0.072	1.00	86.41	GZ00	O1−
ATOM	3065	N	GLN	D	188	1.080	27.116	−4.499	1.00	63.92	GZ00	N
ATOM	3066	CA	GLN	D	188	1.803	27.852	−5.532	1.00	67.27	GZ00	C
ATOM	3067	C	GLN	D	188	3.302	27.589	−5.466	1.00	68.44	GZ00	C
ATOM	3068	O	GLN	D	188	3.959	27.448	−6.507	1.00	68.93	GZ00	O
ATOM	3069	CB	GLN	D	188	1.524	29.347	−5.411	1.00	69.32	GZ00	C
ATOM	3070	CG	GLN	D	188	0.092	29.737	−5.677	1.00	64.52	GZ00	C
ATOM	3071	CD	GLN	D	188	−0.225	31.124	−5.174	1.00	74.32	GZ00	C
ATOM	3072	OE1	GLN	D	188	0.362	31.585	−4.199	1.00	75.61	GZ00	O
ATOM	3073	NE2	GLN	D	188	−1.147	31.808	−5.847	1.00	79.67	GZ00	N
ATOM	3074	N	TRP	D	189	3.865	27.522	−4.255	1.00	65.05	GZ00	N
ATOM	3075	CA	TRP	D	189	5.304	27.301	−4.130	1.00	65.52	GZ00	C
ATOM	3076	C	TRP	D	189	5.697	25.960	−4.734	1.00	70.69	GZ00	C
ATOM	3077	O	TRP	D	189	6.669	25.871	−5.497	1.00	69.56	GZ00	O
ATOM	3078	CB	TRP	D	189	5.730	27.397	−2.659	1.00	64.52	GZ00	C
ATOM	3079	CG	TRP	D	189	7.127	26.879	−2.336	1.00	69.67	GZ00	C
ATOM	3080	CD1	TRP	D	189	7.448	25.892	−1.442	1.00	67.82	GZ00	C
ATOM	3081	CD2	TRP	D	189	8.372	27.335	−2.885	1.00	66.64	GZ00	C
ATOM	3082	NE1	TRP	D	189	8.806	25.699	−1.414	1.00	62.01	GZ00	N
ATOM	3083	CE2	TRP	D	189	9.399	26.569	−2.287	1.00	64.99	GZ00	C
ATOM	3084	CE3	TRP	D	189	8.720	28.305	−3.833	1.00	68.36	GZ00	C
ATOM	3085	CZ2	TRP	D	189	10.750	26.753	−2.592	1.00	66.69	GZ00	C
ATOM	3086	CZ3	TRP	D	189	10.067	28.481	−4.146	1.00	68.79	GZ00	C
ATOM	3087	CH2	TRP	D	189	11.064	27.704	−3.527	1.00	63.38	GZ00	C
ATOM	3088	N	LYS	D	190	4.925	24.909	−4.437	1.00	74.93	GZ00	N
ATOM	3089	CA	LYS	D	190	5.269	23.562	−4.875	1.00	74.61	GZ00	C
ATOM	3090	C	LYS	D	190	4.919	23.317	−6.334	1.00	72.06	GZ00	C
ATOM	3091	O	LYS	D	190	5.471	22.395	−6.946	1.00	76.50	GZ00	O
ATOM	3092	CB	LYS	D	190	4.556	22.538	−3.988	1.00	72.08	GZ00	C
ATOM	3093	CG	LYS	D	190	5.012	22.585	−2.539	1.00	73.58	GZ00	C
ATOM	3094	CD	LYS	D	190	4.154	21.723	−1.635	1.00	86.29	GZ00	C
ATOM	3095	CE	LYS	D	190	4.625	21.833	−0.191	1.00	92.57	GZ00	C
ATOM	3096	NZ	LYS	D	190	3.732	21.118	0.762	1.00	99.72	GZ00	N1+
ATOM	3097	N	SER	D	191	4.050	24.142	−6.915	1.00	68.71	GZ00	N
ATOM	3098	CA	SER	D	191	3.582	23.882	−8.272	1.00	73.46	GZ00	C
ATOM	3099	C	SER	D	191	4.650	24.213	−9.315	1.00	72.57	GZ00	C
ATOM	3100	O	SER	D	191	4.878	23.431	−10.244	1.00	79.90	GZ00	O
ATOM	3101	CB	SER	D	191	2.289	24.655	−8.529	1.00	70.09	GZ00	C
ATOM	3102	OG	SER	D	191	2.531	26.044	−8.539	1.00	81.55	GZ00	O
ATOM	3103	N	HIS	D	192	5.313	25.363	−9.190	1.00	72.67	GZ00	N
ATOM	3104	CA	HIS	D	192	6.267	25.792	−10.210	1.00	69.13	GZ00	C
ATOM	3105	C	HIS	D	192	7.641	25.135	−10.038	1.00	66.99	GZ00	C
ATOM	3106	O	HIS	D	192	8.020	24.695	−8.951	1.00	72.31	GZ00	O
ATOM	3107	CB	HIS	D	192	6.420	27.313	−10.199	1.00	72.85	GZ00	C
ATOM	3108	CG	HIS	D	192	5.178	28.049	−10.597	1.00	71.64	GZ00	C
ATOM	3109	ND1	HIS	D	192	4.172	28.355	−9.704	1.00	70.93	GZ00	N
ATOM	3110	CD2	HIS	D	192	4.763	28.504	−11.803	1.00	68.93	GZ00	C
ATOM	3111	CE1	HIS	D	192	3.202	28.990	−10.338	1.00	65.00	GZ00	C
ATOM	3112	NE2	HIS	D	192	3.534	29.089	−11.614	1.00	73.86	GZ00	N
ATOM	3113	N	ARG	D	193	8.390	25.070	−11.148	1.00	64.89	GZ00	N
ATOM	3114	CA	ARG	D	193	9.731	24.476	−11.135	1.00	69.27	GZ00	C
ATOM	3115	C	ARG	D	193	10.705	25.313	−10.313	1.00	67.85	GZ00	C
ATOM	3116	O	ARG	D	193	11.542	24.769	−9.586	1.00	68.86	GZ00	O
ATOM	3117	CB	ARG	D	193	10.269	24.354	−12.565	1.00	71.73	GZ00	C
ATOM	3118	CG	ARG	D	193	9.414	23.557	−13.540	1.00	81.33	GZ00	C
ATOM	3119	CD	ARG	D	193	9.846	23.822	−14.993	1.00	88.10	GZ00	C
ATOM	3120	NE	ARG	D	193	8.722	24.419	−15.728	1.00	99.94	GZ00	N
ATOM	3121	CZ	ARG	D	193	8.814	25.092	−16.875	1.00	101.58	GZ00	C
ATOM	3122	NH1	ARG	D	193	7.716	25.589	−17.441	1.00	88.37	GZ00	N1+
ATOM	3123	NH2	ARG	D	193	9.997	25.305	−17.440	1.00	99.51	GZ00	N
ATOM	3124	N	SER	D	194	10.619	26.637	−10.428	1.00	68.05	GZ00	N
ATOM	3125	CA	SER	D	194	11.553	27.534	−9.768	1.00	62.46	GZ00	C
ATOM	3126	C	SER	D	194	10.936	28.917	−9.658	1.00	66.77	GZ00	C
ATOM	3127	O	SER	D	194	9.957	29.242	−10.334	1.00	71.03	GZ00	O
ATOM	3128	CB	SER	D	194	12.876	27.622	−10.529	1.00	66.04	GZ00	C
ATOM	3129	OG	SER	D	194	12.739	28.441	−11.681	1.00	66.32	GZ00	O
ATOM	3130	N	TYR	D	195	11.520	29.722	−8.782	1.00	64.92	GZ00	N
ATOM	3131	CA	TYR	D	195	11.219	31.142	−8.688	1.00	63.56	GZ00	C
ATOM	3132	C	TYR	D	195	12.522	31.927	−8.748	1.00	61.50	GZ00	C
ATOM	3133	O	TYR	D	195	13.580	31.431	−8.351	1.00	54.93	GZ00	O
ATOM	3134	CB	TYR	D	195	10.481	31.482	−7.408	1.00	57.26	GZ00	C
ATOM	3135	CG	TYR	D	195	9.037	31.058	−7.392	1.00	64.67	GZ00	C
ATOM	3136	CD1	TYR	D	195	8.679	29.742	−7.126	1.00	69.64	GZ00	C
ATOM	3137	CD2	TYR	D	195	8.025	31.986	−7.618	1.00	66.11	GZ00	C
ATOM	3138	CE1	TYR	D	195	7.350	29.362	−7.094	1.00	72.89	GZ00	C
ATOM	3139	CE2	TYR	D	195	6.704	31.621	−7.592	1.00	63.75	GZ00	C
ATOM	3140	CZ	TYR	D	195	6.369	30.311	−7.336	1.00	69.62	GZ00	C
ATOM	3141	OH	TYR	D	195	5.043	29.958	−7.309	1.00	71.41	GZ00	O
ATOM	3142	N	SER	D	196	12.441	33.161	−9.235	1.00	58.30	GZ00	N
ATOM	3143	CA	SER	D	196	13.627	33.990	−9.396	1.00	54.75	GZ00	C
ATOM	3144	C	SER	D	196	13.387	35.383	−8.852	1.00	52.46	GZ00	C
ATOM	3145	O	SER	D	196	12.282	35.924	−8.944	1.00	50.50	GZ00	O
ATOM	3146	CB	SER	D	196	14.068	34.102	−10.856	1.00	55.06	GZ00	C
ATOM	3147	OG	SER	D	196	14.543	32.862	−11.337	1.00	59.56	GZ00	O
ATOM	3148	N	CYS	D	197	14.434	35.941	−8.263	1.00	51.88	GZ00	N
ATOM	3149	CA	CYS	D	197	14.485	37.334	−7.862	1.00	48.95	GZ00	C
ATOM	3150	C	CYS	D	197	15.499	38.031	−8.771	1.00	49.99	GZ00	C
ATOM	3151	O	CYS	D	197	16.667	37.641	−8.809	1.00	46.06	GZ00	O
ATOM	3152	CB	CYS	D	197	14.868	37.443	−6.389	1.00	50.65	GZ00	C
ATOM	3153	SG	CYS	D	197	14.970	39.121	−5.807	1.00	59.52	GZ00	S
ATOM	3154	N	GLN	D	198	15.048	39.021	−9.538	1.00	50.95	GZ00	N
ATOM	3155	CA	GLN	D	198	15.912	39.731	−10.476	1.00	45.62	GZ00	C
ATOM	3156	C	GLN	D	198	16.058	41.165	−10.006	1.00	45.99	GZ00	C
ATOM	3157	O	GLN	D	198	15.064	41.888	−9.860	1.00	43.74	GZ00	O
ATOM	3158	CB	GLN	D	198	15.372	39.667	−11.901	1.00	43.17	GZ00	C
ATOM	3159	CG	GLN	D	198	15.534	38.283	−12.527	1.00	59.20	GZ00	C
ATOM	3160	CD	GLN	D	198	14.770	38.107	−13.837	1.00	67.77	GZ00	C
ATOM	3161	OE1	GLN	D	198	14.034	38.996	−14.273	1.00	68.74	GZ00	O
ATOM	3162	NE2	GLN	D	198	14.933	36.945	−14.460	1.00	69.92	GZ00	N
ATOM	3163	N	VAL	D	199	17.291	41.556	−9.722	1.00	43.86	GZ00	N
ATOM	3164	CA	VAL	D	199	17.600	42.869	−9.177	1.00	43.86	GZ00	C
ATOM	3165	C	VAL	D	199	18.389	43.626	−10.233	1.00	44.40	GZ00	C
ATOM	3166	O	VAL	D	199	19.480	43.197	−10.619	1.00	41.88	GZ00	O
ATOM	3167	CB	VAL	D	199	18.389	42.750	−7.865	1.00	40.13	GZ00	C
ATOM	3168	CG1	VAL	D	199	18.560	44.088	−7.241	1.00	33.53	GZ00	C
ATOM	3169	CG2	VAL	D	199	17.679	41.778	−6.906	1.00	37.93	GZ00	C
ATOM	3170	N	THR	D	200	17.838	44.732	−10.719	1.00	43.84	GZ00	N
ATOM	3171	CA	THR	D	200	18.513	45.558	−11.712	1.00	42.52	GZ00	C
ATOM	3172	C	THR	D	200	19.125	46.783	−11.044	1.00	39.89	GZ00	C
ATOM	3173	O	THR	D	200	18.442	47.506	−10.310	1.00	39.87	GZ00	O
ATOM	3174	CB	THR	D	200	17.542	45.987	−12.813	1.00	48.84	GZ00	C
ATOM	3175	OG1	THR	D	200	16.958	44.805	−13.380	1.00	46.64	GZ00	O
ATOM	3176	CG2	THR	D	200	18.290	46.806	−13.918	1.00	33.12	GZ00	C
ATOM	3177	N	HIS	D	201	20.406	47.016	−11.313	1.00	40.27	GZ00	N
ATOM	3178	CA	HIS	D	201	21.145	48.125	−10.723	1.00	39.47	GZ00	C
ATOM	3179	C	HIS	D	201	22.047	48.723	−11.790	1.00	44.85	GZ00	C
ATOM	3180	O	HIS	D	201	22.892	48.013	−12.345	1.00	39.41	GZ00	O
ATOM	3181	CB	HIS	D	201	21.973	47.660	−9.532	1.00	37.22	GZ00	C
ATOM	3182	CG	HIS	D	201	22.797	48.738	−8.905	1.00	34.72	GZ00	C
ATOM	3183	ND1	HIS	D	201	24.134	48.915	−9.190	1.00	33.61	GZ00	N
ATOM	3184	CD2	HIS	D	201	22.486	49.658	−7.960	1.00	33.33	GZ00	C
ATOM	3185	CE1	HIS	D	201	24.608	49.907	−8.455	1.00	40.99	GZ00	C
ATOM	3186	NE2	HIS	D	201	23.628	50.377	−7.699	1.00	33.68	GZ00	N
ATOM	3187	N	GLU	D	202	21.840	50.010	−12.100	1.00	47.82	GZ00	N
ATOM	3188	CA	GLU	D	202	22.672	50.726	−13.064	1.00	45.90	GZ00	C
ATOM	3189	C	GLU	D	202	22.753	49.963	−14.385	1.00	44.77	GZ00	C
ATOM	3190	O	GLU	D	202	23.828	49.757	−14.947	1.00	45.87	GZ00	O
ATOM	3191	CB	GLU	D	202	24.068	50.973	−12.485	1.00	40.73	GZ00	C
ATOM	3192	CG	GLU	D	202	24.078	51.833	−11.241	1.00	37.51	GZ00	C
ATOM	3193	CD	GLU	D	202	23.780	53.301	−11.543	1.00	53.62	GZ00	C
ATOM	3194	OE1	GLU	D	202	24.472	53.880	−12.414	1.00	54.80	GZ00	O
ATOM	3195	OE2	GLU	D	202	22.853	53.878	−10.924	1.00	56.28	GZ00	O1−
ATOM	3196	N	GLY	D	203	21.600	49.498	−14.862	1.00	40.18	GZ00	N
ATOM	3197	CA	GLY	D	203	21.584	48.775	−16.117	1.00	41.95	GZ00	C
ATOM	3198	C	GLY	D	203	22.137	47.357	−16.110	1.00	51.05	GZ00	C
ATOM	3199	O	GLY	D	203	22.259	46.760	−17.186	1.00	50.18	GZ00	O
ATOM	3200	N	SER	D	206	22.505	46.793	−14.958	1.00	47.41	GZ00	N
ATOM	3201	CA	SER	D	206	22.921	45.390	−14.906	1.00	50.13	GZ00	C
ATOM	3202	C	SER	D	206	22.101	44.640	−13.874	1.00	46.73	GZ00	C
ATOM	3203	O	SER	D	206	21.921	45.117	−12.747	1.00	45.75	GZ00	O
ATOM	3204	CB	SER	D	206	24.404	45.243	−14.607	1.00	46.12	GZ00	C
ATOM	3205	OG	SER	D	206	25.155	45.750	−15.688	1.00	57.53	GZ00	O
ATOM	3206	N	THR	D	207	21.592	43.477	−14.262	1.00	41.69	GZ00	N
ATOM	3207	CA	THR	D	207	20.697	42.720	−13.400	1.00	50.12	GZ00	C
ATOM	3208	C	THR	D	207	21.425	41.525	−12.797	1.00	47.45	GZ00	C
ATOM	3209	O	THR	D	207	22.129	40.793	−13.501	1.00	43.02	GZ00	O
ATOM	3210	CB	THR	D	207	19.449	42.249	−14.155	1.00	49.49	GZ00	C
ATOM	3211	OG1	THR	D	207	19.797	41.130	−14.968	1.00	59.30	GZ00	O
ATOM	3212	CG2	THR	D	207	18.885	43.358	−15.031	1.00	37.86	GZ00	C
ATOM	3213	N	VAL	D	208	21.234	41.328	−11.495	1.00	45.06	GZ00	N
ATOM	3214	CA	VAL	D	208	21.724	40.163	−10.767	1.00	49.03	GZ00	C
ATOM	3215	C	VAL	D	208	20.514	39.301	−10.447	1.00	44.06	GZ00	C
ATOM	3216	O	VAL	D	208	19.493	39.815	−9.974	1.00	50.95	GZ00	O
ATOM	3217	CB	VAL	D	208	22.467	40.579	−9.484	1.00	48.97	GZ00	C
ATOM	3218	CG1	VAL	D	208	22.858	39.372	−8.668	1.00	41.12	GZ00	C
ATOM	3219	CG2	VAL	D	208	23.700	41.376	−9.829	1.00	39.61	GZ00	C
ATOM	3220	N	GLU	D	209	20.614	38.005	−10.709	1.00	41.82	GZ00	N
ATOM	3221	CA	GLU	D	209	19.483	37.103	−10.538	1.00	43.40	GZ00	C
ATOM	3222	C	GLU	D	209	19.835	35.970	−9.586	1.00	50.61	GZ00	C
ATOM	3223	O	GLU	D	209	20.917	35.383	−9.674	1.00	57.28	GZ00	O
ATOM	3224	CB	GLU	D	209	19.042	36.508	−11.873	1.00	49.58	GZ00	C
ATOM	3225	CG	GLU	D	209	17.851	35.561	−11.761	1.00	62.21	GZ00	C
ATOM	3226	CD	GLU	D	209	17.419	34.999	−13.108	1.00	75.52	GZ00	C
ATOM	3227	OE1	GLU	D	209	17.297	33.759	−13.240	1.00	85.24	GZ00	O
ATOM	3228	OE2	GLU	D	209	17.155	35.806	−14.026	1.00	77.80	GZ00	O1−
ATOM	3229	N	LYS	D	210	18.902	35.636	−8.705	1.00	48.46	GZ00	N
ATOM	3230	CA	LYS	D	210	19.006	34.443	−7.885	1.00	52.58	GZ00	C
ATOM	3231	C	LYS	D	210	17.741	33.630	−8.066	1.00	49.39	GZ00	C
ATOM	3232	O	LYS	D	210	16.639	34.182	−8.150	1.00	51.83	GZ00	O
ATOM	3233	CB	LYS	D	210	19.228	34.785	−6.401	1.00	50.40	GZ00	C
ATOM	3234	CG	LYS	D	210	20.608	35.341	−6.116	1.00	46.93	GZ00	C
ATOM	3235	CD	LYS	D	210	21.675	34.454	−6.726	1.00	45.41	GZ00	C
ATOM	3236	CE	LYS	D	210	23.095	35.008	−6.476	1.00	52.18	GZ00	C
ATOM	3237	NZ	LYS	D	210	23.541	34.804	−5.069	1.00	57.98	GZ00	N1+
ATOM	3238	N	THR	D	211	17.900	32.324	−8.168	1.00	47.49	GZ00	N
ATOM	3239	CA	THR	D	211	16.750	31.460	−8.337	1.00	56.28	GZ00	C
ATOM	3240	C	THR	D	211	16.772	30.374	−7.276	1.00	53.77	GZ00	C
ATOM	3241	O	THR	D	211	17.832	29.917	−6.845	1.00	60.67	GZ00	O
ATOM	3242	CB	THR	D	211	16.708	30.815	−9.722	1.00	53.88	GZ00	C
ATOM	3243	OG1	THR	D	211	17.474	29.617	−9.690	1.00	68.57	GZ00	O
ATOM	3244	CG2	THR	D	211	17.315	31.729	−10.774	1.00	54.97	GZ00	C
ATOM	3245	N	VAL	D	212	15.583	29.943	−6.893	1.00	54.81	GZ00	N
ATOM	3246	CA	VAL	D	212	15.393	28.942	−5.858	1.00	54.01	GZ00	C
ATOM	3247	C	VAL	D	212	14.264	28.011	−6.313	1.00	62.68	GZ00	C
ATOM	3248	O	VAL	D	212	13.334	28.429	−7.016	1.00	62.49	GZ00	O
ATOM	3249	CB	VAL	D	212	15.121	29.656	−4.510	1.00	51.80	GZ00	C
ATOM	3250	CG1	VAL	D	212	13.642	30.033	−4.363	1.00	48.35	GZ00	C
ATOM	3251	CG2	VAL	D	212	15.626	28.849	−3.351	1.00	63.22	GZ00	C
ATOM	3252	N	ALA	D	213	14.367	26.729	−5.951	1.00	62.74	GZ00	N
ATOM	3253	CA	ALA	D	213	13.422	25.713	−6.406	1.00	61.72	GZ00	C
ATOM	3254	C	ALA	D	213	12.828	24.959	−5.225	1.00	66.88	GZ00	C
ATOM	3255	O	ALA	D	213	13.502	24.746	−4.213	1.00	69.81	GZ00	O
ATOM	3256	CB	ALA	D	213	14.074	24.712	−7.370	1.00	52.61	GZ00	C
ATOM	3257	N	PRO	D	214	11.554	24.566	−5.318	1.00	71.94	GZ00	N
ATOM	3258	CA	PRO	D	214	10.911	23.880	−4.181	1.00	73.82	GZ00	C
ATOM	3259	C	PRO	D	214	11.485	22.508	−3.872	1.00	83.15	GZ00	C
ATOM	3260	O	PRO	D	214	11.296	22.024	−2.748	1.00	87.02	GZ00	O
ATOM	3261	CB	PRO	D	214	9.437	23.798	−4.599	1.00	71.13	GZ00	C
ATOM	3262	CG	PRO	D	214	9.430	24.016	−6.077	1.00	76.39	GZ00	C
ATOM	3263	CD	PRO	D	214	10.598	24.897	−6.388	1.00	73.27	GZ00	C
ATOM	3264	N	THR	D	215	12.167	21.863	−4.815	1.00	81.47	GZ00	N
ATOM	3265	CA	THR	D	215	12.918	20.647	−4.512	1.00	88.36	GZ00	C
ATOM	3266	C	THR	D	215	14.100	21.003	−3.608	1.00	95.90	GZ00	C
ATOM	3267	O	THR	D	215	15.126	21.513	−4.071	1.00	92.30	GZ00	O
ATOM	3268	CB	THR	D	215	13.383	19.978	−5.802	1.00	93.99	GZ00	C
ATOM	3269	OG1	THR	D	215	14.373	20.797	−6.434	1.00	97.00	GZ00	O
ATOM	3270	CG2	THR	D	215	12.210	19.791	−6.759	1.00	92.11	GZ00	C
ATOM	3271	N	GLU	D	216	13.956	20.757	−2.306	1.00	96.37	GZ00	N
ATOM	3272	CA	GLU	D	216	14.997	21.115	−1.340	1.00	94.49	GZ00	C
ATOM	3273	C	GLU	D	216	15.586	19.863	−0.689	1.00	103.70	GZ00	C
ATOM	3274	O	GLU	D	216	16.586	19.934	0.031	1.00	103.19	GZ00	O
ATOM	3275	CB	GLU	D	216	14.453	22.060	−0.258	1.00	98.63	GZ00	C
ATOM	3276	CG	GLU	D	216	14.051	23.474	−0.741	1.00	99.48	GZ00	C
ATOM	3277	CD	GLU	D	216	13.551	24.375	0.397	1.00	94.82	GZ00	C
ATOM	3278	OE1	GLU	D	216	14.356	24.704	1.304	1.00	90.53	GZ00	O
ATOM	3279	OE2	GLU	D	216	12.349	24.740	0.394	1.00	84.44	GZ00	O1−
TER
ATOM	3280	N	GLN	A	1	−34.534	69.246	−14.750	1.00	68.93		N
ATOM	3281	CA	GLN	A	1	−35.181	70.408	−14.148	1.00	63.15		C
ATOM	3282	C	GLN	A	1	−34.574	70.759	−12.783	1.00	64.87		C
ATOM	3283	O	GLN	A	1	−34.907	70.176	−11.757	1.00	73.80		O
ATOM	3284	CB	GLN	A	1	−36.678	70.168	−14.001	1.00	72.61		C
ATOM	3285	CG	GLN	A	1	−37.438	71.350	−13.425	1.00	79.05		C
ATOM	3286	CD	GLN	A	1	−38.607	70.901	−12.574	1.00	82.55		C
ATOM	3287	OE1	GLN	A	1	−38.585	69.803	−12.013	1.00	76.25		O
ATOM	3288	NE2	GLN	A	1	−39.638	71.743	−12.478	1.00	75.07		N
ATOM	3289	N	VAL	A	2	−33.670	71.708	−12.792	1.00	52.55		N
ATOM	3290	CA	VAL	A	2	−33.090	72.273	−11.587	1.00	39.46		C
ATOM	3291	C	VAL	A	2	−33.760	73.615	−11.340	1.00	37.36		C
ATOM	3292	O	VAL	A	2	−34.051	74.357	−12.286	1.00	42.98		O
ATOM	3293	CB	VAL	A	2	−31.561	72.402	−11.744	1.00	37.95		C
ATOM	3294	CG1	VAL	A	2	−30.942	73.173	−10.605	1.00	32.40		C
ATOM	3295	CG2	VAL	A	2	−30.938	71.007	−11.812	1.00	38.29		C
ATOM	3296	N	GLN	A	3	−34.074	73.905	−10.086	1.00	28.57		N
ATOM	3297	CA	GLN	A	3	−34.530	75.234	−9.705	1.00	36.17		C
ATOM	3298	C	GLN	A	3	−33.616	75.802	−8.623	1.00	32.07		C
ATOM	3299	O	GLN	A	3	−33.291	75.112	−7.650	1.00	33.31		O
ATOM	3300	CB	GLN	A	3	−35.981	75.198	−9.230	1.00	33.26		C
ATOM	3301	CG	GLN	A	3	−36.980	75.166	−10.396	1.00	48.28		C
ATOM	3302	CD	GLN	A	3	−38.422	75.482	−9.975	1.00	66.43		C
ATOM	3303	OE1	GLN	A	3	−38.748	75.535	−8.779	1.00	59.16		O
ATOM	3304	NE2	GLN	A	3	−39.284	75.714	−10.964	1.00	65.91		N
ATOM	3305	N	LEU	A	4	−33.202	77.051	−8.798	1.00	28.83		N
ATOM	3306	CA	LEU	A	4	−32.404	77.779	−7.823	1.00	34.07		C
ATOM	3307	C	LEU	A	4	−33.199	79.004	−7.385	1.00	31.68		C
ATOM	3308	O	LEU	A	4	−33.759	79.699	−8.231	1.00	35.93		O
ATOM	3309	CB	LEU	A	4	−31.054	78.181	−8.431	1.00	31.35		C
ATOM	3310	CG	LEU	A	4	−30.271	77.022	−9.054	1.00	35.66		C
ATOM	3311	CD1	LEU	A	4	−29.061	77.538	−9.848	1.00	33.22		C
ATOM	3312	CD2	LEU	A	4	−29.820	76.024	−7.986	1.00	28.58		C
ATOM	3313	N	VAL	A	5	−33.296	79.236	−6.074	1.00	31.24		N
ATOM	3314	CA	VAL	A	5	−34.075	80.340	−5.501	1.00	29.71		C
ATOM	3315	C	VAL	A	5	−33.192	81.106	−4.521	1.00	30.40		C
ATOM	3316	O	VAL	A	5	−32.883	80.594	−3.439	1.00	34.07		O
ATOM	3317	CB	VAL	A	5	−35.352	79.849	−4.790	1.00	33.16		C
ATOM	3318	CG1	VAL	A	5	−36.116	81.023	−4.194	1.00	22.32		C
ATOM	3319	CG2	VAL	A	5	−36.244	79.088	−5.746	1.00	27.68		C
ATOM	3320	N	GLU	A	6	−32.830	82.344	−4.866	1.00	27.45		N
ATOM	3321	CA	GLU	A	6	−32.039	83.183	−3.970	1.00	34.31		C
ATOM	3322	C	GLU	A	6	−32.938	83.895	−2.964	1.00	35.66		C
ATOM	3323	O	GLU	A	6	−34.094	84.211	−3.250	1.00	35.15		O
ATOM	3324	CB	GLU	A	6	−31.242	84.251	−4.738	1.00	35.33		C
ATOM	3325	CG	GLU	A	6	−30.370	83.745	−5.877	1.00	36.08		C
ATOM	3326	CD	GLU	A	6	−31.115	83.636	−7.209	1.00	39.10		C
ATOM	3327	OE1	GLU	A	6	−32.369	83.508	−7.199	1.00	35.08		O
ATOM	3328	OE2	GLU	A	6	−30.432	83.628	−8.263	1.00	35.04		O1−
ATOM	3329	N	SER	A	7	−32.368	84.204	−1.800	1.00	36.13		N
ATOM	3330	CA	SER	A	7	−33.075	84.945	−0.763	1.00	34.15		C
ATOM	3331	C	SER	A	7	−32.033	85.588	0.132	1.00	31.67		C
ATOM	3332	O	SER	A	7	−30.848	85.263	0.062	1.00	34.14		O
ATOM	3333	CB	SER	A	7	−34.004	84.045	0.060	1.00	29.39		C
ATOM	3334	OG	SER	A	7	−33.246	83.029	0.704	1.00	39.57		O
ATOM	3335	N	GLY	A	8	−32.484	86.520	0.962	1.00	33.72		N
ATOM	3336	CA	GLY	A	8	−31.621	87.148	1.934	1.00	31.16		C
ATOM	3337	C	GLY	A	8	−31.165	88.543	1.590	1.00	40.14		C
ATOM	3338	O	GLY	A	8	−30.323	89.095	2.311	1.00	41.88		O
ATOM	3339	N	GLY	A	9	−31.679	89.131	0.518	1.00	30.46		N
ATOM	3340	CA	GLY	A	9	−31.281	90.478	0.150	1.00	42.56		C
ATOM	3341	C	GLY	A	9	−31.699	91.554	1.150	1.00	45.12		C
ATOM	3342	O	GLY	A	9	−31.989	91.303	2.319	1.00	45.51		O
ATOM	3343	N	GLY	A	10	−31.614	92.794	0.695	1.00	40.16		N
ATOM	3344	CA	GLY	A	10	−32.173	93.880	1.461	1.00	36.55		C
ATOM	3345	C	GLY	A	10	−31.303	95.118	1.379	1.00	41.88		C
ATOM	3346	O	GLY	A	10	−30.334	95.184	0.617	1.00	34.74		O
ATOM	3347	N	VAL	A	11	−31.676	96.112	2.184	1.00	37.50		N
ATOM	3348	CA	VAL	A	11	−30.953	97.369	2.303	1.00	38.58		C
ATOM	3349	C	VAL	A	11	−30.020	97.243	3.493	1.00	43.54		C
ATOM	3350	O	VAL	A	11	−30.423	96.759	4.555	1.00	47.55		O
ATOM	3351	CB	VAL	A	11	−31.911	98.559	2.483	1.00	48.63		C
ATOM	3352	CG1	VAL	A	11	−31.118	99.850	2.585	1.00	43.07		C
ATOM	3353	CG2	VAL	A	11	−32.901	98.626	1.323	1.00	45.11		C
ATOM	3354	N	VAL	A	12	−28.773	97.676	3.324	1.00	36.28		N
ATOM	3355	CA	VAL	A	12	−27.767	97.511	4.364	1.00	44.38		C
ATOM	3356	C	VAL	A	12	−26.802	98.696	4.298	1.00	42.35		C
ATOM	3357	O	VAL	A	12	−26.638	99.336	3.253	1.00	42.56		O
ATOM	3358	CB	VAL	A	12	−27.051	96.138	4.207	1.00	47.04		C
ATOM	3359	CG1	VAL	A	12	−26.272	96.069	2.897	1.00	44.35		C
ATOM	3360	CG2	VAL	A	12	−26.125	95.864	5.359	1.00	49.20		C
ATOM	3361	N	GLN	A	13	−26.197	99.009	5.427	1.00	43.55		N
ATOM	3362	CA	GLN	A	13	−25.312	100.156	5.405	1.00	44.17		C
ATOM	3363	C	GLN	A	13	−23.884	99.743	5.086	1.00	47.16		C
ATOM	3364	O	GLN	A	13	−23.471	98.619	5.399	1.00	45.14		O
ATOM	3365	CB	GLN	A	13	−25.334	100.881	6.734	1.00	45.16		C
ATOM	3366	CG	GLN	A	13	−26.698	101.357	7.135	1.00	59.94		C
ATOM	3367	CD	GLN	A	13	−26.607	102.516	8.099	1.00	69.00		C
ATOM	3368	OE1	GLN	A	13	−26.037	103.566	7.771	1.00	69.47		O
ATOM	3369	NE2	GLN	A	13	−27.151	102.335	9.297	1.00	70.89		N
ATOM	3370	N	PRO	A	14	−23.132	100.657	4.472	1.00	41.71		N
ATOM	3371	CA	PRO	A	14	−21.726	100.372	4.167	1.00	38.64		C
ATOM	3372	C	PRO	A	14	−21.001	99.888	5.411	1.00	41.46		C
ATOM	3373	O	PRO	A	14	−21.225	100.390	6.512	1.00	43.96		O
ATOM	3374	CB	PRO	A	14	−21.191	101.725	3.683	1.00	36.30		C
ATOM	3375	CG	PRO	A	14	−22.417	102.449	3.166	1.00	37.34		C
ATOM	3376	CD	PRO	A	14	−23.553	101.995	4.015	1.00	42.17		C
ATOM	3377	N	GLY	A	15	−20.150	98.877	5.237	1.00	39.52		N
ATOM	3378	CA	GLY	A	15	−19.389	98.318	6.335	1.00	35.94		C
ATOM	3379	C	GLY	A	15	−20.077	97.199	7.088	1.00	40.72		C
ATOM	3380	O	GLY	A	15	−19.407	96.463	7.826	1.00	44.51		O
ATOM	3381	N	ARG	A	16	−21.388	97.045	6.924	1.00	39.84		N
ATOM	3382	CA	ARG	A	16	−22.114	95.953	7.556	1.00	53.52		C
ATOM	3383	C	ARG	A	16	−21.962	94.660	6.746	1.00	46.84		C
ATOM	3384	O	ARG	A	16	−21.259	94.600	5.727	1.00	39.84		O
ATOM	3385	CB	ARG	A	16	−23.592	96.303	7.706	1.00	54.09		C
ATOM	3386	CG	ARG	A	16	−23.880	97.531	8.533	1.00	61.92		C
ATOM	3387	CD	ARG	A	16	−23.430	97.323	9.960	1.00	69.75		C
ATOM	3388	NE	ARG	A	16	−24.436	97.796	10.906	1.00	97.69		N
ATOM	3389	CZ	ARG	A	16	−24.245	97.901	12.218	1.00	105.26		C
ATOM	3390	NH1	ARG	A	16	−23.075	97.566	12.754	1.00	97.15		N1+
ATOM	3391	NH2	ARG	A	16	−25.226	98.346	12.995	1.00	108.93		N
ATOM	3392	N	SER	A	17	−22.664	93.625	7.206	1.00	37.36		N
ATOM	3393	CA	SER	A	17	−22.586	92.271	6.692	1.00	37.19		C
ATOM	3394	C	SER	A	17	−23.962	91.796	6.274	1.00	41.75		C
ATOM	3395	O	SER	A	17	−24.980	92.251	6.795	1.00	39.73		O
ATOM	3396	CB	SER	A	17	−22.044	91.275	7.738	1.00	42.19		C
ATOM	3397	OG	SER	A	17	−20.664	91.495	7.994	1.00	55.67		O
ATOM	3398	N	LEU	A	18	−23.976	90.833	5.361	1.00	40.66		N
ATOM	3399	CA	LEU	A	18	−25.220	90.256	4.877	1.00	42.98		C
ATOM	3400	C	LEU	A	18	−24.901	88.861	4.361	1.00	40.59		C
ATOM	3401	O	LEU	A	18	−23.804	88.623	3.850	1.00	41.78		O
ATOM	3402	CB	LEU	A	18	−25.806	91.135	3.773	1.00	44.15		C
ATOM	3403	CG	LEU	A	18	−27.278	91.269	3.460	1.00	54.36		C
ATOM	3404	CD1	LEU	A	18	−28.038	91.644	4.712	1.00	49.30		C
ATOM	3405	CD2	LEU	A	18	−27.392	92.395	2.454	1.00	49.78		C
ATOM	3406	N	ARG	A	19	−25.848	87.940	4.497	1.00	30.82		N
ATOM	3407	CA	ARG	A	19	−25.670	86.595	3.965	1.00	34.82		C
ATOM	3408	C	ARG	A	19	−26.783	86.270	2.981	1.00	34.54		C
ATOM	3409	O	ARG	A	19	−27.959	86.364	3.329	1.00	38.10		O
ATOM	3410	CB	ARG	A	19	−25.635	85.549	5.073	1.00	35.74		C
ATOM	3411	CG	ARG	A	19	−25.012	84.268	4.606	1.00	37.23		C
ATOM	3412	CD	ARG	A	19	−25.223	83.128	5.579	1.00	38.05		C
ATOM	3413	NE	ARG	A	19	−26.633	82.826	5.730	1.00	39.69		N
ATOM	3414	CZ	ARG	A	19	−27.107	81.838	6.477	1.00	47.15		C
ATOM	3415	NH1	ARG	A	19	−28.419	81.642	6.559	1.00	43.39		N1+
ATOM	3416	NH2	ARG	A	19	−26.271	81.043	7.130	1.00	46.94		N
ATOM	3417	N	LEU	A	20	−26.416	85.921	1.750	1.00	33.95		N
ATOM	3418	CA	LEU	A	20	−27.386	85.431	0.783	1.00	32.04		C
ATOM	3419	C	LEU	A	20	−27.486	83.908	0.841	1.00	35.48		C
ATOM	3420	O	LEU	A	20	−26.522	83.206	1.174	1.00	34.13		O
ATOM	3421	CB	LEU	A	20	−27.019	85.873	−0.631	1.00	26.84		C
ATOM	3422	CG	LEU	A	20	−26.829	87.380	−0.792	1.00	31.60		C
ATOM	3423	CD1	LEU	A	20	−26.621	87.704	−2.261	1.00	25.55		C
ATOM	3424	CD2	LEU	A	20	−28.028	88.140	−0.220	1.00	24.15		C
ATOM	3425	N	SER	A	21	−28.675	83.403	0.528	1.00	33.17		N
ATOM	3426	CA	SER	A	21	−28.924	81.976	0.391	1.00	32.39		C
ATOM	3427	C	SER	A	21	−29.441	81.658	−1.002	1.00	34.28		C
ATOM	3428	O	SER	A	21	−30.123	82.470	−1.633	1.00	35.15		O
ATOM	3429	CB	SER	A	21	−29.944	81.457	1.411	1.00	29.91		C
ATOM	3430	OG	SER	A	21	−29.401	81.456	2.706	1.00	32.59		O
ATOM	3431	N	CYS	A	22	−29.122	80.452	−1.463	1.00	29.55		N
ATOM	3432	CA	CYS	A	22	−29.608	79.954	−2.740	1.00	29.82		C
ATOM	3433	C	CYS	A	22	−30.059	78.520	−2.506	1.00	34.08		C
ATOM	3434	O	CYS	A	22	−29.225	77.635	−2.286	1.00	33.80		O
ATOM	3435	CB	CYS	A	22	−28.515	80.040	−3.803	1.00	37.60		C
ATOM	3436	SG	CYS	A	22	−28.846	79.175	−5.362	1.00	44.81		S
ATOM	3437	N	ALA	A	23	−31.366	78.297	−2.544	1.00	27.47		N
ATOM	3438	CA	ALA	A	23	−31.956	77.006	−2.235	1.00	31.62		C
ATOM	3439	C	ALA	A	23	−32.152	76.263	−3.540	1.00	32.14		C
ATOM	3440	O	ALA	A	23	−32.753	76.799	−4.480	1.00	32.98		O
ATOM	3441	CB	ALA	A	23	−33.296	77.155	−1.500	1.00	23.36		C
ATOM	3442	N	ALA	A	24	−31.646	75.037	−3.593	1.00	31.79		N
ATOM	3443	CA	ALA	A	24	−31.642	74.239	−4.809	1.00	29.92		C
ATOM	3444	C	ALA	A	24	−32.595	73.062	−4.685	1.00	29.71		C
ATOM	3445	O	ALA	A	24	−32.735	72.476	−3.612	1.00	39.67		O
ATOM	3446	CB	ALA	A	24	−30.238	73.724	−5.104	1.00	27.23		C
ATOM	3447	N	SER	A	25	−33.239	72.708	−5.790	1.00	32.42		N
ATOM	3448	CA	SER	A	25	−34.067	71.515	−5.851	1.00	28.53		C
ATOM	3449	C	SER	A	25	−34.108	70.982	−7.273	1.00	34.80		C
ATOM	3450	O	SER	A	25	−33.754	71.688	−8.228	1.00	28.65		O
ATOM	3451	CB	SER	A	25	−35.484	71.822	−5.400	1.00	36.68		C
ATOM	3452	OG	SER	A	25	−36.046	72.798	−6.269	1.00	34.63		O
ATOM	3453	N	GLY	A	26	−34.558	69.720	−7.410	1.00	31.26		N
ATOM	3454	CA	GLY	A	26	−34.824	69.150	−8.718	1.00	31.69		C
ATOM	3455	C	GLY	A	26	−33.759	68.254	−9.323	1.00	50.48		C
ATOM	3456	O	GLY	A	26	−33.944	67.786	−10.460	1.00	59.29		O
ATOM	3457	N	PHE	A	27	−32.666	68.001	−8.613	1.00	34.76		N
ATOM	3458	CA	PHE	A	27	−31.536	67.198	−9.082	1.00	36.25		C
ATOM	3459	C	PHE	A	27	−30.495	67.347	−8.004	1.00	35.91		C
ATOM	3460	O	PHE	A	27	−30.163	68.473	−7.622	1.00	41.91		O
ATOM	3461	CB	PHE	A	27	−30.986	67.647	−10.455	1.00	34.34		C
ATOM	3462	CG	PHE	A	27	−29.671	66.974	−10.868	1.00	35.77		C
ATOM	3463	CD1	PHE	A	27	−29.467	65.601	−10.706	1.00	38.27		C
ATOM	3464	CD2	PHE	A	27	−28.645	67.728	−11.455	1.00	39.96		C
ATOM	3465	CE1	PHE	A	27	−28.246	64.992	−11.075	1.00	42.34		C
ATOM	3466	CE2	PHE	A	27	−27.422	67.132	−11.848	1.00	39.02		C
ATOM	3467	CZ	PHE	A	27	−27.221	65.758	−11.651	1.00	37.64		C
ATOM	3468	N	THR	A	28	−29.960	66.224	−7.555	1.00	34.00		N
ATOM	3469	CA	THR	A	28	−29.086	66.145	−6.398	1.00	32.16		C
ATOM	3470	C	THR	A	28	−28.160	67.347	−6.297	1.00	32.73		C
ATOM	3471	O	THR	A	28	−27.324	67.570	−7.174	1.00	34.74		O
ATOM	3472	CB	THR	A	28	−28.286	64.858	−6.521	1.00	39.57		C
ATOM	3473	OG1	THR	A	28	−29.211	63.801	−6.780	1.00	48.76		O
ATOM	3474	CG2	THR	A	28	−27.527	64.570	−5.250	1.00	39.97		C
ATOM	3475	N	PHE	A	29	−28.340	68.137	−5.232	1.00	37.84		N
ATOM	3476	CA	PHE	A	29	−27.545	69.348	−5.012	1.00	34.13		C
ATOM	3477	C	PHE	A	29	−26.050	69.063	−5.057	1.00	35.71		C
ATOM	3478	O	PHE	A	29	−25.277	69.821	−5.666	1.00	31.39		O
ATOM	3479	CB	PHE	A	29	−27.924	69.954	−3.661	1.00	33.04		C
ATOM	3480	CG	PHE	A	29	−27.217	71.251	−3.309	1.00	29.10		C
ATOM	3481	CD1	PHE	A	29	−27.347	72.386	−4.112	1.00	28.49		C
ATOM	3482	CD2	PHE	A	29	−26.505	71.364	−2.117	1.00	30.52		C
ATOM	3483	CE1	PHE	A	29	−26.748	73.607	−3.754	1.00	29.07		C
ATOM	3484	CE2	PHE	A	29	−25.893	72.592	−1.755	1.00	33.69		C
ATOM	3485	CZ	PHE	A	29	−26.023	73.707	−2.578	1.00	27.96		C
ATOM	3486	N	SER	A	30	−25.628	67.963	−4.434	1.00	33.43		N
ATOM	3487	CA	SER	A	30	−24.208	67.634	−4.348	1.00	38.52		C
ATOM	3488	C	SER	A	30	−23.621	67.208	−5.682	1.00	33.12		C
ATOM	3489	O	SER	A	30	−22.422	66.936	−5.741	1.00	35.08		O
ATOM	3490	CB	SER	A	30	−23.988	66.534	−3.303	1.00	28.69		C
ATOM	3491	OG	SER	A	30	−24.728	65.385	−3.669	1.00	38.89		O
ATOM	3492	N	SER	A	31	−24.419	67.147	−6.740	1.00	27.16		N
ATOM	3493	CA	SER	A	31	−23.905	66.778	−8.045	1.00	38.98		C
ATOM	3494	C	SER	A	31	−23.443	67.962	−8.896	1.00	39.11		C
ATOM	3495	O	SER	A	31	−23.036	67.740	−10.050	1.00	33.54		O
ATOM	3496	CB	SER	A	31	−24.944	65.966	−8.806	1.00	31.50		C
ATOM	3497	OG	SER	A	31	−25.034	64.689	−8.205	1.00	43.55		O
ATOM	3498	N	TYR	A	32	−23.469	69.194	−8.377	1.00	30.49		N
ATOM	3499	CA	TYR	A	32	−22.942	70.307	−9.164	1.00	28.71		C
ATOM	3500	C	TYR	A	32	−22.356	71.382	−8.268	1.00	29.76		C
ATOM	3501	O	TYR	A	32	−22.712	71.503	−7.092	1.00	29.23		O
ATOM	3502	CB	TYR	A	32	−24.002	70.910	−10.078	1.00	34.80		C
ATOM	3503	CG	TYR	A	32	−25.331	71.155	−9.416	1.00	32.18		C
ATOM	3504	CD1	TYR	A	32	−25.549	72.299	−8.660	1.00	33.21		C
ATOM	3505	CD2	TYR	A	32	−26.364	70.259	−9.562	1.00	32.73		C
ATOM	3506	CE1	TYR	A	32	−26.770	72.536	−8.050	1.00	37.14		C
ATOM	3507	CE2	TYR	A	32	−27.589	70.484	−8.953	1.00	36.08		C
ATOM	3508	CZ	TYR	A	32	−27.783	71.621	−8.202	1.00	34.54		C
ATOM	3509	OH	TYR	A	32	−28.995	71.854	−7.605	1.00	42.41		O
ATOM	3510	N	GLY	A	33	−21.391	72.118	−8.828	1.00	29.06		N
ATOM	3511	CA	GLY	A	33	−20.917	73.336	−8.213	1.00	26.22		C
ATOM	3512	C	GLY	A	33	−21.823	74.508	−8.562	1.00	32.33		C
ATOM	3513	O	GLY	A	33	−22.749	74.389	−9.373	1.00	32.28		O
ATOM	3514	N	LEU	A	34	−21.549	75.660	−7.944	1.00	28.11		N
ATOM	3515	CA	LEU	A	34	−22.397	76.825	−8.149	1.00	28.06		C
ATOM	3516	C	LEU	A	34	−21.579	78.107	−8.137	1.00	32.81		C
ATOM	3517	O	LEU	A	34	−20.482	78.185	−7.562	1.00	30.26		O
ATOM	3518	CB	LEU	A	34	−23.503	76.934	−7.083	1.00	25.69		C
ATOM	3519	CG	LEU	A	34	−24.496	75.772	−7.075	1.00	29.24		C
ATOM	3520	CD1	LEU	A	34	−24.122	74.810	−5.948	1.00	25.51		C
ATOM	3521	CD2	LEU	A	34	−25.937	76.248	−6.951	1.00	28.69		C
ATOM	3522	N	HIS	A	35	−22.174	79.124	−8.757	1.00	25.76		N
ATOM	3523	CA	HIS	A	35	−21.645	80.469	−8.877	1.00	28.30		C
ATOM	3524	C	HIS	A	35	−22.559	81.459	−8.167	1.00	28.45		C
ATOM	3525	O	HIS	A	35	−23.771	81.255	−8.047	1.00	26.56		O
ATOM	3526	CB	HIS	A	35	−21.583	80.946	−10.334	1.00	27.75		C
ATOM	3527	CG	HIS	A	35	−20.599	80.236	−11.204	1.00	34.48		C
ATOM	3528	ND1	HIS	A	35	−19.305	80.689	−11.377	1.00	31.96		N
ATOM	3529	CD2	HIS	A	35	−20.742	79.174	−12.034	1.00	27.73		C
ATOM	3530	CE1	HIS	A	35	−18.693	79.927	−12.263	1.00	30.71		C
ATOM	3531	NE2	HIS	A	35	−19.537	78.989	−12.664	1.00	32.82		N
ATOM	3532	N	TRP	A	36	−21.971	82.583	−7.793	1.00	24.52		N
ATOM	3533	CA	TRP	A	36	−22.702	83.815	−7.578	1.00	24.53		C
ATOM	3534	C	TRP	A	36	−22.276	84.804	−8.656	1.00	30.64		C
ATOM	3535	O	TRP	A	36	−21.078	84.979	−8.895	1.00	31.45		O
ATOM	3536	CB	TRP	A	36	−22.431	84.389	−6.184	1.00	25.38		C
ATOM	3537	CG	TRP	A	36	−23.102	83.636	−5.061	1.00	34.21		C
ATOM	3538	CD1	TRP	A	36	−22.528	82.700	−4.225	1.00	27.01		C
ATOM	3539	CD2	TRP	A	36	−24.483	83.734	−4.662	1.00	29.26		C
ATOM	3540	NE1	TRP	A	36	−23.464	82.236	−3.328	1.00	29.61		N
ATOM	3541	CE2	TRP	A	36	−24.669	82.850	−3.574	1.00	29.15		C
ATOM	3542	CE3	TRP	A	36	−25.569	84.500	−5.104	1.00	31.70		C
ATOM	3543	CZ2	TRP	A	36	−25.902	82.707	−2.925	1.00	29.62		C
ATOM	3544	CZ3	TRP	A	36	−26.795	84.353	−4.464	1.00	31.58		C
ATOM	3545	CH2	TRP	A	36	−26.950	83.447	−3.390	1.00	32.02		C
ATOM	3546	N	VAL	A	37	−23.255	85.430	−9.315	1.00	26.17		N
ATOM	3547	CA	VAL	A	37	−23.052	86.487	−10.305	1.00	26.93		C
ATOM	3548	C	VAL	A	37	−23.911	87.683	−9.909	1.00	31.18		C
ATOM	3549	O	VAL	A	37	−24.979	87.514	−9.311	1.00	32.57		O
ATOM	3550	CB	VAL	A	37	−23.436	86.003	−11.725	1.00	30.07		C
ATOM	3551	CG1	VAL	A	37	−23.336	87.141	−12.741	1.00	25.17		C
ATOM	3552	CG2	VAL	A	37	−22.577	84.797	−12.141	1.00	27.92		C
ATOM	3553	N	ARG	A	38	−23.451	88.900	−10.217	1.00	26.83		N
ATOM	3554	CA	ARG	A	38	−24.222	90.086	−9.838	1.00	28.59		C
ATOM	3555	C	ARG	A	38	−24.327	91.074	−10.987	1.00	32.00		C
ATOM	3556	O	ARG	A	38	−23.546	91.042	−11.942	1.00	34.12		O
ATOM	3557	CB	ARG	A	38	−23.649	90.790	−8.616	1.00	24.52		C
ATOM	3558	CG	ARG	A	38	−22.405	91.581	−8.863	1.00	27.87		C
ATOM	3559	CD	ARG	A	38	−21.832	92.016	−7.532	1.00	25.42		C
ATOM	3560	NE	ARG	A	38	−20.569	92.691	−7.719	1.00	26.21		N
ATOM	3561	CZ	ARG	A	38	−19.825	93.186	−6.735	1.00	33.88		C
ATOM	3562	NH1	ARG	A	38	−20.207	93.058	−5.470	1.00	31.46		N1+
ATOM	3563	NH2	ARG	A	38	−18.700	93.822	−7.026	1.00	27.28		N
ATOM	3564	N	GLN	A	39	−25.317	91.961	−10.874	1.00	31.14		N
ATOM	3565	CA	GLN	A	39	−25.594	92.942	−11.923	1.00	26.67		C
ATOM	3566	C	GLN	A	39	−26.067	94.237	−11.278	1.00	33.37		C
ATOM	3567	O	GLN	A	39	−27.144	94.282	−10.657	1.00	30.44		O
ATOM	3568	CB	GLN	A	39	−26.635	92.419	−12.901	1.00	29.71		C
ATOM	3569	CG	GLN	A	39	−26.977	93.391	−14.031	1.00	30.87		C
ATOM	3570	CD	GLN	A	39	−27.797	92.710	−15.108	1.00	35.35		C
ATOM	3571	OE1	GLN	A	39	−28.796	92.048	−14.812	1.00	37.94		O
ATOM	3572	NE2	GLN	A	39	−27.370	92.841	−16.358	1.00	26.92		N
ATOM	3573	N	ALA	A	40	−25.269	95.279	−11.425	1.00	28.05		N
ATOM	3574	CA	ALA	A	40	−25.664	96.588	−10.926	1.00	34.65		C
ATOM	3575	C	ALA	A	40	−26.709	97.199	−11.859	1.00	34.83		C
ATOM	3576	O	ALA	A	40	−26.757	96.861	−13.039	1.00	32.60		O
ATOM	3577	CB	ALA	A	40	−24.443	97.499	−10.812	1.00	29.23		C
ATOM	3578	N	PRO	A	41	−27.556	98.095	−11.352	1.00	41.70		N
ATOM	3579	CA	PRO	A	41	−28.654	98.645	−12.175	1.00	37.62		C
ATOM	3580	C	PRO	A	41	−28.143	99.327	−13.440	1.00	38.87		C
ATOM	3581	O	PRO	A	41	−27.259	100.188	−13.392	1.00	37.58		O
ATOM	3582	CB	PRO	A	41	−29.330	99.656	−11.236	1.00	34.86		C
ATOM	3583	CG	PRO	A	41	−28.936	99.229	−9.859	1.00	40.20		C
ATOM	3584	CD	PRO	A	41	−27.557	98.641	−9.983	1.00	35.94		C
ATOM	3585	N	GLY	A	42	−28.698	98.918	−14.578	1.00	36.04		N
ATOM	3586	CA	GLY	A	42	−28.295	99.408	−15.887	1.00	32.92		C
ATOM	3587	C	GLY	A	42	−26.969	98.887	−16.429	1.00	42.89		C
ATOM	3588	O	GLY	A	42	−26.492	99.395	−17.446	1.00	48.01		O
ATOM	3589	N	LYS	A	43	−26.358	97.882	−15.817	1.00	37.13		N
ATOM	3590	CA	LYS	A	43	−25.003	97.473	−16.196	1.00	39.84		C
ATOM	3591	C	LYS	A	43	−24.961	95.989	−16.548	1.00	36.76		C
ATOM	3592	O	LYS	A	43	−25.989	95.301	−16.591	1.00	33.65		O
ATOM	3593	CB	LYS	A	43	−24.004	97.816	−15.094	1.00	35.22		C
ATOM	3594	CG	LYS	A	43	−23.960	99.326	−14.833	1.00	42.47		C
ATOM	3595	CD	LYS	A	43	−22.804	99.688	−13.941	1.00	57.71		C
ATOM	3596	CE	LYS	A	43	−22.589	101.201	−13.864	1.00	72.06		C
ATOM	3597	NZ	LYS	A	43	−21.339	101.531	−13.103	1.00	70.64		N1+
ATOM	3598	N	GLY	A	44	−23.743	95.520	−16.834	1.00	31.12		N
ATOM	3599	CA	GLY	A	44	−23.510	94.165	−17.290	1.00	28.92		C
ATOM	3600	C	GLY	A	44	−23.333	93.158	−16.166	1.00	33.92		C
ATOM	3601	O	GLY	A	44	−23.295	93.484	−14.979	1.00	35.65		O
ATOM	3602	N	LEU	A	45	−23.202	91.898	−16.569	1.00	31.47		N
ATOM	3603	CA	LEU	A	45	−22.959	90.839	−15.606	1.00	26.60		C
ATOM	3604	C	LEU	A	45	−21.542	90.959	−15.072	1.00	31.15		C
ATOM	3605	O	LEU	A	45	−20.601	91.246	−15.820	1.00	31.96		O
ATOM	3606	CB	LEU	A	45	−23.173	89.462	−16.256	1.00	28.04		C
ATOM	3607	CG	LEU	A	45	−24.575	89.294	−16.881	1.00	33.18		C
ATOM	3608	CD1	LEU	A	45	−24.804	87.921	−17.544	1.00	29.82		C
ATOM	3609	CD2	LEU	A	45	−25.639	89.585	−15.859	1.00	27.89		C
ATOM	3610	N	GLU	A	46	−21.397	90.735	−13.767	1.00	30.38		N
ATOM	3611	CA	GLU	A	46	−20.101	90.660	−13.112	1.00	31.96		C
ATOM	3612	C	GLU	A	46	−20.049	89.376	−12.306	1.00	28.71		C
ATOM	3613	O	GLU	A	46	−20.899	89.156	−11.440	1.00	28.54		O
ATOM	3614	CB	GLU	A	46	−19.854	91.859	−12.196	1.00	30.82		C
ATOM	3615	CG	GLU	A	46	−18.411	91.886	−11.708	1.00	35.43		C
ATOM	3616	CD	GLU	A	46	−18.145	92.863	−10.551	1.00	42.19		C
ATOM	3617	OE1	GLU	A	46	−19.076	93.544	−10.038	1.00	34.18		O
ATOM	3618	OE2	GLU	A	46	−16.968	92.932	−10.154	1.00	46.04		O1−
ATOM	3619	N	TRP	A	47	−19.052	88.537	−12.584	1.00	28.91		N
ATOM	3620	CA	TRP	A	47	−18.888	87.300	−11.834	1.00	28.05		C
ATOM	3621	C	TRP	A	47	−18.433	87.610	−10.414	1.00	28.38		C
ATOM	3622	O	TRP	A	47	−17.652	88.534	−10.199	1.00	29.03		O
ATOM	3623	CB	TRP	A	47	−17.882	86.396	−12.547	1.00	28.79		C
ATOM	3624	CG	TRP	A	47	−17.570	85.150	−11.808	1.00	27.80		C
ATOM	3625	CD1	TRP	A	47	−18.396	84.090	−11.618	1.00	26.75		C
ATOM	3626	CD2	TRP	A	47	−16.330	84.810	−11.186	1.00	29.28		C
ATOM	3627	NE1	TRP	A	47	−17.759	83.119	−10.900	1.00	30.04		N
ATOM	3628	CE2	TRP	A	47	−16.487	83.529	−10.623	1.00	26.53		C
ATOM	3629	CE3	TRP	A	47	−15.093	85.455	−11.067	1.00	30.37		C
ATOM	3630	CZ2	TRP	A	47	−15.454	82.870	−9.945	1.00	30.41		C
ATOM	3631	CZ3	TRP	A	47	−14.058	84.797	−10.376	1.00	27.15		C
ATOM	3632	CH2	TRP	A	47	−14.251	83.527	−9.832	1.00	30.81		C
ATOM	3633	N	VAL	A	48	−18.923	86.836	−9.441	1.00	26.85		N
ATOM	3634	CA	VAL	A	48	−18.590	87.031	−8.026	1.00	26.22		C
ATOM	3635	C	VAL	A	48	−17.740	85.890	−7.475	1.00	27.91		C
ATOM	3636	O	VAL	A	48	−16.641	86.118	−6.962	1.00	31.20		O
ATOM	3637	CB	VAL	A	48	−19.858	87.245	−7.171	1.00	29.89		C
ATOM	3638	CG1	VAL	A	48	−19.465	87.415	−5.709	1.00	27.30		C
ATOM	3639	CG2	VAL	A	48	−20.640	88.465	−7.680	1.00	27.25		C
ATOM	3640	N	ALA	A	49	−18.234	84.656	−7.552	1.00	27.92		N
ATOM	3641	CA	ALA	A	49	−17.498	83.540	−6.964	1.00	27.21		C
ATOM	3642	C	ALA	A	49	−18.028	82.240	−7.528	1.00	29.25		C
ATOM	3643	O	ALA	A	49	−19.155	82.178	−8.025	1.00	29.04		O
ATOM	3644	CB	ALA	A	49	−17.590	83.500	−5.429	1.00	22.18		C
ATOM	3645	N	VAL	A	50	−17.187	81.190	−7.435	1.00	25.65		N
ATOM	3646	CA	VAL	A	50	−17.592	79.835	−7.777	1.00	25.46		C
ATOM	3647	C	VAL	A	50	−17.129	78.894	−6.678	1.00	28.11		C
ATOM	3648	O	VAL	A	50	−16.137	79.144	−5.988	1.00	30.11		O
ATOM	3649	CB	VAL	A	50	−17.068	79.380	−9.162	1.00	31.87		C
ATOM	3650	CG1	VAL	A	50	−15.561	79.238	−9.175	1.00	28.23		C
ATOM	3651	CG2	VAL	A	50	−17.767	78.084	−9.606	1.00	28.82		C
ATOM	3652	N	ILE	A	51	−17.884	77.821	−6.484	1.00	29.93		N
ATOM	3653	CA	ILE	A	51	−17.514	76.799	−5.522	1.00	25.88		C
ATOM	3654	C	ILE	A	51	−17.657	75.447	−6.203	1.00	26.86		C
ATOM	3655	O	ILE	A	51	−18.486	75.262	−7.100	1.00	26.48		O
ATOM	3656	CB	ILE	A	51	−18.354	76.879	−4.227	1.00	28.38		C
ATOM	3657	CG1	ILE	A	51	−17.776	75.932	−3.163	1.00	29.68		C
ATOM	3658	CG2	ILE	A	51	−19.831	76.565	−4.498	1.00	23.38		C
ATOM	3659	CD1	ILE	A	51	−18.344	76.180	−1.775	1.00	28.59		C
ATOM	3660	N	TRP	A	52	−16.821	74.510	−5.793	1.00	24.08		N
ATOM	3661	CA	TRP	A	52	−16.856	73.188	−6.392	1.00	28.60		C
ATOM	3662	C	TRP	A	52	−18.074	72.397	−5.899	1.00	30.88		C
ATOM	3663	O	TRP	A	52	−18.688	72.722	−4.879	1.00	26.43		O
ATOM	3664	CB	TRP	A	52	−15.559	72.452	−6.066	1.00	30.05		C
ATOM	3665	CG	TRP	A	52	−14.821	71.992	−7.256	1.00	31.59		C
ATOM	3666	CD1	TRP	A	52	−14.551	70.701	−7.601	1.00	34.80		C
ATOM	3667	CD2	TRP	A	52	−14.265	72.811	−8.293	1.00	30.63		C
ATOM	3668	NE1	TRP	A	52	−13.842	70.664	−8.781	1.00	33.66		N
ATOM	3669	CE2	TRP	A	52	−13.652	71.942	−9.228	1.00	31.14		C
ATOM	3670	CE3	TRP	A	52	−14.220	74.183	−8.522	1.00	28.98		C
ATOM	3671	CZ2	TRP	A	52	−12.999	72.404	−10.368	1.00	30.12		C
ATOM	3672	CZ3	TRP	A	52	−13.564	74.646	−9.663	1.00	37.05		C
ATOM	3673	CH2	TRP	A	52	−12.953	73.756	−10.562	1.00	36.23		C
ATOM	3674	N	TYR	A	53	−18.401	71.330	−6.635	1.00	28.62		N
ATOM	3675	CA	TYR	A	53	−19.539	70.484	−6.281	1.00	31.01		C
ATOM	3676	C	TYR	A	53	−19.373	69.846	−4.909	1.00	36.12		C
ATOM	3677	O	TYR	A	53	−20.370	69.557	−4.240	1.00	36.43		O
ATOM	3678	CB	TYR	A	53	−19.743	69.393	−7.329	1.00	31.97		C
ATOM	3679	CG	TYR	A	53	−18.458	68.713	−7.742	1.00	35.13		C
ATOM	3680	CD1	TYR	A	53	−17.918	67.672	−6.989	1.00	37.05		C
ATOM	3681	CD2	TYR	A	53	−17.791	69.104	−8.896	1.00	37.33		C
ATOM	3682	CE1	TYR	A	53	−16.755	67.058	−7.366	1.00	36.11		C
ATOM	3683	CE2	TYR	A	53	−16.614	68.492	−9.286	1.00	40.57		C
ATOM	3684	CZ	TYR	A	53	−16.095	67.479	−8.521	1.00	40.64		C
ATOM	3685	OH	TYR	A	53	−14.916	66.886	−8.923	1.00	51.83		O
ATOM	3686	N	ASP	A	54	−18.136	69.613	−4.468	1.00	31.86		N
ATOM	3687	CA	ASP	A	54	−17.896	69.044	−3.150	1.00	32.47		C
ATOM	3688	C	ASP	A	54	−17.433	70.090	−2.141	1.00	32.55		C
ATOM	3689	O	ASP	A	54	−16.894	69.732	−1.097	1.00	34.26		O
ATOM	3690	CB	ASP	A	54	−16.882	67.901	−3.245	1.00	33.69		C
ATOM	3691	CG	ASP	A	54	−15.550	68.344	−3.878	1.00	41.63		C
ATOM	3692	OD1	ASP	A	54	−15.332	69.574	−4.029	1.00	35.39		O
ATOM	3693	OD2	ASP	A	54	−14.721	67.462	−4.224	1.00	41.66		O1−
ATOM	3694	N	GLY	A	55	−17.633	71.376	−2.428	1.00	35.34		N
ATOM	3695	CA	GLY	A	55	−17.197	72.416	−1.516	1.00	28.60		C
ATOM	3696	C	GLY	A	55	−15.696	72.626	−1.397	1.00	30.85		C
ATOM	3697	O	GLY	A	55	−15.261	73.340	−0.483	1.00	31.85		O
ATOM	3698	N	SER	A	56	−14.880	72.030	−2.271	1.00	31.41		N
ATOM	3699	CA	SER	A	56	−13.427	72.159	−2.138	1.00	28.55		C
ATOM	3700	C	SER	A	56	−12.921	73.456	−2.773	1.00	29.96		C
ATOM	3701	O	SER	A	56	−12.790	74.463	−2.071	1.00	35.87		O
ATOM	3702	CB	SER	A	56	−12.716	70.922	−2.715	1.00	29.73		C
ATOM	3703	OG	SER	A	56	−13.055	70.688	−4.069	1.00	33.14		O
ATOM	3704	N	ASN	A	57	−12.648	73.468	−4.080	1.00	27.89		N
ATOM	3705	CA	ASN	A	57	−12.094	74.669	−4.708	1.00	30.78		C
ATOM	3706	C	ASN	A	57	−13.090	75.836	−4.663	1.00	34.96		C
ATOM	3707	O	ASN	A	57	−14.296	75.655	−4.883	1.00	29.93		O
ATOM	3708	CB	ASN	A	57	−11.712	74.392	−6.167	1.00	28.41		C
ATOM	3709	CG	ASN	A	57	−10.430	73.551	−6.316	1.00	36.02		C
ATOM	3710	OD1	ASN	A	57	−10.034	72.789	−5.427	1.00	31.33		O
ATOM	3711	ND2	ASN	A	57	−9.779	73.703	−7.462	1.00	33.91		N
ATOM	3712	N	LYS	A	58	−12.562	77.042	−4.418	1.00	30.71		N
ATOM	3713	CA	LYS	A	58	−13.307	78.299	−4.384	1.00	31.44		C
ATOM	3714	C	LYS	A	58	−12.504	79.356	−5.117	1.00	31.50		C
ATOM	3715	O	LYS	A	58	−11.306	79.491	−4.858	1.00	35.00		O
ATOM	3716	CB	LYS	A	58	−13.541	78.796	−2.953	1.00	28.26		C
ATOM	3717	CG	LYS	A	58	−14.308	77.853	−2.071	1.00	32.31		C
ATOM	3718	CD	LYS	A	58	−14.359	78.350	−0.623	1.00	29.79		C
ATOM	3719	CE	LYS	A	58	−15.146	77.337	0.247	1.00	31.84		C
ATOM	3720	NZ	LYS	A	58	−15.624	77.954	1.523	1.00	28.78		N1+
ATOM	3721	N	TYR	A	59	−13.143	80.105	−6.025	1.00	31.81		N
ATOM	3722	CA	TYR	A	59	−12.489	81.224	−6.704	1.00	29.74		C
ATOM	3723	C	TYR	A	59	−13.349	82.463	−6.543	1.00	31.86		C
ATOM	3724	O	TYR	A	59	−14.581	82.379	−6.491	1.00	36.21		O
ATOM	3725	CB	TYR	A	59	−12.258	80.990	−8.212	1.00	35.36		C
ATOM	3726	CG	TYR	A	59	−11.620	79.662	−8.593	1.00	35.36		C
ATOM	3727	CD1	TYR	A	59	−10.873	78.936	−7.693	1.00	49.05		C
ATOM	3728	CD2	TYR	A	59	−11.776	79.141	−9.849	1.00	46.01		C
ATOM	3729	CE1	TYR	A	59	−10.317	77.708	−8.033	1.00	56.82		C
ATOM	3730	CE2	TYR	A	59	−11.212	77.925	−10.198	1.00	50.42		C
ATOM	3731	CZ	TYR	A	59	−10.494	77.215	−9.292	1.00	45.11		C
ATOM	3732	OH	TYR	A	59	−9.945	76.014	−9.656	1.00	44.41		O
ATOM	3733	N	TYR	A	60	−12.706	83.617	−6.491	1.00	28.31		N
ATOM	3734	CA	TYR	A	60	−13.418	84.868	−6.277	1.00	31.56		C
ATOM	3735	C	TYR	A	60	−12.950	85.928	−7.263	1.00	33.13		C
ATOM	3736	O	TYR	A	60	−11.782	85.963	−7.657	1.00	36.90		O
ATOM	3737	CB	TYR	A	60	−13.221	85.407	−4.884	1.00	26.95		C
ATOM	3738	CG	TYR	A	60	−13.706	84.522	−3.780	1.00	31.53		C
ATOM	3739	CD1	TYR	A	60	−12.877	83.520	−3.249	1.00	34.43		C
ATOM	3740	CD2	TYR	A	60	−14.958	84.703	−3.225	1.00	29.79		C
ATOM	3741	CE1	TYR	A	60	−13.308	82.707	−2.215	1.00	28.05		C
ATOM	3742	CE2	TYR	A	60	−15.400	83.896	−2.183	1.00	32.79		C
ATOM	3743	CZ	TYR	A	60	−14.567	82.900	−1.679	1.00	33.02		C
ATOM	3744	OH	TYR	A	60	−14.995	82.098	−0.641	1.00	31.57		O
ATOM	3745	N	ALA	A	61	−13.872	86.804	−7.650	1.00	23.00		N
ATOM	3746	CA	ALA	A	61	−13.464	87.976	−8.406	1.00	28.65		C
ATOM	3747	C	ALA	A	61	−12.612	88.888	−7.526	1.00	32.06		C
ATOM	3748	O	ALA	A	61	−12.759	88.923	−6.301	1.00	30.34		O
ATOM	3749	CB	ALA	A	61	−14.679	88.736	−8.937	1.00	25.89		C
ATOM	3750	N	ASP	A	62	−11.713	89.633	−8.171	1.00	32.65		N
ATOM	3751	CA	ASP	A	62	−10.805	90.522	−7.445	1.00	32.02		C
ATOM	3752	C	ASP	A	62	−11.551	91.559	−6.605	1.00	31.30		C
ATOM	3753	O	ASP	A	62	−11.125	91.882	−5.492	1.00	33.95		O
ATOM	3754	CB	ASP	A	62	−9.856	91.208	−8.428	1.00	30.42		C
ATOM	3755	CG	ASP	A	62	−8.574	90.404	−8.671	1.00	42.21		C
ATOM	3756	OD1	ASP	A	62	−8.521	89.196	−8.308	1.00	50.07		O
ATOM	3757	OD2	ASP	A	62	−7.625	90.972	−9.257	1.00	56.07		O1−
ATOM	3758	N	SER	A	63	−12.672	92.082	−7.106	1.00	28.74		N
ATOM	3759	CA	SER	A	63	−13.409	93.118	−6.383	1.00	32.42		C
ATOM	3760	C	SER	A	63	−13.980	92.646	−5.048	1.00	39.97		C
ATOM	3761	O	SER	A	63	−14.490	93.477	−4.280	1.00	38.00		O
ATOM	3762	CB	SER	A	63	−14.542	93.641	−7.263	1.00	35.16		C
ATOM	3763	OG	SER	A	63	−15.314	92.561	−7.747	1.00	42.20		O
ATOM	3764	N	VAL	A	64	−13.865	91.356	−4.740	1.00	33.69		N
ATOM	3765	CA	VAL	A	64	−14.600	90.717	−3.663	1.00	31.03		C
ATOM	3766	C	VAL	A	64	−13.681	89.860	−2.780	1.00	35.18		C
ATOM	3767	O	VAL	A	64	−14.040	89.490	−1.651	1.00	33.73		O
ATOM	3768	CB	VAL	A	64	−15.740	89.918	−4.330	1.00	34.61		C
ATOM	3769	CG1	VAL	A	64	−15.732	88.417	−4.001	1.00	22.27		C
ATOM	3770	CG2	VAL	A	64	−17.031	90.609	−4.115	1.00	28.14		C
ATOM	3771	N	LYS	A	65	−12.476	89.566	−3.273	1.00	30.69		N
ATOM	3772	CA	LYS	A	65	−11.498	88.785	−2.511	1.00	32.30		C
ATOM	3773	C	LYS	A	65	−11.300	89.377	−1.126	1.00	35.92		C
ATOM	3774	O	LYS	A	65	−11.119	90.590	−0.975	1.00	37.34		O
ATOM	3775	CB	LYS	A	65	−10.155	88.769	−3.242	1.00	31.37		C
ATOM	3776	CG	LYS	A	65	−10.056	87.772	−4.365	1.00	35.93		C
ATOM	3777	CD	LYS	A	65	−8.637	87.667	−4.881	1.00	39.14		C
ATOM	3778	CE	LYS	A	65	−8.443	86.411	−5.742	1.00	40.69		C
ATOM	3779	NZ	LYS	A	65	−9.097	86.500	−7.077	1.00	44.27		N1+
ATOM	3780	N	GLY	A	66	−11.300	88.509	−0.118	1.00	36.76		N
ATOM	3781	CA	GLY	A	66	−11.109	88.926	1.249	1.00	34.77		C
ATOM	3782	C	GLY	A	66	−12.355	89.409	1.957	1.00	37.43		C
ATOM	3783	O	GLY	A	66	−12.361	89.462	3.185	1.00	43.41		O
ATOM	3784	N	ARG	A	67	−13.407	89.779	1.231	1.00	37.34		N
ATOM	3785	CA	ARG	A	67	−14.630	90.281	1.849	1.00	34.16		C
ATOM	3786	C	ARG	A	67	−15.789	89.302	1.783	1.00	32.20		C
ATOM	3787	O	ARG	A	67	−16.554	89.208	2.745	1.00	35.10		O
ATOM	3788	CB	ARG	A	67	−15.047	91.609	1.199	1.00	28.81		C
ATOM	3789	CG	ARG	A	67	−14.047	92.745	1.481	1.00	38.29		C
ATOM	3790	CD	ARG	A	67	−14.504	94.103	0.942	1.00	39.40		C
ATOM	3791	NE	ARG	A	67	−14.857	94.018	−0.470	1.00	34.94		N
ATOM	3792	CZ	ARG	A	67	−16.086	94.209	−0.939	1.00	36.27		C
ATOM	3793	NH1	ARG	A	67	−17.074	94.532	−0.113	1.00	29.46		N1+
ATOM	3794	NH2	ARG	A	67	−16.325	94.083	−2.236	1.00	33.40		N
ATOM	3795	N	PHE	A	68	−15.936	88.558	0.688	1.00	31.92		N
ATOM	3796	CA	PHE	A	68	−17.046	87.626	0.523	1.00	33.41		C
ATOM	3797	C	PHE	A	68	−16.540	86.204	0.697	1.00	34.08		C
ATOM	3798	O	PHE	A	68	−15.382	85.903	0.405	1.00	35.01		O
ATOM	3799	CB	PHE	A	68	−17.727	87.743	−0.850	1.00	29.41		C
ATOM	3800	CG	PHE	A	68	−18.410	89.076	−1.108	1.00	31.18		C
ATOM	3801	CD1	PHE	A	68	−18.242	90.156	−0.256	1.00	28.93		C
ATOM	3802	CD2	PHE	A	68	−19.236	89.231	−2.206	1.00	29.68		C
ATOM	3803	CE1	PHE	A	68	−18.851	91.388	−0.518	1.00	33.26		C
ATOM	3804	CE2	PHE	A	68	−19.865	90.444	−2.462	1.00	36.39		C
ATOM	3805	CZ	PHE	A	68	−19.660	91.532	−1.618	1.00	35.74		C
ATOM	3806	N	THR	A	69	−17.413	85.325	1.177	1.00	33.37		N
ATOM	3807	CA	THR	A	69	−17.054	83.917	1.293	1.00	32.05		C
ATOM	3808	C	THR	A	69	−18.206	83.085	0.775	1.00	30.76		C
ATOM	3809	O	THR	A	69	−19.354	83.292	1.177	1.00	28.56		O
ATOM	3810	CB	THR	A	69	−16.720	83.513	2.739	1.00	38.78		C
ATOM	3811	OG1	THR	A	69	−15.552	84.216	3.173	1.00	33.71		O
ATOM	3812	CG2	THR	A	69	−16.475	81.992	2.856	1.00	30.01		C
ATOM	3813	N	ILE	A	70	−17.892	82.169	−0.143	1.00	28.12		N
ATOM	3814	CA	ILE	A	70	−18.862	81.246	−0.708	1.00	31.36		C
ATOM	3815	C	ILE	A	70	−18.754	79.918	0.040	1.00	32.93		C
ATOM	3816	O	ILE	A	70	−17.655	79.472	0.402	1.00	33.29		O
ATOM	3817	CB	ILE	A	70	−18.656	81.079	−2.230	1.00	31.45		C
ATOM	3818	CG1	ILE	A	70	−19.832	80.302	−2.852	1.00	29.85		C
ATOM	3819	CG2	ILE	A	70	−17.257	80.401	−2.554	1.00	29.79		C
ATOM	3820	CD1	ILE	A	70	−19.805	80.244	−4.411	1.00	27.30		C
ATOM	3821	N	SER	A	71	−19.899	79.300	0.307	1.00	30.39		N
ATOM	3822	CA	SER	A	71	−19.935	78.023	1.017	1.00	34.30		C
ATOM	3823	C	SER	A	71	−21.233	77.320	0.648	1.00	30.83		C
ATOM	3824	O	SER	A	71	−22.137	77.905	0.046	1.00	34.13		O
ATOM	3825	CB	SER	A	71	−19.827	78.201	2.544	1.00	28.89		C
ATOM	3826	OG	SER	A	71	−20.944	78.930	3.075	1.00	31.85		O
ATOM	3827	N	ARG	A	72	−21.333	76.064	1.046	1.00	33.01		N
ATOM	3828	CA	ARG	A	72	−22.531	75.307	0.753	1.00	33.51		C
ATOM	3829	C	ARG	A	72	−22.820	74.404	1.941	1.00	36.68		C
ATOM	3830	O	ARG	A	72	−21.918	74.070	2.713	1.00	32.75		O
ATOM	3831	CB	ARG	A	72	−22.364	74.492	−0.545	1.00	29.96		C
ATOM	3832	CG	ARG	A	72	−21.230	73.458	−0.489	1.00	29.86		C
ATOM	3833	CD	ARG	A	72	−20.985	72.827	−1.859	1.00	31.26		C
ATOM	3834	NE	ARG	A	72	−22.179	72.130	−2.344	1.00	36.14		N
ATOM	3835	CZ	ARG	A	72	−22.480	71.942	−3.627	1.00	33.42		C
ATOM	3836	NH1	ARG	A	72	−21.683	72.400	−4.575	1.00	31.33		N1+
ATOM	3837	NH2	ARG	A	72	−23.599	71.322	−3.972	1.00	33.70		N
ATOM	3838	N	ASP	A	73	−24.094	74.046	2.108	1.00	35.23		N
ATOM	3839	CA	ASP	A	73	−24.523	73.070	3.119	1.00	36.76		C
ATOM	3840	C	ASP	A	73	−25.407	72.032	2.428	1.00	39.51		C
ATOM	3841	O	ASP	A	73	−26.597	72.270	2.181	1.00	34.82		O
ATOM	3842	CB	ASP	A	73	−25.251	73.761	4.266	1.00	34.22		C
ATOM	3843	CG	ASP	A	73	−25.616	72.808	5.397	1.00	42.95		C
ATOM	3844	OD1	ASP	A	73	−25.733	71.576	5.175	1.00	42.54		O
ATOM	3845	OD2	ASP	A	73	−25.774	73.306	6.532	1.00	48.48		O1−
ATOM	3846	N	ASN	A	74	−24.825	70.874	2.117	1.00	37.32		N
ATOM	3847	CA	ASN	A	74	−25.569	69.888	1.350	1.00	37.99		C
ATOM	3848	C	ASN	A	74	−26.773	69.366	2.126	1.00	38.75		C
ATOM	3849	O	ASN	A	74	−27.823	69.104	1.530	1.00	38.15		O
ATOM	3850	CB	ASN	A	74	−24.634	68.757	0.923	1.00	38.26		C
ATOM	3851	CG	ASN	A	74	−23.691	69.174	−0.228	1.00	43.82		C
ATOM	3852	OD1	ASN	A	74	−23.726	70.314	−0.699	1.00	41.08		O
ATOM	3853	ND2	ASN	A	74	−22.837	68.252	−0.664	1.00	42.34		N
ATOM	3854	N	SER	A	75	−26.678	69.273	3.454	1.00	37.68		N
ATOM	3855	CA	SER	A	75	−27.820	68.764	4.205	1.00	40.41		C
ATOM	3856	C	SER	A	75	−29.031	69.694	4.108	1.00	39.19		C
ATOM	3857	O	SER	A	75	−30.152	69.250	4.331	1.00	38.81		O
ATOM	3858	CB	SER	A	75	−27.433	68.533	5.666	1.00	34.54		C
ATOM	3859	OG	SER	A	75	−27.418	69.751	6.380	1.00	41.65		O
ATOM	3860	N	LYS	A	76	−28.840	70.966	3.765	1.00	39.96		N
ATOM	3861	CA	LYS	A	76	−29.947	71.888	3.540	1.00	32.91		C
ATOM	3862	C	LYS	A	76	−30.127	72.270	2.076	1.00	33.45		C
ATOM	3863	O	LYS	A	76	−30.819	73.255	1.793	1.00	32.73		O
ATOM	3864	CB	LYS	A	76	−29.760	73.156	4.371	1.00	34.21		C
ATOM	3865	CG	LYS	A	76	−29.536	72.893	5.843	1.00	39.47		C
ATOM	3866	CD	LYS	A	76	−29.433	74.203	6.610	1.00	37.51		C
ATOM	3867	CE	LYS	A	76	−29.059	73.960	8.060	1.00	36.30		C
ATOM	3868	NZ	LYS	A	76	−28.974	75.226	8.812	1.00	53.39		N1+
ATOM	3869	N	ASN	A	77	−29.486	71.560	1.142	1.00	34.23		N
ATOM	3870	CA	ASN	A	77	−29.510	71.936	−0.275	1.00	34.08		C
ATOM	3871	C	ASN	A	77	−29.340	73.439	−0.531	1.00	33.69		C
ATOM	3872	O	ASN	A	77	−30.019	73.994	−1.395	1.00	31.88		O
ATOM	3873	CB	ASN	A	77	−30.814	71.468	−0.910	1.00	35.11		C
ATOM	3874	CG	ASN	A	77	−30.897	69.952	−1.020	1.00	45.26		C
ATOM	3875	OD1	ASN	A	77	−29.889	69.267	−1.184	1.00	51.24		O
ATOM	3876	ND2	ASN	A	77	−32.095	69.426	−0.909	1.00	53.41		N
ATOM	3877	N	THR	A	78	−28.427	74.101	0.184	1.00	28.09		N
ATOM	3878	CA	THR	A	78	−28.320	75.550	0.139	1.00	34.16		C
ATOM	3879	C	THR	A	78	−26.883	75.999	−0.101	1.00	31.55		C
ATOM	3880	O	THR	A	78	−25.941	75.476	0.499	1.00	29.95		O
ATOM	3881	CB	THR	A	78	−28.867	76.150	1.432	1.00	32.28		C
ATOM	3882	OG1	THR	A	78	−30.230	75.746	1.559	1.00	36.31		O
ATOM	3883	CG2	THR	A	78	−28.789	77.662	1.405	1.00	32.86		C
ATOM	3884	N	LEU	A	79	−26.747	76.977	−0.989	1.00	33.81		N
ATOM	3885	CA	LEU	A	79	−25.515	77.701	−1.273	1.00	30.18		C
ATOM	3886	C	LEU	A	79	−25.571	79.060	−0.585	1.00	32.22		C
ATOM	3887	O	LEU	A	79	−26.606	79.724	−0.617	1.00	34.07		O
ATOM	3888	CB	LEU	A	79	−25.381	77.913	−2.782	1.00	31.42		C
ATOM	3889	CG	LEU	A	79	−24.281	78.860	−3.263	1.00	32.10		C
ATOM	3890	CD1	LEU	A	79	−22.973	78.101	−3.223	1.00	23.19		C
ATOM	3891	CD2	LEU	A	79	−24.601	79.393	−4.668	1.00	27.71		C
ATOM	3892	N	TYR	A	80	−24.450	79.498	−0.015	1.00	30.45		N
ATOM	3893	CA	TYR	A	80	−24.385	80.758	0.715	1.00	29.65		C
ATOM	3894	C	TYR	A	80	−23.352	81.714	0.114	1.00	36.35		C
ATOM	3895	O	TYR	A	80	−22.353	81.294	−0.486	1.00	29.45		O
ATOM	3896	CB	TYR	A	80	−24.022	80.536	2.194	1.00	29.90		C
ATOM	3897	CG	TYR	A	80	−24.972	79.655	2.914	1.00	35.65		C
ATOM	3898	CD1	TYR	A	80	−26.209	80.148	3.347	1.00	31.27		C
ATOM	3899	CD2	TYR	A	80	−24.656	78.311	3.162	1.00	32.71		C
ATOM	3900	CE1	TYR	A	80	−27.109	79.334	4.006	1.00	30.61		C
ATOM	3901	CE2	TYR	A	80	−25.548	77.480	3.834	1.00	34.98		C
ATOM	3902	CZ	TYR	A	80	−26.780	77.999	4.253	1.00	43.60		C
ATOM	3903	OH	TYR	A	80	−27.691	77.183	4.903	1.00	43.60		O
ATOM	3904	N	LEU	A	81	−23.608	83.016	0.286	1.00	33.92		N
ATOM	3905	CA	LEU	A	81	−22.616	84.067	0.062	1.00	32.11		C
ATOM	3906	C	LEU	A	81	−22.609	84.955	1.294	1.00	35.72		C
ATOM	3907	O	LEU	A	81	−23.559	85.712	1.534	1.00	31.37		O
ATOM	3908	CB	LEU	A	81	−22.899	84.890	−1.193	1.00	29.72		C
ATOM	3909	CG	LEU	A	81	−21.820	85.907	−1.554	1.00	30.90		C
ATOM	3910	CD1	LEU	A	81	−20.535	85.193	−2.008	1.00	31.13		C
ATOM	3911	CD2	LEU	A	81	−22.311	86.863	−2.620	1.00	29.96		C
ATOM	3912	N	GLN	A	82	−21.546	84.836	2.077	1.00	35.14		N
ATOM	3913	CA	GLN	A	82	−21.322	85.681	3.236	1.00	35.67		C
ATOM	3914	C	GLN	A	82	−20.628	86.948	2.753	1.00	33.89		C
ATOM	3915	O	GLN	A	82	−19.504	86.883	2.239	1.00	36.17		O
ATOM	3916	CB	GLN	A	82	−20.463	84.940	4.264	1.00	33.97		C
ATOM	3917	CG	GLN	A	82	−20.206	85.726	5.526	1.00	35.10		C
ATOM	3918	CD	GLN	A	82	−21.509	86.106	6.226	1.00	41.65		C
ATOM	3919	OE1	GLN	A	82	−22.419	85.279	6.375	1.00	41.07		O
ATOM	3920	NE2	GLN	A	82	−21.598	87.354	6.669	1.00	39.37		N
ATOM	3921	N	MET	A	83	−21.290	88.089	2.892	1.00	34.01		N
ATOM	3922	CA	MET	A	83	−20.762	89.349	2.360	1.00	40.25		C
ATOM	3923	C	MET	A	83	−20.390	90.231	3.540	1.00	34.20		C
ATOM	3924	O	MET	A	83	−21.271	90.753	4.231	1.00	43.36		O
ATOM	3925	CB	MET	A	83	−21.782	90.054	1.460	1.00	35.88		C
ATOM	3926	CG	MET	A	83	−22.247	89.246	0.242	1.00	40.32		C
ATOM	3927	SD	MET	A	83	−23.444	90.120	−0.837	1.00	45.75		S
ATOM	3928	CE	MET	A	83	−24.869	90.178	0.214	1.00	39.89		C
ATOM	3929	N	ASN	A	84	−19.098	90.416	3.767	1.00	34.41		N
ATOM	3930	CA	ASN	A	84	−18.649	91.282	4.849	1.00	35.66		C
ATOM	3931	C	ASN	A	84	−18.114	92.576	4.266	1.00	35.32		C
ATOM	3932	O	ASN	A	84	−17.798	92.660	3.078	1.00	37.11		O
ATOM	3933	CB	ASN	A	84	−17.563	90.616	5.694	1.00	33.02		C
ATOM	3934	CG	ASN	A	84	−18.033	89.347	6.358	1.00	38.60		C
ATOM	3935	OD1	ASN	A	84	−19.196	89.206	6.717	1.00	38.86		O
ATOM	3936	ND2	ASN	A	84	−17.127	88.398	6.499	1.00	43.30		N
ATOM	3937	N	SER	A	85	−18.051	93.598	5.113	1.00	37.32		N
ATOM	3938	CA	SER	A	85	−17.446	94.870	4.742	1.00	40.34		C
ATOM	3939	C	SER	A	85	−18.091	95.435	3.483	1.00	36.53		C
ATOM	3940	O	SER	A	85	−17.417	95.833	2.536	1.00	42.50		O
ATOM	3941	CB	SER	A	85	−15.936	94.707	4.545	1.00	41.25		C
ATOM	3942	OG	SER	A	85	−15.303	94.426	5.777	1.00	48.30		O
ATOM	3943	N	LEU	A	86	−19.419	95.440	3.469	1.00	36.42		N
ATOM	3944	CA	LEU	A	86	−20.121	95.839	2.269	1.00	30.29		C
ATOM	3945	C	LEU	A	86	−19.768	97.269	1.898	1.00	37.87		C
ATOM	3946	O	LEU	A	86	−19.530	98.126	2.759	1.00	39.88		O
ATOM	3947	CB	LEU	A	86	−21.620	95.670	2.458	1.00	37.21		C
ATOM	3948	CG	LEU	A	86	−22.026	94.199	2.267	1.00	41.48		C
ATOM	3949	CD1	LEU	A	86	−23.420	93.965	2.745	1.00	31.33		C
ATOM	3950	CD2	LEU	A	86	−21.912	93.809	0.788	1.00	34.28		C
ATOM	3951	N	ARG	A	87	−19.673	97.500	0.601	1.00	31.11		N
ATOM	3952	CA	ARG	A	87	−19.397	98.809	0.054	1.00	36.58		C
ATOM	3953	C	ARG	A	87	−20.539	99.186	−0.890	1.00	37.14		C
ATOM	3954	O	ARG	A	87	−21.233	98.322	−1.439	1.00	30.93		O
ATOM	3955	CB	ARG	A	87	−18.047	98.816	−0.688	1.00	36.84		C
ATOM	3956	CG	ARG	A	87	−16.843	98.100	−0.017	1.00	39.75		C
ATOM	3957	CD	ARG	A	87	−15.620	98.762	−0.560	1.00	50.01		C
ATOM	3958	NE	ARG	A	87	−14.715	97.898	−1.313	1.00	57.70		N
ATOM	3959	CZ	ARG	A	87	−13.636	97.274	−0.840	1.00	54.84		C
ATOM	3960	NH1	ARG	A	87	−13.275	97.378	0.442	1.00	55.39		N1+
ATOM	3961	NH2	ARG	A	87	−12.907	96.541	−1.682	1.00	46.24		N
ATOM	3962	N	VAL	A	88	−20.706	100.495	−1.088	1.00	33.94		N
ATOM	3963	CA	VAL	A	88	−21.786	101.015	−1.927	1.00	35.85		C
ATOM	3964	C	VAL	A	88	−21.768	100.348	−3.297	1.00	33.17		C
ATOM	3965	O	VAL	A	88	−22.812	99.996	−3.856	1.00	34.21		O
ATOM	3966	CB	VAL	A	88	−21.681	102.557	−2.018	1.00	41.36		C
ATOM	3967	CG1	VAL	A	88	−22.508	103.125	−3.182	1.00	34.83		C
ATOM	3968	CG2	VAL	A	88	−22.191	103.172	−0.697	1.00	32.83		C
ATOM	3969	N	GLU	A	89	−20.577	100.142	−3.842	1.00	32.51		N
ATOM	3970	CA	GLU	A	89	−20.416	99.535	−5.149	1.00	32.60		C
ATOM	3971	C	GLU	A	89	−20.831	98.070	−5.195	1.00	35.92		C
ATOM	3972	O	GLU	A	89	−20.914	97.531	−6.303	1.00	32.77		O
ATOM	3973	CB	GLU	A	89	−18.947	99.625	−5.598	1.00	33.36		C
ATOM	3974	CG	GLU	A	89	−18.249	100.917	−5.267	1.00	52.01		C
ATOM	3975	CD	GLU	A	89	−17.581	100.894	−3.898	1.00	57.81		C
ATOM	3976	OE1	GLU	A	89	−18.121	101.544	−2.969	1.00	46.95		O
ATOM	3977	OE2	GLU	A	89	−16.513	100.230	−3.762	1.00	68.05		O1−
ATOM	3978	N	ASP	A	90	−21.123	97.427	−4.048	1.00	30.72		N
ATOM	3979	CA	ASP	A	90	−21.653	96.063	−4.058	1.00	34.90		C
ATOM	3980	C	ASP	A	90	−23.142	96.017	−4.360	1.00	35.83		C
ATOM	3981	O	ASP	A	90	−23.710	94.912	−4.422	1.00	33.53		O
ATOM	3982	CB	ASP	A	90	−21.377	95.351	−2.721	1.00	28.51		C
ATOM	3983	CG	ASP	A	90	−19.884	95.173	−2.453	1.00	37.19		C
ATOM	3984	OD1	ASP	A	90	−19.142	94.821	−3.411	1.00	36.43		O
ATOM	3985	OD2	ASP	A	90	−19.439	95.412	−1.300	1.00	36.43		O1−
ATOM	3986	N	THR	A	91	−23.778	97.180	−4.534	1.00	30.48		N
ATOM	3987	CA	THR	A	91	−25.207	97.244	−4.843	1.00	34.41		C
ATOM	3988	C	THR	A	91	−25.488	96.586	−6.183	1.00	29.60		C
ATOM	3989	O	THR	A	91	−24.889	96.958	−7.192	1.00	33.51		O
ATOM	3990	CB	THR	A	91	−25.655	98.705	−4.865	1.00	34.98		C
ATOM	3991	OG1	THR	A	91	−25.482	99.260	−3.556	1.00	33.04		O
ATOM	3992	CG2	THR	A	91	−27.119	98.836	−5.317	1.00	22.08		C
ATOM	3993	N	ALA	A	92	−26.384	95.601	−6.196	1.00	26.49		N
ATOM	3994	CA	ALA	A	92	−26.628	94.831	−7.418	1.00	33.82		C
ATOM	3995	C	ALA	A	92	−27.764	93.858	−7.167	1.00	31.11		C
ATOM	3996	O	ALA	A	92	−28.109	93.559	−6.019	1.00	33.45		O
ATOM	3997	CB	ALA	A	92	−25.374	94.036	−7.893	1.00	29.95		C
ATOM	3998	N	VAL	A	93	−28.318	93.336	−8.255	1.00	27.74		N
ATOM	3999	CA	VAL	A	93	−29.052	92.083	−8.161	1.00	27.69		C
ATOM	4000	C	VAL	A	93	−28.035	90.949	−8.156	1.00	32.05		C
ATOM	4001	O	VAL	A	93	−27.098	90.935	−8.970	1.00	32.98		O
ATOM	4002	CB	VAL	A	93	−30.043	91.925	−9.321	1.00	30.90		C
ATOM	4003	CG1	VAL	A	93	−30.675	90.530	−9.260	1.00	27.42		C
ATOM	4004	CG2	VAL	A	93	−31.106	93.006	−9.272	1.00	22.48		C
ATOM	4005	N	TYR	A	94	−28.210	90.005	−7.236	1.00	28.80		N
ATOM	4006	CA	TYR	A	94	−27.333	88.851	−7.090	1.00	27.10		C
ATOM	4007	C	TYR	A	94	−28.052	87.579	−7.535	1.00	30.77		C
ATOM	4008	O	TYR	A	94	−29.164	87.290	−7.070	1.00	32.21		O
ATOM	4009	CB	TYR	A	94	−26.849	88.711	−5.643	1.00	25.98		C
ATOM	4010	CG	TYR	A	94	−25.744	89.678	−5.299	1.00	35.21		C
ATOM	4011	CD1	TYR	A	94	−26.003	91.042	−5.195	1.00	33.48		C
ATOM	4012	CD2	TYR	A	94	−24.448	89.235	−5.071	1.00	28.53		C
ATOM	4013	CE1	TYR	A	94	−25.011	91.927	−4.887	1.00	31.11		C
ATOM	4014	CE2	TYR	A	94	−23.439	90.127	−4.754	1.00	34.57		C
ATOM	4015	CZ	TYR	A	94	−23.734	91.482	−4.674	1.00	34.25		C
ATOM	4016	OH	TYR	A	94	−22.756	92.410	−4.395	1.00	31.02		O
ATOM	4017	N	TYR	A	95	−27.399	86.815	−8.412	1.00	27.50		N
ATOM	4018	CA	TYR	A	95	−27.904	85.566	−8.958	1.00	28.28		C
ATOM	4019	C	TYR	A	95	−26.990	84.436	−8.531	1.00	30.88		C
ATOM	4020	O	TYR	A	95	−25.769	84.610	−8.464	1.00	30.35		O
ATOM	4021	CB	TYR	A	95	−27.948	85.576	−10.497	1.00	23.11		C
ATOM	4022	CG	TYR	A	95	−28.742	86.673	−11.106	1.00	28.17		C
ATOM	4023	CD1	TYR	A	95	−30.120	86.537	−11.313	1.00	35.38		C
ATOM	4024	CD2	TYR	A	95	−28.128	87.864	−11.486	1.00	31.26		C
ATOM	4025	CE1	TYR	A	95	−30.863	87.559	−11.882	1.00	29.38		C
ATOM	4026	CE2	TYR	A	95	−28.854	88.887	−12.059	1.00	27.86		C
ATOM	4027	CZ	TYR	A	95	−30.210	88.733	−12.251	1.00	32.29		C
ATOM	4028	OH	TYR	A	95	−30.913	89.752	−12.812	1.00	36.01		O
ATOM	4029	N	CYS	A	96	−27.576	83.288	−8.237	1.00	28.07		N
ATOM	4030	CA	CYS	A	96	−26.795	82.069	−8.201	1.00	31.83		C
ATOM	4031	C	CYS	A	96	−27.035	81.314	−9.498	1.00	30.66		C
ATOM	4032	O	CYS	A	96	−28.063	81.482	−10.165	1.00	27.69		O
ATOM	4033	CB	CYS	A	96	−27.113	81.176	−6.989	1.00	35.63		C
ATOM	4034	SG	CYS	A	96	−28.807	80.660	−6.800	1.00	52.39		S
ATOM	4035	N	ALA	A	97	−26.055	80.500	−9.860	1.00	25.32		N
ATOM	4036	CA	ALA	A	97	−26.171	79.615	−11.005	1.00	29.44		C
ATOM	4037	C	ALA	A	97	−25.383	78.346	−10.695	1.00	29.42		C
ATOM	4038	O	ALA	A	97	−24.512	78.346	−9.823	1.00	32.47		O
ATOM	4039	CB	ALA	A	97	−25.671	80.294	−12.287	1.00	26.70		C
ATOM	4040	N	ASN	A	98	−25.693	77.251	−11.396	1.00	25.38		N
ATOM	4041	CA	ASN	A	98	−24.856	76.072	−11.236	1.00	31.07		C
ATOM	4042	C	ASN	A	98	−23.922	75.893	−12.441	1.00	25.38		C
ATOM	4043	O	ASN	A	98	−23.936	76.655	−13.416	1.00	26.89		O
ATOM	4044	CB	ASN	A	98	−25.714	74.832	−10.962	1.00	26.42		C
ATOM	4045	CG	ASN	A	98	−26.528	74.385	−12.153	1.00	31.33		C
ATOM	4046	OD1	ASN	A	98	−26.444	74.948	−13.257	1.00	31.54		O
ATOM	4047	ND2	ASN	A	98	−27.362	73.366	−11.925	1.00	34.14		N
ATOM	4048	N	TRP	A	99	−23.088	74.869	−12.372	1.00	27.06		N
ATOM	4049	CA	TRP	A	99	−22.251	74.549	−13.521	1.00	30.36		C
ATOM	4050	C	TRP	A	99	−22.064	73.046	−13.590	1.00	30.04		C
ATOM	4051	O	TRP	A	99	−21.903	72.391	−12.555	1.00	29.39		O
ATOM	4052	CB	TRP	A	99	−20.897	75.266	−13.450	1.00	25.45		C
ATOM	4053	CG	TRP	A	99	−19.972	74.863	−12.353	1.00	29.81		C
ATOM	4054	CD1	TRP	A	99	−19.834	75.449	−11.122	1.00	28.02		C
ATOM	4055	CD2	TRP	A	99	−18.997	73.810	−12.408	1.00	26.75		C
ATOM	4056	NE1	TRP	A	99	−18.818	74.830	−10.414	1.00	23.44		N
ATOM	4057	CE2	TRP	A	99	−18.300	73.816	−11.178	1.00	25.89		C
ATOM	4058	CE3	TRP	A	99	−18.634	72.880	−13.385	1.00	28.32		C
ATOM	4059	CZ2	TRP	A	99	−17.278	72.904	−10.891	1.00	30.78		C
ATOM	4060	CZ3	TRP	A	99	−17.613	71.972	−13.101	1.00	30.19		C
ATOM	4061	CH2	TRP	A	99	−16.951	71.992	−11.859	1.00	28.00		C
ATOM	4062	N	TYR	A	100	−22.084	72.513	−14.814	1.00	30.79		N
ATOM	4063	CA	TYR	A	100	−22.044	71.070	−15.081	1.00	34.23		C
ATOM	4064	C	TYR	A	100	−20.741	70.594	−15.703	1.00	36.36		C
ATOM	4065	O	TYR	A	100	−20.246	69.521	−15.339	1.00	31.49		O
ATOM	4066	CB	TYR	A	100	−23.188	70.657	−16.023	1.00	29.48		C
ATOM	4067	CG	TYR	A	100	−24.563	70.844	−15.457	1.00	29.45		C
ATOM	4068	CD1	TYR	A	100	−24.812	70.621	−14.106	1.00	32.61		C
ATOM	4069	CD2	TYR	A	100	−25.623	71.233	−16.273	1.00	31.46		C
ATOM	4070	CE1	TYR	A	100	−26.081	70.796	−13.576	1.00	32.67		C
ATOM	4071	CE2	TYR	A	100	−26.904	71.403	−15.756	1.00	30.44		C
ATOM	4072	CZ	TYR	A	100	−27.124	71.173	−14.404	1.00	31.95		C
ATOM	4073	OH	TYR	A	100	−28.372	71.337	−13.866	1.00	30.17		O
ATOM	4074	N	TYR	A	101	−20.183	71.382	−16.626	1.00	29.07		N
ATOM	4075	CA	TYR	A	101	−19.125	70.940	−17.527	1.00	29.25		C
ATOM	4076	C	TYR	A	101	−17.797	71.608	−17.189	1.00	34.28		C
ATOM	4077	O	TYR	A	101	−16.868	70.944	−16.723	1.00	35.11		O
ATOM	4078	CB	TYR	A	101	−19.548	71.243	−18.955	1.00	24.67		C
ATOM	4079	CG	TYR	A	101	−20.914	70.690	−19.282	1.00	32.07		C
ATOM	4080	CD1	TYR	A	101	−21.119	69.317	−19.342	1.00	32.40		C
ATOM	4081	CD2	TYR	A	101	−21.996	71.534	−19.549	1.00	27.53		C
ATOM	4082	CE1	TYR	A	101	−22.357	68.791	−19.657	1.00	33.92		C
ATOM	4083	CE2	TYR	A	101	−23.255	71.019	−19.850	1.00	27.34		C
ATOM	4084	CZ	TYR	A	101	−23.419	69.641	−19.902	1.00	34.29		C
ATOM	4085	OH	TYR	A	101	−24.622	69.081	−20.215	1.00	35.46		O
ATOM	4086	N	TYR	A	102	−17.670	72.911	−17.415	1.00	28.83		N
ATOM	4087	CA	TYR	A	102	−16.483	73.631	−16.998	1.00	29.54		C
ATOM	4088	C	TYR	A	102	−16.872	74.660	−15.951	1.00	31.00		C
ATOM	4089	O	TYR	A	102	−17.957	75.244	−16.004	1.00	33.23		O
ATOM	4090	CB	TYR	A	102	−15.761	74.287	−18.187	1.00	27.78		C
ATOM	4091	CG	TYR	A	102	−16.664	74.965	−19.187	1.00	30.93		C
ATOM	4092	CD1	TYR	A	102	−17.186	74.251	−20.261	1.00	31.23		C
ATOM	4093	CD2	TYR	A	102	−16.985	76.326	−19.074	1.00	27.14		C
ATOM	4094	CE1	TYR	A	102	−18.004	74.864	−21.204	1.00	29.52		C
ATOM	4095	CE2	TYR	A	102	−17.801	76.957	−20.027	1.00	26.32		C
ATOM	4096	CZ	TYR	A	102	−18.311	76.217	−21.086	1.00	29.71		C
ATOM	4097	OH	TYR	A	102	−19.120	76.803	−22.045	1.00	27.38		O
ATOM	4098	N	TYR	A	103	−15.960	74.870	−15.000	1.00	33.17		N
ATOM	4099	CA	TYR	A	103	−16.282	75.569	−13.768	1.00	30.18		C
ATOM	4100	C	TYR	A	103	−16.585	77.043	−13.983	1.00	30.85		C
ATOM	4101	O	TYR	A	103	−17.198	77.659	−13.111	1.00	31.82		O
ATOM	4102	CB	TYR	A	103	−15.133	75.420	−12.772	1.00	30.32		C
ATOM	4103	CG	TYR	A	103	−13.820	76.094	−13.175	1.00	36.74		C
ATOM	4104	CD1	TYR	A	103	−12.864	75.419	−13.922	1.00	34.48		C
ATOM	4105	CD2	TYR	A	103	−13.527	77.399	−12.776	1.00	36.39		C
ATOM	4106	CE1	TYR	A	103	−11.652	76.031	−14.266	1.00	37.99		C
ATOM	4107	CE2	TYR	A	103	−12.332	78.012	−13.120	1.00	34.39		C
ATOM	4108	CZ	TYR	A	103	−11.394	77.329	−13.860	1.00	40.90		C
ATOM	4109	OH	TYR	A	103	−10.196	77.947	−14.206	1.00	43.10		O
ATOM	4110	N	TYR	A	104	−16.189	77.616	−15.112	1.00	27.43		N
ATOM	4111	CA	TYR	A	104	−16.416	79.027	−15.373	1.00	29.07		C
ATOM	4112	C	TYR	A	104	−17.599	79.242	−16.291	1.00	28.87		C
ATOM	4113	O	TYR	A	104	−17.791	80.354	−16.780	1.00	35.12		O
ATOM	4114	CB	TYR	A	104	−15.149	79.690	−15.953	1.00	25.68		C
ATOM	4115	CG	TYR	A	104	−14.499	78.931	−17.095	1.00	30.36		C
ATOM	4116	CD1	TYR	A	104	−13.573	77.894	−16.846	1.00	29.10		C
ATOM	4117	CD2	TYR	A	104	−14.813	79.233	−18.429	1.00	27.13		C
ATOM	4118	CE1	TYR	A	104	−12.964	77.181	−17.913	1.00	27.53		C
ATOM	4119	CE2	TYR	A	104	−14.225	78.528	−19.494	1.00	27.81		C
ATOM	4120	CZ	TYR	A	104	−13.296	77.508	−19.232	1.00	31.37		C
ATOM	4121	OH	TYR	A	104	−12.708	76.829	−20.282	1.00	33.25		O
ATOM	4122	N	GLY	A	105	−18.385	78.199	−16.546	1.00	33.05		N
ATOM	4123	CA	GLY	A	105	−19.642	78.324	−17.262	1.00	28.37		C
ATOM	4124	C	GLY	A	105	−20.806	78.259	−16.290	1.00	33.54		C
ATOM	4125	O	GLY	A	105	−20.731	77.601	−15.262	1.00	36.54		O
ATOM	4126	N	MET	A	106	−21.885	78.955	−16.614	1.00	33.38		N
ATOM	4127	CA	MET	A	106	−23.107	78.909	−15.818	1.00	33.92		C
ATOM	4128	C	MET	A	106	−24.192	78.210	−16.619	1.00	33.40		C
ATOM	4129	O	MET	A	106	−24.516	78.645	−17.727	1.00	41.54		O
ATOM	4130	CB	MET	A	106	−23.575	80.314	−15.438	1.00	31.98		C
ATOM	4131	CG	MET	A	106	−22.640	81.023	−14.492	1.00	38.84		C
ATOM	4132	SD	MET	A	106	−21.690	82.292	−15.342	1.00	39.21		S
ATOM	4133	CE	MET	A	106	−20.191	82.280	−14.355	1.00	44.14		C
ATOM	4134	N	ASP	A	107	−24.786	77.161	−16.049	1.00	30.51		N
ATOM	4135	CA	ASP	A	107	−25.760	76.380	−16.809	1.00	30.12		C
ATOM	4136	C	ASP	A	107	−27.213	76.688	−16.421	1.00	31.04		C
ATOM	4137	O	ASP	A	107	−28.019	76.977	−17.300	1.00	30.61		O
ATOM	4138	CB	ASP	A	107	−25.432	74.882	−16.678	1.00	32.36		C
ATOM	4139	CG	ASP	A	107	−24.108	74.509	−17.383	1.00	34.37		C
ATOM	4140	OD1	ASP	A	107	−24.105	74.413	−18.627	1.00	32.86		O1−
ATOM	4141	OD2	ASP	A	107	−23.060	74.339	−16.705	1.00	36.09		O
ATOM	4142	N	VAL	A	108	−27.581	76.603	−15.138	1.00	32.41		N
ATOM	4143	CA	VAL	A	108	−28.922	76.954	−14.662	1.00	26.51		C
ATOM	4144	C	VAL	A	108	−28.818	78.175	−13.754	1.00	32.76		C
ATOM	4145	O	VAL	A	108	−27.911	78.254	−12.920	1.00	31.62		O
ATOM	4146	CB	VAL	A	108	−29.590	75.776	−13.915	1.00	28.43		C
ATOM	4147	CG1	VAL	A	108	−31.028	76.146	−13.506	1.00	27.65		C
ATOM	4148	CG2	VAL	A	108	−29.617	74.516	−14.803	1.00	30.87		C
ATOM	4149	N	TRP	A	109	−29.752	79.117	−13.893	1.00	33.08		N
ATOM	4150	CA	TRP	A	109	−29.744	80.348	−13.102	1.00	34.02		C
ATOM	4151	C	TRP	A	109	−30.981	80.440	−12.208	1.00	33.68		C
ATOM	4152	O	TRP	A	109	−32.064	79.966	−12.563	1.00	33.19		O
ATOM	4153	CB	TRP	A	109	−29.716	81.605	−13.997	1.00	30.84		C
ATOM	4154	CG	TRP	A	109	−28.485	81.762	−14.834	1.00	36.98		C
ATOM	4155	CD1	TRP	A	109	−28.097	80.972	−15.893	1.00	30.27		C
ATOM	4156	CD2	TRP	A	109	−27.503	82.805	−14.730	1.00	31.30		C
ATOM	4157	NE1	TRP	A	109	−26.927	81.459	−16.432	1.00	31.83		N
ATOM	4158	CE2	TRP	A	109	−26.534	82.571	−15.731	1.00	29.54		C
ATOM	4159	CE3	TRP	A	109	−27.339	83.902	−13.875	1.00	30.44		C
ATOM	4160	CZ2	TRP	A	109	−25.409	83.392	−15.896	1.00	31.19		C
ATOM	4161	CZ3	TRP	A	109	−26.223	84.723	−14.042	1.00	30.38		C
ATOM	4162	CH2	TRP	A	109	−25.271	84.460	−15.043	1.00	29.90		C
ATOM	4163	N	GLY	A	110	−30.820	81.113	−11.066	1.00	29.11		N
ATOM	4164	CA	GLY	A	110	−31.931	81.457	−10.200	1.00	35.80		C
ATOM	4165	C	GLY	A	110	−32.644	82.701	−10.704	1.00	37.01		C
ATOM	4166	O	GLY	A	110	−32.532	83.075	−11.871	1.00	37.79		O
ATOM	4167	N	GLN	A	111	−33.399	83.358	−9.817	1.00	35.07		N
ATOM	4168	CA	GLN	A	111	−34.189	84.495	−10.276	1.00	30.15		C
ATOM	4169	C	GLN	A	111	−33.645	85.841	−9.831	1.00	32.38		C
ATOM	4170	O	GLN	A	111	−34.080	86.862	−10.372	1.00	33.82		O
ATOM	4171	CB	GLN	A	111	−35.644	84.410	−9.787	1.00	37.66		C
ATOM	4172	CG	GLN	A	111	−35.874	85.115	−8.454	1.00	36.90		C
ATOM	4173	CD	GLN	A	111	−35.642	84.208	−7.281	1.00	42.01		C
ATOM	4174	OE1	GLN	A	111	−35.896	82.996	−7.380	1.00	52.02		O
ATOM	4175	NE2	GLN	A	111	−35.176	84.777	−6.142	1.00	30.60		N
ATOM	4176	N	GLY	A	112	−32.755	85.872	−8.846	1.00	31.52		N
ATOM	4177	CA	GLY	A	112	−32.098	87.079	−8.391	1.00	29.27		C
ATOM	4178	C	GLY	A	112	−32.707	87.635	−7.114	1.00	30.54		C
ATOM	4179	O	GLY	A	112	−33.900	87.487	−6.840	1.00	36.59		O
ATOM	4180	N	THR	A	113	−31.873	88.297	−6.326	1.00	32.24		N
ATOM	4181	CA	THR	A	113	−32.301	89.057	−5.166	1.00	33.85		C
ATOM	4182	C	THR	A	113	−31.459	90.323	−5.122	1.00	32.53		C
ATOM	4183	O	THR	A	113	−30.284	90.295	−5.496	1.00	30.25		O
ATOM	4184	CB	THR	A	113	−32.150	88.240	−3.878	1.00	31.09		C
ATOM	4185	OG1	THR	A	113	−32.645	89.016	−2.780	1.00	36.12		O
ATOM	4186	CG2	THR	A	113	−30.672	87.868	−3.623	1.00	30.38		C
ATOM	4187	N	ATHR	A	114	−32.052	91.460	−4.734	0.50	32.93		N
ATOM	4188	CA	ATHR	A	114	−31.300	92.714	−4.776	0.50	30.39		C
ATOM	4189	C	ATHR	A	114	−30.691	93.019	−3.419	0.50	31.37		C
ATOM	4190	O	ATHR	A	114	−31.310	92.805	−2.374	0.50	33.91		O
ATOM	4191	CB	ATHR	A	114	−32.120	93.928	−5.266	0.50	31.38		C
ATOM	4192	OG1	ATHR	A	114	−31.978	95.061	−4.375	0.50	27.49		O
ATOM	4193	CG2	ATHR	A	114	−33.533	93.593	−5.476	0.50	26.66		C
ATOM	4194	N	BTHR	A	114	−32.061	91.410	−4.642	0.50	32.98		N
ATOM	4195	CA	BTHR	A	114	−31.413	92.712	−4.641	0.50	30.32		C
ATOM	4196	C	BTHR	A	114	−30.650	92.930	−3.345	0.50	31.38		C
ATOM	4197	O	BTHR	A	114	−31.141	92.610	−2.260	0.50	34.03		O
ATOM	4198	CB	BTHR	A	114	−32.434	93.834	−4.810	0.50	30.28		C
ATOM	4199	OG1	BTHR	A	114	−33.299	93.846	−3.681	0.50	37.62		O
ATOM	4200	CG2	BTHR	A	114	−33.258	93.627	−6.018	0.50	25.95		C
ATOM	4201	N	VAL	A	115	−29.451	93.489	−3.463	1.00	29.38		N
ATOM	4202	CA	VAL	A	115	−28.711	93.973	−2.317	1.00	31.80		C
ATOM	4203	C	VAL	A	115	−28.460	95.452	−2.583	1.00	32.96		C
ATOM	4204	O	VAL	A	115	−27.891	95.811	−3.622	1.00	32.78		O
ATOM	4205	CB	VAL	A	115	−27.392	93.209	−2.130	1.00	36.32		C
ATOM	4206	CG1	VAL	A	115	−26.569	93.856	−1.020	1.00	35.15		C
ATOM	4207	CG2	VAL	A	115	−27.651	91.686	−1.886	1.00	32.11		C
ATOM	4208	N	THR	A	116	−28.917	96.307	−1.676	1.00	32.75		N
ATOM	4209	CA	THR	A	116	−28.678	97.741	−1.754	1.00	34.57		C
ATOM	4210	C	THR	A	116	−27.787	98.139	−0.584	1.00	34.59		C
ATOM	4211	O	THR	A	116	−28.121	97.881	0.580	1.00	36.50		O
ATOM	4212	CB	THR	A	116	−29.995	98.522	−1.736	1.00	43.36		C
ATOM	4213	OG1	THR	A	116	−30.802	98.125	−2.856	1.00	40.71		O
ATOM	4214	CG2	THR	A	116	−29.731	100.021	−1.809	1.00	29.94		C
ATOM	4215	N	VAL	A	117	−26.649	98.738	−0.890	1.00	34.23		N
ATOM	4216	CA	VAL	A	117	−25.719	99.181	0.134	1.00	34.01		C
ATOM	4217	C	VAL	A	117	−25.756	100.691	0.076	1.00	33.64		C
ATOM	4218	O	VAL	A	117	−25.318	101.293	−0.906	1.00	37.46		O
ATOM	4219	CB	VAL	A	117	−24.301	98.631	−0.073	1.00	36.31		C
ATOM	4220	CG1	VAL	A	117	−23.392	99.053	1.093	1.00	33.46		C
ATOM	4221	CG2	VAL	A	117	−24.317	97.090	−0.232	1.00	29.32		C
ATOM	4222	N	SER	A	118	−26.359	101.302	1.081	1.00	39.03		N
ATOM	4223	CA	SER	A	118	−26.566	102.738	1.077	1.00	39.96		C
ATOM	4224	C	SER	A	118	−26.419	103.243	2.497	1.00	45.19		C
ATOM	4225	O	SER	A	118	−26.858	102.579	3.439	1.00	47.46		O
ATOM	4226	CB	SER	A	118	−27.961	103.097	0.529	1.00	38.81		C
ATOM	4227	OG	SER	A	118	−28.165	104.501	0.460	1.00	48.85		O
ATOM	4228	N	SER	A	119	−25.802	104.406	2.653	1.00	46.28		N
ATOM	4229	CA	SER	A	119	−25.847	105.090	3.935	1.00	53.97		C
ATOM	4230	C	SER	A	119	−26.871	106.217	3.954	1.00	56.65		C
ATOM	4231	O	SER	A	119	−26.985	106.913	4.961	1.00	67.20		O
ATOM	4232	CB	SER	A	119	−24.468	105.628	4.292	1.00	47.03		C
ATOM	4233	OG	SER	A	119	−23.903	106.260	3.168	1.00	54.58		O
ATOM	4234	N	ALA	A	120	−27.649	106.385	2.890	1.00	48.46		N
ATOM	4235	CA	ALA	A	120	−28.631	107.451	2.863	1.00	46.93		C
ATOM	4236	C	ALA	A	120	−29.791	107.119	3.793	1.00	50.99		C
ATOM	4237	O	ALA	A	120	−30.104	105.957	4.047	1.00	62.07		O
ATOM	4238	CB	ALA	A	120	−29.138	107.672	1.439	1.00	43.79		C
ATOM	4239	N	SER	A	121	−30.399	108.159	4.341	1.00	61.71	GZ00	N
ATOM	4240	CA	SER	A	121	−31.605	108.063	5.149	1.00	54.23	GZ00	C
ATOM	4241	C	SER	A	121	−32.579	109.105	4.648	1.00	47.84	GZ00	C
ATOM	4242	O	SER	A	121	−32.202	110.015	3.907	1.00	55.11	GZ00	O
ATOM	4243	CB	SER	A	121	−31.338	108.273	6.640	1.00	50.17	GZ00	C
ATOM	4244	OG	SER	A	121	−30.386	109.312	6.829	1.00	66.59	GZ00	O
ATOM	4245	N	THR	A	122	−33.838	108.938	5.041	1.00	46.14	GZ00	N
ATOM	4246	CA	THR	A	122	−34.934	109.776	4.572	1.00	52.42	GZ00	C
ATOM	4247	C	THR	A	122	−34.557	111.248	4.510	1.00	56.26	GZ00	C
ATOM	4248	O	THR	A	122	−33.924	111.783	5.426	1.00	48.53	GZ00	O
ATOM	4249	CB	THR	A	122	−36.129	109.606	5.486	1.00	52.24	GZ00	C
ATOM	4250	OG1	THR	A	122	−36.428	108.215	5.593	1.00	57.02	GZ00	O
ATOM	4251	CG2	THR	A	122	−37.310	110.342	4.912	1.00	53.18	GZ00	C
ATOM	4252	N	LYS	A	123	−34.894	111.876	3.385	1.00	54.75	GZ00	N
ATOM	4253	CA	LYS	A	123	−34.659	113.296	3.176	1.00	45.96	GZ00	C
ATOM	4254	C	LYS	A	123	−35.645	113.763	2.125	1.00	53.79	GZ00	C
ATOM	4255	O	LYS	A	123	−35.799	113.095	1.099	1.00	47.21	GZ00	O
ATOM	4256	CB	LYS	A	123	−33.228	113.577	2.727	1.00	48.41	GZ00	C
ATOM	4257	CG	LYS	A	123	−32.969	115.041	2.451	1.00	46.73	GZ00	C
ATOM	4258	CD	LYS	A	123	−31.559	115.291	1.972	1.00	52.19	GZ00	C
ATOM	4259	CE	LYS	A	123	−31.365	116.750	1.520	1.00	54.71	GZ00	C
ATOM	4260	NZ	LYS	A	123	−32.367	117.163	0.481	1.00	49.08	GZ00	N1+
ATOM	4261	N	GLY	A	124	−36.311	114.898	2.382	1.00	53.18	GZ00	N
ATOM	4262	CA	GLY	A	124	−37.243	115.482	1.440	1.00	35.65	GZ00	C
ATOM	4263	C	GLY	A	124	−36.503	116.234	0.347	1.00	38.66	GZ00	C
ATOM	4264	O	GLY	A	124	−35.330	116.589	0.499	1.00	39.24	GZ00	O
ATOM	4265	N	PRO	A	125	−37.165	116.475	−0.782	1.00	39.30	GZ00	N
ATOM	4266	CA	PRO	A	125	−36.474	117.071	−1.933	1.00	45.65	GZ00	C
ATOM	4267	C	PRO	A	125	−36.378	118.586	−1.844	1.00	46.64	GZ00	C
ATOM	4268	O	PRO	A	125	−37.212	119.253	−1.230	1.00	46.44	GZ00	O
ATOM	4269	CB	PRO	A	125	−37.378	116.684	−3.110	1.00	44.97	GZ00	C
ATOM	4270	CG	PRO	A	125	−38.764	116.674	−2.504	1.00	34.50	GZ00	C
ATOM	4271	CD	PRO	A	125	−38.573	116.145	−1.088	1.00	36.15	GZ00	C
ATOM	4272	N	SER	A	126	−35.358	119.126	−2.502	1.00	46.29	GZ00	N
ATOM	4273	CA	SER	A	126	−35.329	120.540	−2.858	1.00	46.55	GZ00	C
ATOM	4274	C	SER	A	126	−35.926	120.698	−4.247	1.00	51.08	GZ00	C
ATOM	4275	O	SER	A	126	−35.646	119.893	−5.139	1.00	52.88	GZ00	O
ATOM	4276	CB	SER	A	126	−33.903	121.093	−2.860	1.00	40.26	GZ00	C
ATOM	4277	OG	SER	A	126	−33.293	120.973	−1.591	1.00	55.79	GZ00	O
ATOM	4278	N	VAL	A	127	−36.744	121.735	−4.438	1.00	47.44	GZ00	N
ATOM	4279	CA	VAL	A	127	−37.420	121.956	−5.713	1.00	40.11	GZ00	C
ATOM	4280	C	VAL	A	127	−36.980	123.290	−6.314	1.00	43.78	GZ00	C
ATOM	4281	O	VAL	A	127	−37.076	124.339	−5.665	1.00	52.62	GZ00	O
ATOM	4282	CB	VAL	A	127	−38.948	121.898	−5.553	1.00	45.33	GZ00	C
ATOM	4283	CG1	VAL	A	127	−39.618	122.036	−6.908	1.00	44.26	GZ00	C
ATOM	4284	CG2	VAL	A	127	−39.359	120.584	−4.873	1.00	41.94	GZ00	C
ATOM	4285	N	PHE	A	128	−36.517	123.250	−7.564	1.00	40.88	GZ00	N
ATOM	4286	CA	PHE	A	128	−36.074	124.425	−8.285	1.00	43.70	GZ00	C
ATOM	4287	C	PHE	A	128	−36.857	124.590	−9.578	1.00	46.15	GZ00	C
ATOM	4288	O	PHE	A	128	−37.192	123.598	−10.227	1.00	47.49	GZ00	O
ATOM	4289	CB	PHE	A	128	−34.582	124.356	−8.615	1.00	42.40	GZ00	C
ATOM	4290	CG	PHE	A	128	−33.714	124.253	−7.406	1.00	49.59	GZ00	C
ATOM	4291	CD1	PHE	A	128	−33.404	125.389	−6.666	1.00	47.01	GZ00	C
ATOM	4292	CD2	PHE	A	128	−33.188	123.033	−7.012	1.00	45.42	GZ00	C
ATOM	4293	CE1	PHE	A	128	−32.604	125.308	−5.538	1.00	45.05	GZ00	C
ATOM	4294	CE2	PHE	A	128	−32.379	122.946	−5.890	1.00	55.33	GZ00	C
ATOM	4295	CZ	PHE	A	128	−32.084	124.085	−5.152	1.00	51.39	GZ00	C
ATOM	4296	N	PRO	A	129	−37.153	125.823	−9.985	1.00	44.34	GZ00	N
ATOM	4297	CA	PRO	A	129	−37.894	126.021	−11.233	1.00	46.78	GZ00	C
ATOM	4298	C	PRO	A	129	−36.975	125.867	−12.426	1.00	45.16	GZ00	C
ATOM	4299	O	PRO	A	129	−35.815	126.280	−12.397	1.00	53.62	GZ00	O
ATOM	4300	CB	PRO	A	129	−38.404	127.460	−11.109	1.00	47.94	GZ00	C
ATOM	4301	CG	PRO	A	129	−37.334	128.141	−10.336	1.00	40.44	GZ00	C
ATOM	4302	CD	PRO	A	129	−36.844	127.103	−9.323	1.00	47.69	GZ00	C
ATOM	4303	N	LEU	A	130	−37.486	125.227	−13.465	1.00	44.60	GZ00	N
ATOM	4304	CA	LEU	A	130	−36.794	125.147	−14.749	1.00	49.12	GZ00	C
ATOM	4305	C	LEU	A	130	−37.528	126.108	−15.677	1.00	54.30	GZ00	C
ATOM	4306	O	LEU	A	130	−38.580	125.769	−16.225	1.00	53.88	GZ00	O
ATOM	4307	CB	LEU	A	130	−36.764	123.714	−15.283	1.00	52.10	GZ00	C
ATOM	4308	CG	LEU	A	130	−36.085	122.707	−14.338	1.00	49.99	GZ00	C
ATOM	4309	CD1	LEU	A	130	−36.064	121.284	−14.876	1.00	44.72	GZ00	C
ATOM	4310	CD2	LEU	A	130	−34.670	123.167	−14.003	1.00	49.22	GZ00	C
ATOM	4311	N	ALA	A	131	−36.979	127.339	−15.828	1.00	51.83	GZ00	N
ATOM	4312	CA	ALA	A	131	−37.752	128.405	−16.461	1.00	60.57	GZ00	C
ATOM	4313	C	ALA	A	131	−37.777	128.241	−17.979	1.00	58.44	GZ00	C
ATOM	4314	O	ALA	A	131	−36.767	127.860	−18.578	1.00	62.01	GZ00	O
ATOM	4315	CB	ALA	A	131	−37.182	129.780	−16.118	1.00	52.12	GZ00	C
ATOM	4316	N	PRO	A	132	−38.922	128.508	−18.610	1.00	63.89	GZ00	N
ATOM	4317	CA	PRO	A	132	−38.974	128.551	−20.076	1.00	60.84	GZ00	C
ATOM	4318	C	PRO	A	132	−38.312	129.818	−20.583	1.00	68.50	GZ00	C
ATOM	4319	O	PRO	A	132	−38.605	130.917	−20.107	1.00	78.71	GZ00	O
ATOM	4320	CB	PRO	A	132	−40.477	128.546	−20.374	1.00	61.98	GZ00	C
ATOM	4321	CG	PRO	A	132	−41.076	129.218	−19.186	1.00	59.91	GZ00	C
ATOM	4322	CD	PRO	A	132	−40.239	128.787	−18.005	1.00	64.04	GZ00	C
ATOM	4323	N	SER	A	133	−37.403	129.660	−21.536	1.00	78.25	GZ00	N
ATOM	4324	CA	SER	A	133	−36.712	130.783	−22.151	1.00	90.93	GZ00	C
ATOM	4325	C	SER	A	133	−36.986	130.784	−23.647	1.00	95.12	GZ00	C
ATOM	4326	O	SER	A	133	−37.432	129.785	−24.219	1.00	92.73	GZ00	O
ATOM	4327	CB	SER	A	133	−35.195	130.741	−21.878	1.00	93.56	GZ00	C
ATOM	4328	OG	SER	A	133	−34.721	129.411	−21.727	1.00	92.59	GZ00	O
ATOM	4329	N	SER	A	134	−36.724	131.923	−24.279	1.00	101.62	GZ00	N
ATOM	4330	CA	SER	A	134	−37.027	132.073	−25.696	1.00	101.63	GZ00	C
ATOM	4331	C	SER	A	134	−35.957	131.408	−26.549	1.00	98.00	GZ00	C
ATOM	4332	O	SER	A	134	−36.000	130.197	−26.770	1.00	105.90	GZ00	O
ATOM	4333	CB	SER	A	134	−37.165	133.548	−26.069	1.00	96.91	GZ00	C
ATOM	4334	OG	SER	A	134	−37.994	133.692	−27.209	1.00	104.41	GZ00	O
ATOM	4335	N	GLY	A	139	−42.971	131.608	−30.259	1.00	100.95	GZ00	N
ATOM	4336	CA	GLY	A	139	−44.001	130.908	−31.008	1.00	110.26	GZ00	C
ATOM	4337	C	GLY	A	139	−43.531	129.600	−31.626	1.00	116.15	GZ00	C
ATOM	4338	O	GLY	A	139	−42.529	129.576	−32.345	1.00	129.42	GZ00	O
ATOM	4339	N	GLY	A	140	−44.252	128.512	−31.352	1.00	102.94	GZ00	N
ATOM	4340	CA	GLY	A	140	−45.429	128.577	−30.509	1.00	98.08	GZ00	C
ATOM	4341	C	GLY	A	140	−45.549	127.510	−29.435	1.00	93.20	GZ00	C
ATOM	4342	O	GLY	A	140	−46.648	127.229	−28.960	1.00	88.91	GZ00	O
ATOM	4343	N	THR	A	141	−44.427	126.906	−29.049	1.00	94.52	GZ00	N
ATOM	4344	CA	THR	A	141	−44.434	125.891	−28.005	1.00	84.86	GZ00	C
ATOM	4345	C	THR	A	141	−43.275	126.163	−27.053	1.00	82.99	GZ00	C
ATOM	4346	O	THR	A	141	−42.191	126.566	−27.485	1.00	81.83	GZ00	O
ATOM	4347	CB	THR	A	141	−44.353	124.474	−28.595	1.00	90.26	GZ00	C
ATOM	4348	OG1	THR	A	141	−44.628	123.513	−27.566	1.00	85.35	GZ00	O
ATOM	4349	CG2	THR	A	141	−42.971	124.203	−29.232	1.00	79.54	GZ00	C
ATOM	4350	N	ALA	A	142	−43.506	125.953	−25.756	1.00	80.86	GZ00	N
ATOM	4351	CA	ALA	A	142	−42.487	126.212	−24.745	1.00	77.11	GZ00	C
ATOM	4352	C	ALA	A	142	−42.460	125.082	−23.731	1.00	70.08	GZ00	C
ATOM	4353	O	ALA	A	142	−43.508	124.527	−23.382	1.00	69.86	GZ00	O
ATOM	4354	CB	ALA	A	142	−42.731	127.539	−24.014	1.00	76.03	GZ00	C
ATOM	4355	N	ALA	A	143	−41.262	124.748	−23.262	1.00	59.75	GZ00	N
ATOM	4356	CA	ALA	A	143	−41.079	123.717	−22.248	1.00	63.56	GZ00	C
ATOM	4357	C	ALA	A	143	−40.608	124.351	−20.947	1.00	58.18	GZ00	C
ATOM	4358	O	ALA	A	143	−39.664	125.152	−20.948	1.00	54.35	GZ00	O
ATOM	4359	CB	ALA	A	143	−40.072	122.666	−22.710	1.00	62.26	GZ00	C
ATOM	4360	N	LEU	A	144	−41.241	123.961	−19.840	1.00	51.02	GZ00	N
ATOM	4361	CA	LEU	A	144	−40.864	124.417	−18.507	1.00	54.73	GZ00	C
ATOM	4362	C	LEU	A	144	−41.027	123.254	−17.537	1.00	53.32	GZ00	C
ATOM	4363	O	LEU	A	144	−41.753	122.293	−17.812	1.00	53.18	GZ00	O
ATOM	4364	CB	LEU	A	144	−41.709	125.621	−18.047	1.00	46.73	GZ00	C
ATOM	4365	CG	LEU	A	144	−43.215	125.351	−17.951	1.00	56.02	GZ00	C
ATOM	4366	CD1	LEU	A	144	−43.665	125.025	−16.521	1.00	52.68	GZ00	C
ATOM	4367	CD2	LEU	A	144	−44.014	126.520	−18.513	1.00	58.59	GZ00	C
ATOM	4368	N	GLY	A	145	−40.359	123.341	−16.391	1.00	51.88	GZ00	N
ATOM	4369	CA	GLY	A	145	−40.399	122.209	−15.497	1.00	48.27	GZ00	C
ATOM	4370	C	GLY	A	145	−39.960	122.514	−14.085	1.00	51.16	GZ00	C
ATOM	4371	O	GLY	A	145	−39.791	123.673	−13.698	1.00	53.82	GZ00	O
ATOM	4372	N	CYS	A	146	−39.798	121.434	−13.315	1.00	44.69	GZ00	N
ATOM	4373	CA	CYS	A	146	−39.413	121.470	−11.910	1.00	47.10	GZ00	C
ATOM	4374	C	CYS	A	146	−38.297	120.462	−11.680	1.00	45.37	GZ00	C
ATOM	4375	O	CYS	A	146	−38.433	119.290	−12.038	1.00	42.62	GZ00	O
ATOM	4376	CB	CYS	A	146	−40.597	121.139	−10.990	1.00	47.73	GZ00	C
ATOM	4377	SG	CYS	A	146	−41.531	122.590	−10.443	1.00	76.23	GZ00	S
ATOM	4378	N	LEU	A	147	−37.207	120.910	−11.080	1.00	47.76	GZ00	N
ATOM	4379	CA	LEU	A	147	−36.102	120.037	−10.725	1.00	40.76	GZ00	C
ATOM	4380	C	LEU	A	147	−36.281	119.619	−9.279	1.00	43.78	GZ00	C
ATOM	4381	O	LEU	A	147	−36.273	120.470	−8.388	1.00	44.48	GZ00	O
ATOM	4382	CB	LEU	A	147	−34.767	120.742	−10.938	1.00	37.72	GZ00	C
ATOM	4383	CG	LEU	A	147	−33.513	120.047	−10.400	1.00	47.51	GZ00	C
ATOM	4384	CD1	LEU	A	147	−33.360	118.653	−10.996	1.00	40.15	GZ00	C
ATOM	4385	CD2	LEU	A	147	−32.260	120.918	−10.669	1.00	37.25	GZ00	C
ATOM	4386	N	VAL	A	148	−36.396	118.311	−9.046	1.00	48.64	GZ00	N
ATOM	4387	CA	VAL	A	148	−36.699	117.743	−7.733	1.00	46.35	GZ00	C
ATOM	4388	C	VAL	A	148	−35.441	117.031	−7.252	1.00	49.34	GZ00	C
ATOM	4389	O	VAL	A	148	−35.200	115.861	−7.576	1.00	50.72	GZ00	O
ATOM	4390	CB	VAL	A	148	−37.896	116.788	−7.790	1.00	38.94	GZ00	C
ATOM	4391	CG1	VAL	A	148	−38.234	116.266	−6.410	1.00	40.39	GZ00	C
ATOM	4392	CG2	VAL	A	148	−39.087	117.487	−8.380	1.00	40.04	GZ00	C
ATOM	4393	N	LYS	A	149	−34.660	117.721	−6.440	1.00	45.78	GZ00	N
ATOM	4394	CA	LYS	A	149	−33.291	117.334	−6.155	1.00	45.80	GZ00	C
ATOM	4395	C	LYS	A	149	−33.137	116.710	−4.774	1.00	47.10	GZ00	C
ATOM	4396	O	LYS	A	149	−33.791	117.126	−3.815	1.00	47.43	GZ00	O
ATOM	4397	CB	LYS	A	149	−32.379	118.554	−6.266	1.00	47.24	GZ00	C
ATOM	4398	CG	LYS	A	149	−31.174	118.293	−7.097	1.00	56.69	GZ00	C
ATOM	4399	CD	LYS	A	149	−29.975	119.004	−6.564	1.00	59.82	GZ00	C
ATOM	4400	CE	LYS	A	149	−30.099	120.481	−6.760	1.00	57.45	GZ00	C
ATOM	4401	NZ	LYS	A	149	−28.781	121.117	−6.434	1.00	60.94	GZ00	N1+
ATOM	4402	N	ASP	A	150	−32.254	115.710	−4.694	1.00	49.92	GZ00	N
ATOM	4403	CA	ASP	A	150	−31.630	115.231	−3.456	1.00	45.59	GZ00	C
ATOM	4404	C	ASP	A	150	−32.643	114.736	−2.423	1.00	44.92	GZ00	C
ATOM	4405	O	ASP	A	150	−32.679	115.208	−1.289	1.00	51.88	GZ00	O
ATOM	4406	CB	ASP	A	150	−30.741	116.314	−2.838	1.00	42.77	GZ00	C
ATOM	4407	CG	ASP	A	150	−29.533	116.637	−3.689	1.00	56.92	GZ00	C
ATOM	4408	OD1	ASP	A	150	−29.136	115.782	−4.512	1.00	57.01	GZ00	O
ATOM	4409	OD2	ASP	A	150	−28.970	117.747	−3.525	1.00	62.51	GZ00	O1−
ATOM	4410	N	TYR	A	151	−33.415	113.725	−2.802	1.00	45.00	GZ00	N
ATOM	4411	CA	TYR	A	151	−34.367	113.102	−1.894	1.00	49.20	GZ00	C
ATOM	4412	C	TYR	A	151	−34.088	111.606	−1.765	1.00	57.02	GZ00	C
ATOM	4413	O	TYR	A	151	−33.356	111.009	−2.563	1.00	54.16	GZ00	O
ATOM	4414	CB	TYR	A	151	−35.807	113.316	−2.346	1.00	41.84	GZ00	C
ATOM	4415	CG	TYR	A	151	−36.146	112.630	−3.642	1.00	53.39	GZ00	C
ATOM	4416	CD1	TYR	A	151	−36.579	111.294	−3.672	1.00	58.67	GZ00	C
ATOM	4417	CD2	TYR	A	151	−36.045	113.316	−4.845	1.00	47.72	GZ00	C
ATOM	4418	CE1	TYR	A	151	−36.898	110.679	−4.879	1.00	55.52	GZ00	C
ATOM	4419	CE2	TYR	A	151	−36.365	112.718	−6.041	1.00	47.90	GZ00	C
ATOM	4420	CZ	TYR	A	151	−36.782	111.403	−6.063	1.00	54.44	GZ00	C
ATOM	4421	OH	TYR	A	151	−37.077	110.834	−7.286	1.00	56.96	GZ00	O
ATOM	4422	N	PHE	A	152	−34.688	111.011	−0.737	1.00	52.17	GZ00	N
ATOM	4423	CA	PHE	A	152	−34.494	109.613	−0.424	1.00	56.95	GZ00	C
ATOM	4424	C	PHE	A	152	−35.543	109.170	0.575	1.00	59.21	GZ00	C
ATOM	4425	O	PHE	A	152	−35.877	109.929	1.472	1.00	56.82	GZ00	O
ATOM	4426	CB	PHE	A	152	−33.097	109.382	0.144	1.00	56.68	GZ00	C
ATOM	4427	CG	PHE	A	152	−32.764	107.946	0.349	1.00	56.75	GZ00	C
ATOM	4428	CD1	PHE	A	152	−33.106	107.301	1.528	1.00	57.37	GZ00	C
ATOM	4429	CD2	PHE	A	152	−32.097	107.233	−0.640	1.00	61.45	GZ00	C
ATOM	4430	CE1	PHE	A	152	−32.796	105.963	1.718	1.00	62.30	GZ00	C
ATOM	4431	CE2	PHE	A	152	−31.784	105.899	−0.457	1.00	54.88	GZ00	C
ATOM	4432	CZ	PHE	A	152	−32.136	105.258	0.722	1.00	52.68	GZ00	C
ATOM	4433	N	PRO	A	153	−36.081	107.947	0.414	1.00	64.15	GZ00	N
ATOM	4434	CA	PRO	A	153	−35.890	107.052	−0.728	1.00	60.57	GZ00	C
ATOM	4435	C	PRO	A	153	−36.949	107.343	−1.784	1.00	57.01	GZ00	C
ATOM	4436	O	PRO	A	153	−37.736	108.261	−1.579	1.00	57.18	GZ00	O
ATOM	4437	CB	PRO	A	153	−36.104	105.684	−0.109	1.00	56.69	GZ00	C
ATOM	4438	CG	PRO	A	153	−37.250	105.962	0.843	1.00	50.72	GZ00	C
ATOM	4439	CD	PRO	A	153	−36.942	107.317	1.434	1.00	59.37	GZ00	C
ATOM	4440	N	GLU	A	154	−37.022	106.550	−2.848	1.00	55.69	GZ00	N
ATOM	4441	CA	GLU	A	154	−38.086	106.727	−3.833	1.00	52.35	GZ00	C
ATOM	4442	C	GLU	A	154	−39.389	106.318	−3.182	1.00	47.39	GZ00	C
ATOM	4443	O	GLU	A	154	−39.364	105.619	−2.171	1.00	52.96	GZ00	O
ATOM	4444	CB	GLU	A	154	−37.805	105.905	−5.093	1.00	53.56	GZ00	C
ATOM	4445	CG	GLU	A	154	−36.530	106.322	−5.818	1.00	58.65	GZ00	C
ATOM	4446	CD	GLU	A	154	−36.727	106.415	−7.315	1.00	67.26	GZ00	C
ATOM	4447	OE1	GLU	A	154	−36.043	105.662	−8.041	1.00	74.85	GZ00	O
ATOM	4448	OE2	GLU	A	154	−37.572	107.227	−7.765	1.00	66.72	GZ00	O1−
ATOM	4449	N	PRO	A	155	−40.533	106.779	−3.713	1.00	45.32	GZ00	N
ATOM	4450	CA	PRO	A	155	−40.792	107.703	−4.827	1.00	55.68	GZ00	C
ATOM	4451	C	PRO	A	155	−41.144	109.144	−4.437	1.00	57.15	GZ00	C
ATOM	4452	O	PRO	A	155	−41.413	109.427	−3.272	1.00	61.59	GZ00	O
ATOM	4453	CB	PRO	A	155	−42.020	107.086	−5.474	1.00	54.31	GZ00	C
ATOM	4454	CG	PRO	A	155	−42.813	106.627	−4.281	1.00	36.78	GZ00	C
ATOM	4455	CD	PRO	A	155	−41.792	106.177	−3.235	1.00	36.78	GZ00	C
ATOM	4456	N	VAL	A	156	−41.135	110.047	−5.417	1.00	56.20	GZ00	N
ATOM	4457	CA	VAL	A	156	−41.884	111.294	−5.339	1.00	56.13	GZ00	C
ATOM	4458	C	VAL	A	156	−42.962	111.242	−6.407	1.00	55.59	GZ00	C
ATOM	4459	O	VAL	A	156	−42.818	110.570	−7.432	1.00	66.78	GZ00	O
ATOM	4460	CB	VAL	A	156	−41.023	112.567	−5.514	1.00	57.46	GZ00	C
ATOM	4461	CG1	VAL	A	156	−40.008	112.698	−4.399	1.00	56.24	GZ00	C
ATOM	4462	CG2	VAL	A	156	−40.327	112.555	−6.838	1.00	58.46	GZ00	C
ATOM	4463	N	THR	A	157	−44.052	111.949	−6.156	1.00	55.63	GZ00	N
ATOM	4464	CA	THR	A	157	−45.091	112.189	−7.145	1.00	48.48	GZ00	C
ATOM	4465	C	THR	A	157	−45.079	113.673	−7.480	1.00	56.97	GZ00	C
ATOM	4466	O	THR	A	157	−44.819	114.506	−6.606	1.00	54.54	GZ00	O
ATOM	4467	CB	THR	A	157	−46.464	111.777	−6.608	1.00	58.63	GZ00	C
ATOM	4468	OG1	THR	A	157	−46.837	112.659	−5.542	1.00	69.16	GZ00	O
ATOM	4469	CG2	THR	A	157	−46.413	110.369	−6.046	1.00	52.02	GZ00	C
ATOM	4470	N	VAL	A	158	−45.317	114.003	−8.747	1.00	52.48	GZ00	N
ATOM	4471	CA	VAL	A	158	−45.344	115.385	−9.209	1.00	49.55	GZ00	C
ATOM	4472	C	VAL	A	158	−46.619	115.606	−10.001	1.00	53.68	GZ00	C
ATOM	4473	O	VAL	A	158	−46.942	114.809	−10.885	1.00	58.24	GZ00	O
ATOM	4474	CB	VAL	A	158	−44.131	115.743	−10.087	1.00	53.34	GZ00	C
ATOM	4475	CG1	VAL	A	158	−44.181	117.245	−10.447	1.00	47.23	GZ00	C
ATOM	4476	CG2	VAL	A	158	−42.819	115.357	−9.407	1.00	50.02	GZ00	C
ATOM	4477	N	SER	A	159	−47.337	116.684	−9.693	1.00	53.96	GZ00	N
ATOM	4478	CA	SER	A	159	−48.485	117.098	−10.485	1.00	54.02	GZ00	C
ATOM	4479	C	SER	A	159	−48.334	118.563	−10.856	1.00	57.99	GZ00	C
ATOM	4480	O	SER	A	159	−47.487	119.282	−10.319	1.00	58.35	GZ00	O
ATOM	4481	CB	SER	A	159	−49.802	116.870	−9.741	1.00	57.03	GZ00	C
ATOM	4482	OG	SER	A	159	−49.841	117.623	−8.548	1.00	64.29	GZ00	O
ATOM	4483	N	TRP	A	160	−49.143	119.008	−11.804	1.00	52.93	GZ00	N
ATOM	4484	CA	TRP	A	160	−49.127	120.403	−12.198	1.00	53.69	GZ00	C
ATOM	4485	C	TRP	A	160	−50.507	120.996	−11.965	1.00	60.22	GZ00	C
ATOM	4486	O	TRP	A	160	−51.524	120.353	−12.254	1.00	56.05	GZ00	O
ATOM	4487	CB	TRP	A	160	−48.667	120.551	−13.654	1.00	52.01	GZ00	C
ATOM	4488	CG	TRP	A	160	−47.199	120.239	−13.791	1.00	61.18	GZ00	C
ATOM	4489	CD1	TRP	A	160	−46.630	119.002	−13.982	1.00	51.63	GZ00	C
ATOM	4490	CD2	TRP	A	160	−46.108	121.169	−13.703	1.00	51.85	GZ00	C
ATOM	4491	NE1	TRP	A	160	−45.260	119.116	−14.035	1.00	51.65	GZ00	N
ATOM	4492	CE2	TRP	A	160	−44.914	120.433	−13.871	1.00	55.17	GZ00	C
ATOM	4493	CE3	TRP	A	160	−46.025	122.550	−13.513	1.00	49.96	GZ00	C
ATOM	4494	CZ2	TRP	A	160	−43.654	121.035	−13.847	1.00	52.75	GZ00	C
ATOM	4495	CZ3	TRP	A	160	−44.772	123.148	−13.502	1.00	55.98	GZ00	C
ATOM	4496	CH2	TRP	A	160	−43.604	122.389	−13.663	1.00	51.25	GZ00	C
ATOM	4497	N	ASN	A	161	−50.521	122.215	−11.417	1.00	59.30	GZ00	N
ATOM	4498	CA	ASN	A	161	−51.738	122.946	−11.048	1.00	53.77	GZ00	C
ATOM	4499	C	ASN	A	161	−52.737	122.039	−10.336	1.00	58.01	GZ00	C
ATOM	4500	O	ASN	A	161	−53.929	122.014	−10.642	1.00	64.68	GZ00	O
ATOM	4501	CB	ASN	A	161	−52.353	123.615	−12.267	1.00	42.97	GZ00	C
ATOM	4502	CG	ASN	A	161	−51.430	124.645	−12.851	1.00	59.88	GZ00	C
ATOM	4503	OD1	ASN	A	161	−50.421	124.988	−12.231	1.00	57.52	GZ00	O
ATOM	4504	ND2	ASN	A	161	−51.743	125.141	−14.043	1.00	62.17	GZ00	N
ATOM	4505	N	SER	A	162	−52.218	121.280	−9.367	1.00	60.34	GZ00	N
ATOM	4506	CA	SER	A	162	−53.022	120.430	−8.483	1.00	66.27	GZ00	C
ATOM	4507	C	SER	A	162	−53.790	119.353	−9.244	1.00	71.65	GZ00	C
ATOM	4508	O	SER	A	162	−54.873	118.941	−8.821	1.00	79.00	GZ00	O
ATOM	4509	CB	SER	A	162	−53.984	121.273	−7.641	1.00	67.29	GZ00	C
ATOM	4510	OG	SER	A	162	−53.287	122.322	−6.987	1.00	70.91	GZ00	O
ATOM	4511	N	GLY	A	163	−53.224	118.858	−10.349	1.00	70.85	GZ00	N
ATOM	4512	CA	GLY	A	163	−53.876	117.868	−11.181	1.00	59.17	GZ00	C
ATOM	4513	C	GLY	A	163	−54.598	118.443	−12.385	1.00	68.56	GZ00	C
ATOM	4514	O	GLY	A	163	−55.017	117.675	−13.255	1.00	76.49	GZ00	O
ATOM	4515	N	ALA	A	164	−54.744	119.772	−12.463	1.00	67.36	GZ00	N
ATOM	4516	CA	ALA	A	164	−55.483	120.392	−13.561	1.00	63.96	GZ00	C
ATOM	4517	C	ALA	A	164	−54.755	120.239	−14.885	1.00	68.34	GZ00	C
ATOM	4518	O	ALA	A	164	−55.391	120.060	−15.927	1.00	75.07	GZ00	O
ATOM	4519	CB	ALA	A	164	−55.712	121.879	−13.280	1.00	57.29	GZ00	C
ATOM	4520	N	LEU	A	165	−53.431	120.361	−14.874	1.00	70.33	GZ00	N
ATOM	4521	CA	LEU	A	165	−52.620	120.265	−16.082	1.00	64.91	GZ00	C
ATOM	4522	C	LEU	A	165	−52.055	118.846	−16.163	1.00	69.76	GZ00	C
ATOM	4523	O	LEU	A	165	−51.263	118.438	−15.303	1.00	66.93	GZ00	O
ATOM	4524	CB	LEU	A	165	−51.521	121.324	−16.062	1.00	64.77	GZ00	C
ATOM	4525	CG	LEU	A	165	−50.556	121.397	−17.245	1.00	68.60	GZ00	C
ATOM	4526	CD1	LEU	A	165	−51.313	121.483	−18.560	1.00	68.89	GZ00	C
ATOM	4527	CD2	LEU	A	165	−49.654	122.612	−17.083	1.00	68.22	GZ00	C
ATOM	4528	N	THR	A	166	−52.506	118.076	−17.164	1.00	75.54	GZ00	N
ATOM	4529	CA	THR	A	166	−52.042	116.700	−17.363	1.00	72.10	GZ00	C
ATOM	4530	C	THR	A	166	−51.554	116.504	−18.792	1.00	68.22	GZ00	C
ATOM	4531	O	THR	A	166	−50.624	115.732	−19.042	1.00	71.78	GZ00	O
ATOM	4532	CB	THR	A	166	−53.133	115.662	−17.055	1.00	67.33	GZ00	C
ATOM	4533	OG1	THR	A	166	−54.242	115.850	−17.938	1.00	72.47	GZ00	O
ATOM	4534	CG2	THR	A	166	−53.609	115.751	−15.608	1.00	70.69	GZ00	C
ATOM	4535	N	SER	A	167	−52.193	117.175	−19.742	1.00	70.73	GZ00	N
ATOM	4536	CA	SER	A	167	−51.742	117.096	−21.121	1.00	77.77	GZ00	C
ATOM	4537	C	SER	A	167	−50.357	117.710	−21.242	1.00	66.92	GZ00	C
ATOM	4538	O	SER	A	167	−50.104	118.796	−20.717	1.00	69.96	GZ00	O
ATOM	4539	CB	SER	A	167	−52.734	117.819	−22.039	1.00	74.39	GZ00	C
ATOM	4540	OG	SER	A	167	−52.114	118.270	−23.233	1.00	68.17	GZ00	O
ATOM	4541	N	GLY	A	168	−49.455	117.012	−21.932	1.00	64.19	GZ00	N
ATOM	4542	CA	GLY	A	168	−48.125	117.554	−22.141	1.00	62.50	GZ00	C
ATOM	4543	C	GLY	A	168	−47.169	117.414	−20.977	1.00	58.51	GZ00	C
ATOM	4544	O	GLY	A	168	−46.115	118.053	−20.994	1.00	54.75	GZ00	O
ATOM	4545	N	VAL	A	169	−47.512	116.619	−19.963	1.00	59.87	GZ00	N
ATOM	4546	CA	VAL	A	169	−46.709	116.442	−18.757	1.00	53.22	GZ00	C
ATOM	4547	C	VAL	A	169	−45.837	115.206	−18.906	1.00	57.24	GZ00	C
ATOM	4548	O	VAL	A	169	−46.341	114.121	−19.219	1.00	54.95	GZ00	O
ATOM	4549	CB	VAL	A	169	−47.605	116.322	−17.514	1.00	52.90	GZ00	C
ATOM	4550	CG1	VAL	A	169	−46.789	115.872	−16.311	1.00	50.21	GZ00	C
ATOM	4551	CG2	VAL	A	169	−48.279	117.657	−17.237	1.00	56.97	GZ00	C
ATOM	4552	N	HIS	A	170	−44.533	115.362	−18.656	1.00	49.30	GZ00	N
ATOM	4553	CA	HIS	A	170	−43.571	114.263	−18.742	1.00	46.23	GZ00	C
ATOM	4554	C	HIS	A	170	−42.653	114.312	−17.519	1.00	45.18	GZ00	C
ATOM	4555	O	HIS	A	170	−41.702	115.095	−17.482	1.00	48.42	GZ00	O
ATOM	4556	CB	HIS	A	170	−42.786	114.360	−20.050	1.00	46.88	GZ00	C
ATOM	4557	CG	HIS	A	170	−41.995	113.136	−20.400	1.00	50.83	GZ00	C
ATOM	4558	ND1	HIS	A	170	−41.756	112.109	−19.507	1.00	51.60	GZ00	N
ATOM	4559	CD2	HIS	A	170	−41.374	112.784	−21.551	1.00	45.43	GZ00	C
ATOM	4560	CE1	HIS	A	170	−41.020	111.180	−20.092	1.00	44.58	GZ00	C
ATOM	4561	NE2	HIS	A	170	−40.776	111.565	−21.332	1.00	49.60	GZ00	N
ATOM	4562	N	THR	A	171	−42.927	113.466	−16.529	1.00	43.26	GZ00	N
ATOM	4563	CA	THR	A	171	−42.052	113.277	−15.380	1.00	42.92	GZ00	C
ATOM	4564	C	THR	A	171	−41.082	112.128	−15.662	1.00	43.51	GZ00	C
ATOM	4565	O	THR	A	171	−41.505	111.018	−15.974	1.00	42.46	GZ00	O
ATOM	4566	CB	THR	A	171	−42.883	113.022	−14.124	1.00	37.89	GZ00	C
ATOM	4567	OG1	THR	A	171	−43.681	114.176	−13.878	1.00	47.19	GZ00	O
ATOM	4568	CG2	THR	A	171	−42.006	112.776	−12.906	1.00	32.66	GZ00	C
ATOM	4569	N	PHE	A	172	−39.793	112.421	−15.634	1.00	46.02	GZ00	N
ATOM	4570	CA	PHE	A	172	−38.722	111.494	−15.965	1.00	45.07	GZ00	C
ATOM	4571	C	PHE	A	172	−38.336	110.651	−14.754	1.00	49.93	GZ00	C
ATOM	4572	O	PHE	A	172	−38.364	111.141	−13.628	1.00	51.84	GZ00	O
ATOM	4573	CB	PHE	A	172	−37.501	112.256	−16.475	1.00	38.72	GZ00	C
ATOM	4574	CG	PHE	A	172	−37.680	112.793	−17.855	1.00	43.18	GZ00	C
ATOM	4575	CD1	PHE	A	172	−38.599	113.810	−18.104	1.00	42.98	GZ00	C
ATOM	4576	CD2	PHE	A	172	−36.942	112.277	−18.917	1.00	40.18	GZ00	C
ATOM	4577	CE1	PHE	A	172	−38.782	114.304	−19.389	1.00	43.59	GZ00	C
ATOM	4578	CE2	PHE	A	172	−37.108	112.779	−20.216	1.00	44.39	GZ00	C
ATOM	4579	CZ	PHE	A	172	−38.030	113.797	−20.449	1.00	45.10	GZ00	C
ATOM	4580	N	PRO	A	173	−37.971	109.388	−14.970	1.00	45.23	GZ00	N
ATOM	4581	CA	PRO	A	173	−37.427	108.573	−13.877	1.00	46.41	GZ00	C
ATOM	4582	C	PRO	A	173	−36.181	109.215	−13.275	1.00	46.24	GZ00	C
ATOM	4583	O	PRO	A	173	−35.412	109.890	−13.963	1.00	49.60	GZ00	O
ATOM	4584	CB	PRO	A	173	−37.083	107.243	−14.568	1.00	43.84	GZ00	C
ATOM	4585	CG	PRO	A	173	−37.966	107.212	−15.777	1.00	42.54	GZ00	C
ATOM	4586	CD	PRO	A	173	−38.103	108.633	−16.230	1.00	42.67	GZ00	C
ATOM	4587	N	ALA	A	174	−35.971	108.971	−11.983	1.00	43.82	GZ00	N
ATOM	4588	CA	ALA	A	174	−34.906	109.615	−11.225	1.00	43.70	GZ00	C
ATOM	4589	C	ALA	A	174	−33.520	109.033	−11.547	1.00	43.64	GZ00	C
ATOM	4590	O	ALA	A	174	−33.392	107.905	−12.020	1.00	48.77	GZ00	O
ATOM	4591	CB	ALA	A	174	−35.195	109.486	−9.733	1.00	46.19	GZ00	C
ATOM	4592	N	VAL	A	175	−32.460	109.857	−11.304	1.00	40.72	GZ00	N
ATOM	4593	CA	VAL	A	175	−31.066	109.414	−11.216	1.00	40.07	GZ00	C
ATOM	4594	C	VAL	A	175	−30.766	109.037	−9.779	1.00	49.10	GZ00	C
ATOM	4595	O	VAL	A	175	−31.260	109.680	−8.847	1.00	49.26	GZ00	O
ATOM	4596	CB	VAL	A	175	−30.053	110.495	−11.665	1.00	47.05	GZ00	C
ATOM	4597	CG1	VAL	A	175	−29.752	110.424	−13.122	1.00	49.41	GZ00	C
ATOM	4598	CG2	VAL	A	175	−30.479	111.906	−11.241	1.00	43.16	GZ00	C
ATOM	4599	N	LEU	A	176	−29.930	108.011	−9.593	1.00	45.95	GZ00	N
ATOM	4600	CA	LEU	A	176	−29.317	107.724	−8.305	1.00	45.89	GZ00	C
ATOM	4601	C	LEU	A	176	−27.916	108.315	−8.322	1.00	50.82	GZ00	C
ATOM	4602	O	LEU	A	176	−27.048	107.853	−9.066	1.00	64.34	GZ00	O
ATOM	4603	CB	LEU	A	176	−29.278	106.231	−8.012	1.00	50.15	GZ00	C
ATOM	4604	CG	LEU	A	176	−28.524	105.913	−6.714	1.00	55.35	GZ00	C
ATOM	4605	CD1	LEU	A	176	−29.054	106.726	−5.525	1.00	46.25	GZ00	C
ATOM	4606	CD2	LEU	A	176	−28.546	104.409	−6.408	1.00	46.32	GZ00	C
ATOM	4607	N	GLN	A	177	−27.691	109.322	−7.492	1.00	52.50	GZ00	N
ATOM	4608	CA	GLN	A	177	−26.422	110.026	−7.518	1.00	63.27	GZ00	C
ATOM	4609	C	GLN	A	177	−25.368	109.285	−6.697	1.00	56.88	GZ00	C
ATOM	4610	O	GLN	A	177	−25.678	108.456	−5.831	1.00	51.21	GZ00	O
ATOM	4611	CB	GLN	A	177	−26.600	111.448	−6.985	1.00	64.89	GZ00	C
ATOM	4612	CG	GLN	A	177	−27.646	112.247	−7.732	1.00	67.73	GZ00	C
ATOM	4613	CD	GLN	A	177	−27.955	113.563	−7.061	1.00	68.75	GZ00	C
ATOM	4614	OE1	GLN	A	177	−27.236	114.552	−7.240	1.00	87.07	GZ00	O
ATOM	4615	NE2	GLN	A	177	−29.018	113.581	−6.259	1.00	58.03	GZ00	N
ATOM	4616	N	SER	A	178	−24.100	109.596	−6.997	1.00	53.78	GZ00	N
ATOM	4617	CA	SER	A	178	−22.982	109.070	−6.216	1.00	54.16	GZ00	C
ATOM	4618	C	SER	A	178	−23.113	109.421	−4.744	1.00	58.69	GZ00	C
ATOM	4619	O	SER	A	178	−22.550	108.730	−3.889	1.00	66.24	GZ00	O
ATOM	4620	CB	SER	A	178	−21.648	109.588	−6.769	1.00	54.96	GZ00	C
ATOM	4621	OG	SER	A	178	−21.589	111.004	−6.780	1.00	68.48	GZ00	O
ATOM	4622	N	SER	A	179	−23.821	110.508	−4.432	1.00	59.99	GZ00	N
ATOM	4623	CA	SER	A	179	−24.134	110.871	−3.058	1.00	57.94	GZ00	C
ATOM	4624	C	SER	A	179	−25.059	109.870	−2.372	1.00	50.10	GZ00	C
ATOM	4625	O	SER	A	179	−25.232	109.952	−1.154	1.00	50.29	GZ00	O
ATOM	4626	CB	SER	A	179	−24.787	112.254	−3.030	1.00	52.99	GZ00	C
ATOM	4627	OG	SER	A	179	−26.135	112.159	−3.478	1.00	61.58	GZ00	O
ATOM	4628	N	GLY	A	180	−25.671	108.949	−3.113	1.00	43.93	GZ00	N
ATOM	4629	CA	GLY	A	180	−26.698	108.079	−2.571	1.00	44.88	GZ00	C
ATOM	4630	C	GLY	A	180	−28.110	108.631	−2.606	1.00	52.65	GZ00	C
ATOM	4631	O	GLY	A	180	−29.037	107.923	−2.196	1.00	57.69	GZ00	O
ATOM	4632	N	LEU	A	181	−28.306	109.863	−3.094	1.00	54.40	GZ00	N
ATOM	4633	CA	LEU	A	181	−29.609	110.513	−3.171	1.00	55.39	GZ00	C
ATOM	4634	C	LEU	A	181	−30.141	110.518	−4.600	1.00	52.55	GZ00	C
ATOM	4635	O	LEU	A	181	−29.377	110.492	−5.571	1.00	47.86	GZ00	O
ATOM	4636	CB	LEU	A	181	−29.523	111.954	−2.660	1.00	50.22	GZ00	C
ATOM	4637	CG	LEU	A	181	−29.108	112.109	−1.207	1.00	54.13	GZ00	C
ATOM	4638	CD1	LEU	A	181	−28.919	113.590	−0.837	1.00	45.91	GZ00	C
ATOM	4639	CD2	LEU	A	181	−30.175	111.435	−0.357	1.00	50.94	GZ00	C
ATOM	4640	N	TYR	A	182	−31.469	110.607	−4.712	1.00	45.18	GZ00	N
ATOM	4641	CA	TYR	A	182	−32.159	110.643	−5.991	1.00	44.17	GZ00	C
ATOM	4642	C	TYR	A	182	−32.489	112.069	−6.403	1.00	48.41	GZ00	C
ATOM	4643	O	TYR	A	182	−32.683	112.946	−5.562	1.00	50.13	GZ00	O
ATOM	4644	CB	TYR	A	182	−33.454	109.832	−5.939	1.00	51.31	GZ00	C
ATOM	4645	CG	TYR	A	182	−33.222	108.357	−5.719	1.00	51.52	GZ00	C
ATOM	4646	CD1	TYR	A	182	−32.971	107.499	−6.796	1.00	53.09	GZ00	C
ATOM	4647	CD2	TYR	A	182	−33.255	107.817	−4.441	1.00	49.04	GZ00	C
ATOM	4648	CE1	TYR	A	182	−32.746	106.144	−6.595	1.00	57.42	GZ00	C
ATOM	4649	CE2	TYR	A	182	−33.037	106.464	−4.231	1.00	58.73	GZ00	C
ATOM	4650	CZ	TYR	A	182	−32.784	105.634	−5.305	1.00	56.88	GZ00	C
ATOM	4651	OH	TYR	A	182	−32.567	104.299	−5.082	1.00	64.47	GZ00	O
ATOM	4652	N	SER	A	183	−32.565	112.285	−7.718	1.00	46.87	GZ00	N
ATOM	4653	CA	SER	A	183	−33.102	113.509	−8.298	1.00	44.44	GZ00	C
ATOM	4654	C	SER	A	183	−33.911	113.162	−9.541	1.00	46.59	GZ00	C
ATOM	4655	O	SER	A	183	−33.582	112.222	−10.262	1.00	44.22	GZ00	O
ATOM	4656	CB	SER	A	183	−31.992	114.502	−8.679	1.00	39.93	GZ00	C
ATOM	4657	OG	SER	A	183	−31.284	114.978	−7.545	1.00	50.25	GZ00	O
ATOM	4658	N	LEU	A	184	−34.945	113.951	−9.821	1.00	43.36	GZ00	N
ATOM	4659	CA	LEU	A	184	−35.653	113.810	−11.084	1.00	43.02	GZ00	C
ATOM	4660	C	LEU	A	184	−36.113	115.182	−11.552	1.00	47.62	GZ00	C
ATOM	4661	O	LEU	A	184	−36.058	116.171	−10.815	1.00	47.17	GZ00	O
ATOM	4662	CB	LEU	A	184	−36.840	112.839	−10.975	1.00	38.26	GZ00	C
ATOM	4663	CG	LEU	A	184	−38.061	113.103	−10.085	1.00	43.98	GZ00	C
ATOM	4664	CD1	LEU	A	184	−38.998	114.216	−10.603	1.00	40.01	GZ00	C
ATOM	4665	CD2	LEU	A	184	−38.840	111.795	−9.902	1.00	43.99	GZ00	C
ATOM	4666	N	SER	A	185	−36.568	115.229	−12.801	1.00	43.75	GZ00	N
ATOM	4667	CA	SER	A	185	−37.198	116.411	−13.358	1.00	38.83	GZ00	C
ATOM	4668	C	SER	A	185	−38.565	116.044	−13.909	1.00	43.09	GZ00	C
ATOM	4669	O	SER	A	185	−38.803	114.901	−14.312	1.00	45.04	GZ00	O
ATOM	4670	CB	SER	A	185	−36.346	117.037	−14.462	1.00	38.03	GZ00	C
ATOM	4671	OG	SER	A	185	−35.075	117.365	−13.952	1.00	38.25	GZ00	O
ATOM	4672	N	SER	A	186	−39.468	117.023	−13.889	1.00	39.49	GZ00	N
ATOM	4673	CA	SER	A	186	−40.767	116.950	−14.544	1.00	41.04	GZ00	C
ATOM	4674	C	SER	A	186	−40.899	118.159	−15.449	1.00	42.89	GZ00	C
ATOM	4675	O	SER	A	186	−40.584	119.272	−15.032	1.00	44.02	GZ00	O
ATOM	4676	CB	SER	A	186	−41.917	116.931	−13.536	1.00	44.24	GZ00	C
ATOM	4677	OG	SER	A	186	−43.174	117.016	−14.199	1.00	48.30	GZ00	O
ATOM	4678	N	VAL	A	187	−41.298	117.945	−16.698	1.00	47.04	GZ00	N
ATOM	4679	CA	VAL	A	187	−41.489	119.062	−17.613	1.00	45.11	GZ00	C
ATOM	4680	C	VAL	A	187	−42.849	118.971	−18.275	1.00	51.54	GZ00	C
ATOM	4681	O	VAL	A	187	−43.401	117.887	−18.494	1.00	53.22	GZ00	O
ATOM	4682	CB	VAL	A	187	−40.385	119.152	−18.666	1.00	43.95	GZ00	C
ATOM	4683	CG1	VAL	A	187	−39.102	119.540	−17.976	1.00	54.28	GZ00	C
ATOM	4684	CG2	VAL	A	187	−40.236	117.828	−19.352	1.00	52.33	GZ00	C
ATOM	4685	N	VAL	A	188	−43.405	120.132	−18.564	1.00	54.43	GZ00	N
ATOM	4686	CA	VAL	A	188	−44.641	120.228	−19.315	1.00	58.17	GZ00	C
ATOM	4687	C	VAL	A	188	−44.385	121.161	−20.480	1.00	59.55	GZ00	C
ATOM	4688	O	VAL	A	188	−43.710	122.188	−20.330	1.00	58.11	GZ00	O
ATOM	4689	CB	VAL	A	188	−45.821	120.710	−18.443	1.00	59.93	GZ00	C
ATOM	4690	CG1	VAL	A	188	−45.449	121.979	−17.680	1.00	60.26	GZ00	C
ATOM	4691	CG2	VAL	A	188	−47.062	120.912	−19.297	1.00	61.12	GZ00	C
ATOM	4692	N	THR	A	189	−44.859	120.768	−21.655	1.00	62.33	GZ00	N
ATOM	4693	CA	THR	A	189	−44.814	121.638	−22.815	1.00	66.67	GZ00	C
ATOM	4694	C	THR	A	189	−46.153	122.362	−22.930	1.00	69.89	GZ00	C
ATOM	4695	O	THR	A	189	−47.220	121.739	−22.815	1.00	62.33	GZ00	O
ATOM	4696	CB	THR	A	189	−44.477	120.837	−24.072	1.00	67.75	GZ00	C
ATOM	4697	OG1	THR	A	189	−44.384	119.450	−23.731	1.00	69.60	GZ00	O
ATOM	4698	CG2	THR	A	189	−43.130	121.278	−24.620	1.00	74.71	GZ00	C
ATOM	4699	N	VAL	A	190	−46.084	123.681	−23.102	1.00	66.60	GZ00	N
ATOM	4700	CA	VAL	A	190	−47.263	124.547	−23.133	1.00	66.10	GZ00	C
ATOM	4701	C	VAL	A	190	−47.136	125.490	−24.322	1.00	73.09	GZ00	C
ATOM	4702	O	VAL	A	190	−46.045	125.641	−24.901	1.00	71.87	GZ00	O
ATOM	4703	CB	VAL	A	190	−47.425	125.349	−21.818	1.00	64.66	GZ00	C
ATOM	4704	CG1	VAL	A	190	−47.569	124.428	−20.610	1.00	58.32	GZ00	C
ATOM	4705	CG2	VAL	A	190	−46.261	126.316	−21.640	1.00	59.75	GZ00	C
ATOM	4706	N	PRO	A	191	−48.245	126.108	−24.739	1.00	74.14	GZ00	N
ATOM	4707	CA	PRO	A	191	−48.160	127.158	−25.763	1.00	74.58	GZ00	C
ATOM	4708	C	PRO	A	191	−47.354	128.344	−25.261	1.00	76.75	GZ00	C
ATOM	4709	O	PRO	A	191	−47.577	128.839	−24.154	1.00	81.03	GZ00	O
ATOM	4710	CB	PRO	A	191	−49.625	127.539	−26.000	1.00	69.86	GZ00	C
ATOM	4711	CG	PRO	A	191	−50.402	126.339	−25.563	1.00	73.10	GZ00	C
ATOM	4712	CD	PRO	A	191	−49.645	125.802	−24.391	1.00	71.77	GZ00	C
ATOM	4713	N	SER	A	192	−46.422	128.813	−26.093	1.00	74.74	GZ00	N
ATOM	4714	CA	SER	A	192	−45.569	129.925	−25.684	1.00	84.32	GZ00	C
ATOM	4715	C	SER	A	192	−46.375	131.203	−25.449	1.00	87.52	GZ00	C
ATOM	4716	O	SER	A	192	−46.000	132.033	−24.611	1.00	90.45	GZ00	O
ATOM	4717	CB	SER	A	192	−44.469	130.145	−26.720	1.00	82.62	GZ00	C
ATOM	4718	OG	SER	A	192	−45.022	130.471	−27.977	1.00	97.04	GZ00	O
ATOM	4719	N	SER	A	193	−47.472	131.392	−26.187	1.00	89.79	GZ00	N
ATOM	4720	CA	SER	A	193	−48.307	132.573	−25.998	1.00	89.74	GZ00	C
ATOM	4721	C	SER	A	193	−48.972	132.612	−24.626	1.00	93.59	GZ00	C
ATOM	4722	O	SER	A	193	−49.320	133.699	−24.148	1.00	95.20	GZ00	O
ATOM	4723	CB	SER	A	193	−49.389	132.613	−27.076	1.00	81.94	GZ00	C
ATOM	4724	OG	SER	A	193	−50.265	131.503	−26.929	1.00	74.81	GZ00	O
ATOM	4725	N	SER	A	194	−49.138	131.462	−23.975	1.00	87.57	GZ00	N
ATOM	4726	CA	SER	A	194	−49.771	131.416	−22.662	1.00	89.09	GZ00	C
ATOM	4727	C	SER	A	194	−48.823	131.758	−21.516	1.00	91.10	GZ00	C
ATOM	4728	O	SER	A	194	−49.278	131.840	−20.368	1.00	89.32	GZ00	O
ATOM	4729	CB	SER	A	194	−50.372	130.030	−22.418	1.00	81.55	GZ00	C
ATOM	4730	OG	SER	A	194	−49.347	129.061	−22.241	1.00	88.02	GZ00	O
ATOM	4731	N	LEU	A	195	−47.528	131.951	−21.791	1.00	87.53	GZ00	N
ATOM	4732	CA	LEU	A	195	−46.560	132.107	−20.708	1.00	88.74	GZ00	C
ATOM	4733	C	LEU	A	195	−46.827	133.359	−19.882	1.00	89.05	GZ00	C
ATOM	4734	O	LEU	A	195	−46.677	133.340	−18.654	1.00	89.42	GZ00	O
ATOM	4735	CB	LEU	A	195	−45.137	132.120	−21.267	1.00	85.76	GZ00	C
ATOM	4736	CG	LEU	A	195	−44.685	130.772	−21.838	1.00	84.17	GZ00	C
ATOM	4737	CD1	LEU	A	195	−43.245	130.846	−22.337	1.00	78.51	GZ00	C
ATOM	4738	CD2	LEU	A	195	−44.872	129.643	−20.827	1.00	71.43	GZ00	C
ATOM	4739	N	GLY	A	196	−47.240	134.451	−20.529	1.00	92.67	GZ00	N
ATOM	4740	CA	GLY	A	196	−47.552	135.661	−19.789	1.00	83.87	GZ00	C
ATOM	4741	C	GLY	A	196	−48.867	135.611	−19.045	1.00	82.81	GZ00	C
ATOM	4742	O	GLY	A	196	−49.054	136.368	−18.090	1.00	84.91	GZ00	O
ATOM	4743	N	THR	A	197	−49.775	134.728	−19.455	1.00	85.57	GZ00	N
ATOM	4744	CA	THR	A	197	−51.143	134.692	−18.952	1.00	86.43	GZ00	C
ATOM	4745	C	THR	A	197	−51.368	133.631	−17.888	1.00	86.30	GZ00	C
ATOM	4746	O	THR	A	197	−52.058	133.892	−16.898	1.00	86.17	GZ00	O
ATOM	4747	CB	THR	A	197	−52.121	134.417	−20.097	1.00	86.40	GZ00	C
ATOM	4748	OG1	THR	A	197	−51.849	135.303	−21.187	1.00	91.08	GZ00	O
ATOM	4749	CG2	THR	A	197	−53.569	134.569	−19.626	1.00	80.19	GZ00	C
ATOM	4750	N	GLN	A	198	−50.770	132.454	−18.048	1.00	84.30	GZ00	N
ATOM	4751	CA	GLN	A	198	−51.154	131.288	−17.272	1.00	78.44	GZ00	C
ATOM	4752	C	GLN	A	198	−50.118	131.004	−16.194	1.00	79.40	GZ00	C
ATOM	4753	O	GLN	A	198	−48.910	131.155	−16.412	1.00	78.37	GZ00	O
ATOM	4754	CB	GLN	A	198	−51.315	130.071	−18.184	1.00	76.20	GZ00	C
ATOM	4755	CG	GLN	A	198	−51.543	128.762	−17.443	1.00	79.56	GZ00	C
ATOM	4756	CD	GLN	A	198	−52.867	128.724	−16.710	1.00	81.18	GZ00	C
ATOM	4757	OE1	GLN	A	198	−53.881	129.172	−17.236	1.00	93.21	GZ00	O
ATOM	4758	NE2	GLN	A	198	−52.867	128.185	−15.493	1.00	73.89	GZ00	N
ATOM	4759	N	THR	A	199	−50.606	130.551	−15.043	1.00	73.01	GZ00	N
ATOM	4760	CA	THR	A	199	−49.774	130.248	−13.891	1.00	76.95	GZ00	C
ATOM	4761	C	THR	A	199	−49.518	128.747	−13.834	1.00	74.20	GZ00	C
ATOM	4762	O	THR	A	199	−50.462	127.944	−13.805	1.00	70.39	GZ00	O
ATOM	4763	CB	THR	A	199	−50.445	130.746	−12.610	1.00	71.33	GZ00	C
ATOM	4764	OG1	THR	A	199	−50.421	132.179	−12.601	1.00	73.00	GZ00	O
ATOM	4765	CG2	THR	A	199	−49.728	130.224	−11.382	1.00	65.14	GZ00	C
ATOM	4766	N	TYR	A	200	−48.242	128.376	−13.805	1.00	68.08	GZ00	N
ATOM	4767	CA	TYR	A	200	−47.829	126.982	−13.781	1.00	61.58	GZ00	C
ATOM	4768	C	TYR	A	200	−47.135	126.697	−12.461	1.00	60.20	GZ00	C
ATOM	4769	O	TYR	A	200	−46.093	127.293	−12.153	1.00	57.85	GZ00	O
ATOM	4770	CB	TYR	A	200	−46.911	126.674	−14.955	1.00	57.54	GZ00	C
ATOM	4771	CG	TYR	A	200	−47.580	126.881	−16.287	1.00	62.50	GZ00	C
ATOM	4772	CD1	TYR	A	200	−48.564	126.013	−16.731	1.00	61.12	GZ00	C
ATOM	4773	CD2	TYR	A	200	−47.218	127.943	−17.106	1.00	67.26	GZ00	C
ATOM	4774	CE1	TYR	A	200	−49.178	126.194	−17.951	1.00	65.39	GZ00	C
ATOM	4775	CE2	TYR	A	200	−47.820	128.135	−18.333	1.00	69.26	GZ00	C
ATOM	4776	CZ	TYR	A	200	−48.802	127.257	−18.753	1.00	70.05	GZ00	C
ATOM	4777	OH	TYR	A	200	−49.409	127.447	−19.979	1.00	69.68	GZ00	O
ATOM	4778	N	ILE	A	201	−47.710	125.775	−11.699	1.00	54.42	GZ00	N
ATOM	4779	CA	ILE	A	201	−47.224	125.396	−10.384	1.00	55.01	GZ00	C
ATOM	4780	C	ILE	A	201	−47.026	123.891	−10.383	1.00	53.67	GZ00	C
ATOM	4781	O	ILE	A	201	−47.944	123.147	−10.738	1.00	51.99	GZ00	O
ATOM	4782	CB	ILE	A	201	−48.220	125.791	−9.275	1.00	53.52	GZ00	C
ATOM	4783	CG1	ILE	A	201	−48.406	127.304	−9.225	1.00	59.92	GZ00	C
ATOM	4784	CG2	ILE	A	201	−47.757	125.257	−7.920	1.00	51.50	GZ00	C
ATOM	4785	CD1	ILE	A	201	−49.568	127.719	−8.359	1.00	59.25	GZ00	C
ATOM	4786	N	CYS	A	202	−45.846	123.434	−9.979	1.00	49.43	GZ00	N
ATOM	4787	CA	CYS	A	202	−45.655	122.005	−9.794	1.00	52.57	GZ00	C
ATOM	4788	C	CYS	A	202	−45.814	121.642	−8.324	1.00	50.37	GZ00	C
ATOM	4789	O	CYS	A	202	−45.364	122.364	−7.433	1.00	52.12	GZ00	O
ATOM	4790	CB	CYS	A	202	−44.301	121.549	−10.331	1.00	62.40	GZ00	C
ATOM	4791	SG	CYS	A	202	−42.952	121.799	−9.238	1.00	64.20	GZ00	S
ATOM	4792	N	ASN	A	203	−46.465	120.516	−8.082	1.00	47.36	GZ00	N
ATOM	4793	CA	ASN	A	203	−46.831	120.068	−6.747	1.00	46.99	GZ00	C
ATOM	4794	C	ASN	A	203	−46.058	118.791	−6.497	1.00	48.88	GZ00	C
ATOM	4795	O	ASN	A	203	−46.287	117.778	−7.163	1.00	57.36	GZ00	O
ATOM	4796	CB	ASN	A	203	−48.342	119.850	−6.635	1.00	48.02	GZ00	C
ATOM	4797	CG	ASN	A	203	−49.137	120.936	−7.344	1.00	55.33	GZ00	C
ATOM	4798	OD1	ASN	A	203	−49.750	120.696	−8.385	1.00	60.59	GZ00	O
ATOM	4799	ND2	ASN	A	203	−49.148	122.139	−6.765	1.00	49.46	GZ00	N
ATOM	4800	N	VAL	A	204	−45.120	118.858	−5.568	1.00	44.47	GZ00	N
ATOM	4801	CA	VAL	A	204	−44.215	117.764	−5.274	1.00	47.87	GZ00	C
ATOM	4802	C	VAL	A	204	−44.619	117.151	−3.949	1.00	46.74	GZ00	C
ATOM	4803	O	VAL	A	204	−44.770	117.864	−2.952	1.00	50.77	GZ00	O
ATOM	4804	CB	VAL	A	204	−42.755	118.248	−5.231	1.00	44.63	GZ00	C
ATOM	4805	CG1	VAL	A	204	−41.843	117.090	−4.887	1.00	38.03	GZ00	C
ATOM	4806	CG2	VAL	A	204	−42.380	118.903	−6.567	1.00	40.53	GZ00	C
ATOM	4807	N	ASN	A	205	−44.767	115.832	−3.928	1.00	48.79	GZ00	N
ATOM	4808	CA	ASN	A	205	−45.133	115.123	−2.714	1.00	47.93	GZ00	C
ATOM	4809	C	ASN	A	205	−44.153	113.974	−2.534	1.00	49.20	GZ00	C
ATOM	4810	O	ASN	A	205	−43.964	113.166	−3.445	1.00	60.40	GZ00	O
ATOM	4811	CB	ASN	A	205	−46.588	114.648	−2.781	1.00	53.37	GZ00	C
ATOM	4812	CG	ASN	A	205	−47.095	114.117	−1.449	1.00	66.37	GZ00	C
ATOM	4813	OD1	ASN	A	205	−46.479	114.336	−0.404	1.00	69.20	GZ00	O
ATOM	4814	ND2	ASN	A	205	−48.254	113.468	−1.473	1.00	77.20	GZ00	N
ATOM	4815	N	HIS	A	206	−43.476	113.954	−1.396	1.00	45.52	GZ00	N
ATOM	4816	CA	HIS	A	206	−42.524	112.919	−1.028	1.00	43.97	GZ00	C
ATOM	4817	C	HIS	A	206	−42.971	112.323	0.309	1.00	53.01	GZ00	C
ATOM	4818	O	HIS	A	206	−42.520	112.750	1.378	1.00	53.77	GZ00	O
ATOM	4819	CB	HIS	A	206	−41.137	113.478	−0.951	1.00	40.28	GZ00	C
ATOM	4820	CG	HIS	A	206	−40.104	112.463	−0.585	1.00	48.58	GZ00	C
ATOM	4821	ND1	HIS	A	206	−39.422	112.498	0.611	1.00	53.96	GZ00	N
ATOM	4822	CD2	HIS	A	206	−39.646	111.374	−1.247	1.00	48.75	GZ00	C
ATOM	4823	CE1	HIS	A	206	−38.579	111.482	0.667	1.00	51.43	GZ00	C
ATOM	4824	NE2	HIS	A	206	−38.689	110.790	−0.453	1.00	52.90	GZ00	N
ATOM	4825	N	LYS	A	207	−43.829	111.306	0.233	1.00	54.92	GZ00	N
ATOM	4826	CA	LYS	A	207	−44.424	110.729	1.434	1.00	48.15	GZ00	C
ATOM	4827	C	LYS	A	207	−43.418	110.140	2.423	1.00	52.26	GZ00	C
ATOM	4828	O	LYS	A	207	−43.648	110.282	3.635	1.00	59.42	GZ00	O
ATOM	4829	CB	LYS	A	207	−45.481	109.710	1.007	1.00	49.63	GZ00	C
ATOM	4830	CG	LYS	A	207	−46.665	110.413	0.313	1.00	60.89	GZ00	C
ATOM	4831	CD	LYS	A	207	−47.752	109.458	−0.167	1.00	75.35	GZ00	C
ATOM	4832	CE	LYS	A	207	−48.892	110.226	−0.848	1.00	81.98	GZ00	C
ATOM	4833	NZ	LYS	A	207	−49.961	109.352	−1.445	1.00	90.80	GZ00	N1+
ATOM	4834	N	PRO	A	208	−42.313	109.506	2.016	1.00	53.20	GZ00	N
ATOM	4835	CA	PRO	A	208	−41.376	108.969	3.026	1.00	54.32	GZ00	C
ATOM	4836	C	PRO	A	208	−40.864	109.993	4.034	1.00	57.05	GZ00	C
ATOM	4837	O	PRO	A	208	−40.579	109.623	5.178	1.00	57.60	GZ00	O
ATOM	4838	CB	PRO	A	208	−40.231	108.409	2.174	1.00	48.60	GZ00	C
ATOM	4839	CG	PRO	A	208	−40.871	108.022	0.913	1.00	50.40	GZ00	C
ATOM	4840	CD	PRO	A	208	−41.948	109.055	0.660	1.00	50.23	GZ00	C
ATOM	4841	N	SER	A	209	−40.691	111.254	3.636	1.00	61.65	GZ00	N
ATOM	4842	CA	SER	A	209	−40.273	112.325	4.535	1.00	62.97	GZ00	C
ATOM	4843	C	SER	A	209	−41.416	113.260	4.930	1.00	61.87	GZ00	C
ATOM	4844	O	SER	A	209	−41.174	114.251	5.630	1.00	60.78	GZ00	O
ATOM	4845	CB	SER	A	209	−39.165	113.147	3.879	1.00	59.23	GZ00	C
ATOM	4846	OG	SER	A	209	−39.685	113.856	2.755	1.00	55.04	GZ00	O
ATOM	4847	N	ASN	A	210	−42.646	112.940	4.539	1.00	55.47	GZ00	N
ATOM	4848	CA	ASN	A	210	−43.808	113.822	4.651	1.00	56.64	GZ00	C
ATOM	4849	C	ASN	A	210	−43.460	115.261	4.290	1.00	56.98	GZ00	C
ATOM	4850	O	ASN	A	210	−43.558	116.181	5.100	1.00	62.92	GZ00	O
ATOM	4851	CB	ASN	A	210	−44.398	113.761	6.053	1.00	60.66	GZ00	C
ATOM	4852	CG	ASN	A	210	−44.555	112.358	6.550	1.00	60.50	GZ00	C
ATOM	4853	OD1	ASN	A	210	−45.556	111.702	6.273	1.00	64.24	GZ00	O
ATOM	4854	ND2	ASN	A	210	−43.562	111.880	7.288	1.00	60.19	GZ00	N
ATOM	4855	N	THR	A	211	−43.011	115.442	3.057	1.00	54.32	GZ00	N
ATOM	4856	CA	THR	A	211	−42.767	116.765	2.504	1.00	47.32	GZ00	C
ATOM	4857	C	THR	A	211	−43.723	117.022	1.349	1.00	47.89	GZ00	C
ATOM	4858	O	THR	A	211	−43.910	116.159	0.489	1.00	54.45	GZ00	O
ATOM	4859	CB	THR	A	211	−41.317	116.913	2.046	1.00	49.88	GZ00	C
ATOM	4860	OG1	THR	A	211	−40.444	116.645	3.148	1.00	51.07	GZ00	O
ATOM	4861	CG2	THR	A	211	−41.061	118.318	1.560	1.00	42.66	GZ00	C
ATOM	4862	N	LYS	A	212	−44.338	118.194	1.339	1.00	50.89	GZ00	N
ATOM	4863	CA	LYS	A	212	−45.112	118.659	0.198	1.00	47.65	GZ00	C
ATOM	4864	C	LYS	A	212	−44.570	120.029	−0.168	1.00	47.72	GZ00	C
ATOM	4865	O	LYS	A	212	−44.386	120.878	0.712	1.00	52.21	GZ00	O
ATOM	4866	CB	LYS	A	212	−46.611	118.715	0.514	1.00	52.77	GZ00	C
ATOM	4867	CG	LYS	A	212	−47.140	117.383	1.052	1.00	63.53	GZ00	C
ATOM	4868	CD	LYS	A	212	−48.662	117.295	1.167	1.00	63.25	GZ00	C
ATOM	4869	CE	LYS	A	212	−49.049	116.010	1.920	1.00	71.43	GZ00	C
ATOM	4870	NZ	LYS	A	212	−50.290	115.345	1.415	1.00	66.03	GZ00	N1+
ATOM	4871	N	VAL	A	213	−44.223	120.212	−1.437	1.00	41.63	GZ00	N
ATOM	4872	CA	VAL	A	213	−43.729	121.485	−1.935	1.00	44.71	GZ00	C
ATOM	4873	C	VAL	A	213	−44.585	121.894	−3.121	1.00	48.49	GZ00	C
ATOM	4874	O	VAL	A	213	−44.882	121.063	−3.983	1.00	53.14	GZ00	O
ATOM	4875	CB	VAL	A	213	−42.246	121.419	−2.347	1.00	43.73	GZ00	C
ATOM	4876	CG1	VAL	A	213	−41.816	122.764	−2.924	1.00	39.48	GZ00	C
ATOM	4877	CG2	VAL	A	213	−41.362	121.029	−1.165	1.00	37.84	GZ00	C
ATOM	4878	N	ASP	A	214	−45.015	123.156	−3.139	1.00	47.97	GZ00	N
ATOM	4879	CA	ASP	A	214	−45.585	123.795	−4.317	1.00	44.59	GZ00	C
ATOM	4880	C	ASP	A	214	−44.598	124.838	−4.810	1.00	46.54	GZ00	C
ATOM	4881	O	ASP	A	214	−44.025	125.579	−4.009	1.00	54.01	GZ00	O
ATOM	4882	CB	ASP	A	214	−46.929	124.477	−4.017	1.00	51.53	GZ00	C
ATOM	4883	CG	ASP	A	214	−47.982	123.512	−3.513	1.00	63.26	GZ00	C
ATOM	4884	OD2	ASP	A	214	−48.796	123.914	−2.654	1.00	87.44	GZ00	O1−
ATOM	4885	OD1	ASP	A	214	−48.012	122.352	−3.969	1.00	69.85	GZ00	O
ATOM	4886	N	LYS	A	215	−44.377	124.888	−6.119	1.00	44.93	GZ00	N
ATOM	4887	CA	LYS	A	215	−43.442	125.855	−6.679	1.00	46.63	GZ00	C
ATOM	4888	C	LYS	A	215	−43.978	126.399	−7.988	1.00	52.58	GZ00	C
ATOM	4889	O	LYS	A	215	−44.348	125.626	−8.878	1.00	52.15	GZ00	O
ATOM	4890	CB	LYS	A	215	−42.051	125.248	−6.899	1.00	47.58	GZ00	C
ATOM	4891	CG	LYS	A	215	−40.969	125.964	−6.129	1.00	50.19	GZ00	C
ATOM	4892	CD	LYS	A	215	−40.152	126.858	−7.027	1.00	48.08	GZ00	C
ATOM	4893	CE	LYS	A	215	−39.413	127.923	−6.211	1.00	55.88	GZ00	C
ATOM	4894	NZ	LYS	A	215	−38.638	127.415	−5.023	1.00	63.59	GZ00	N1+
ATOM	4895	N	LYS	A	216	−44.024	127.727	−8.093	1.00	50.59	GZ00	N
ATOM	4896	CA	LYS	A	216	−44.437	128.396	−9.312	1.00	51.04	GZ00	C
ATOM	4897	C	LYS	A	216	−43.241	128.550	−10.244	1.00	53.52	GZ00	C
ATOM	4898	O	LYS	A	216	−42.135	128.880	−9.807	1.00	49.36	GZ00	O
ATOM	4899	CB	LYS	A	216	−45.052	129.760	−8.996	1.00	56.62	GZ00	C
ATOM	4900	CG	LYS	A	216	−45.566	130.514	−10.215	1.00	61.12	GZ00	C
ATOM	4901	CD	LYS	A	216	−46.136	131.864	−9.823	1.00	67.36	GZ00	C
ATOM	4902	CE	LYS	A	216	−46.919	132.483	−10.962	1.00	66.87	GZ00	C
ATOM	4903	NZ	LYS	A	216	−47.732	133.632	−10.483	1.00	75.15	GZ00	N1+
ATOM	4904	N	VAL	A	217	−43.462	128.277	−11.526	1.00	51.79	GZ00	N
ATOM	4905	CA	VAL	A	217	−42.414	128.342	−12.536	1.00	53.46	GZ00	C
ATOM	4906	C	VAL	A	217	−42.741	129.494	−13.465	1.00	54.54	GZ00	C
ATOM	4907	O	VAL	A	217	−43.747	129.455	−14.179	1.00	59.89	GZ00	O
ATOM	4908	CB	VAL	A	217	−42.292	127.021	−13.308	1.00	55.15	GZ00	C
ATOM	4909	CG1	VAL	A	217	−41.110	127.076	−14.255	1.00	49.43	GZ00	C
ATOM	4910	CG2	VAL	A	217	−42.184	125.845	−12.330	1.00	40.65	GZ00	C
ATOM	4911	N	GLU	A	218	−41.905	130.525	−13.455	1.00	58.16	GZ00	N
ATOM	4912	CA	GLU	A	218	−42.169	131.714	−14.244	1.00	61.44	GZ00	C
ATOM	4913	C	GLU	A	218	−41.064	131.965	−15.263	1.00	73.28	GZ00	C
ATOM	4914	O	GLU	A	218	−39.904	131.589	−15.043	1.00	69.38	GZ00	O
ATOM	4915	CB	GLU	A	218	−42.312	132.955	−13.350	1.00	65.18	GZ00	C
ATOM	4916	CG	GLU	A	218	−43.436	132.867	−12.323	1.00	71.84	GZ00	C
ATOM	4917	CD	GLU	A	218	−43.518	134.104	−11.427	1.00	80.98	GZ00	C
ATOM	4918	OE1	GLU	A	218	−42.537	134.884	−11.391	1.00	69.24	GZ00	O
ATOM	4919	OE2	GLU	A	218	−44.568	134.295	−10.769	1.00	78.83	GZ00	O1−
ATOM	4920	N	PRO	A	219	−41.401	132.592	−16.400	1.00	72.81	GZ00	N
ATOM	4921	CA	PRO	A	219	−40.374	133.004	−17.371	1.00	73.28	GZ00	C
ATOM	4922	C	PRO	A	219	−39.387	134.017	−16.815	1.00	77.52	GZ00	C
ATOM	4923	O	PRO	A	219	−39.500	134.420	−15.653	1.00	81.78	GZ00	O
ATOM	4924	CB	PRO	A	219	−41.194	133.614	−18.517	1.00	73.25	GZ00	C
ATOM	4925	CG	PRO	A	219	−42.619	133.679	−18.024	1.00	67.58	GZ00	C
ATOM	4926	CD	PRO	A	219	−42.759	132.663	−16.958	1.00	67.19	GZ00	C
ATOM	4927	N	LYS	A	220	−38.405	134.405	−17.627	1.00	81.29	GZ00	N
ATOM	4928	CA	LYS	A	220	−37.376	135.375	−17.234	1.00	82.90	GZ00	C
ATOM	4929	C	LYS	A	220	−36.507	134.815	−16.117	1.00	88.96	GZ00	C
ATOM	4930	O	LYS	A	220	−36.186	133.626	−16.112	1.00	89.60	GZ00	O
ATOM	4931	CB	LYS	A	220	−38.003	136.710	−16.809	1.00	83.44	GZ00	C
ATOM	4932	CG	LYS	A	220	−37.004	137.772	−16.372	1.00	79.50	GZ00	C
ATOM	4933	CD	LYS	A	220	−36.117	138.217	−17.516	1.00	78.87	GZ00	C
ATOM	4934	CE	LYS	A	220	−35.095	139.231	−17.031	1.00	76.44	GZ00	C
ATOM	4935	NZ	LYS	A	220	−34.316	139.811	−18.154	1.00	72.11	GZ00	N1+
TER
ATOM	4936	N	GLN	X	1	−13.182	99.213	−18.301	1.00	76.62		N
ATOM	4937	CA	GLN	X	1	−13.330	98.583	−19.611	1.00	76.63		C
ATOM	4938	C	GLN	X	1	−13.561	97.073	−19.505	1.00	74.72		C
ATOM	4939	O	GLN	X	1	−12.891	96.390	−18.727	1.00	80.15		O
ATOM	4940	CB	GLN	X	1	−12.095	98.863	−20.464	1.00	81.35		C
ATOM	4941	CG	GLN	X	1	−11.908	100.324	−20.759	1.00	87.31		C
ATOM	4942	CD	GLN	X	1	−13.144	100.930	−21.400	1.00	101.98		C
ATOM	4943	OE1	GLN	X	1	−13.815	101.779	−20.806	1.00	102.82		O
ATOM	4944	NE2	GLN	X	1	−13.454	100.491	−22.619	1.00	97.35		N
ATOM	4945	N	SER	X	2	−14.506	96.551	−20.287	1.00	67.44		N
ATOM	4946	CA	SER	X	2	−14.749	95.113	−20.298	1.00	60.09		C
ATOM	4947	C	SER	X	2	−13.572	94.377	−20.927	1.00	57.36		C
ATOM	4948	O	SER	X	2	−12.944	94.860	−21.875	1.00	53.67		O
ATOM	4949	CB	SER	X	2	−16.026	94.785	−21.086	1.00	46.51		C
ATOM	4950	OG	SER	X	2	−17.130	94.586	−20.224	1.00	58.04		O
ATOM	4951	N	VAL	X	3	−13.284	93.183	−20.403	1.00	47.89		N
ATOM	4952	CA	VAL	X	3	−12.146	92.428	−20.923	1.00	46.54		C
ATOM	4953	C	VAL	X	3	−12.475	91.869	−22.301	1.00	47.23		C
ATOM	4954	O	VAL	X	3	−11.622	91.855	−23.201	1.00	45.87		O
ATOM	4955	CB	VAL	X	3	−11.731	91.309	−19.951	1.00	44.31		C
ATOM	4956	CG1	VAL	X	3	−10.685	90.401	−20.593	1.00	34.16		C
ATOM	4957	CG2	VAL	X	3	−11.202	91.895	−18.640	1.00	39.33		C
ATOM	4958	N	LEU	X	4	−13.716	91.408	−22.490	1.00	42.72		N
ATOM	4959	CA	LEU	X	4	−14.234	91.004	−23.790	1.00	40.50		C
ATOM	4960	C	LEU	X	4	−15.023	92.164	−24.377	1.00	38.73		C
ATOM	4961	O	LEU	X	4	−15.756	92.844	−23.656	1.00	38.68		O
ATOM	4962	CB	LEU	X	4	−15.120	89.761	−23.666	1.00	32.58		C
ATOM	4963	CG	LEU	X	4	−14.559	88.652	−22.763	1.00	35.07		C
ATOM	4964	CD1	LEU	X	4	−15.572	87.502	−22.591	1.00	33.11		C
ATOM	4965	CD2	LEU	X	4	−13.193	88.130	−23.260	1.00	26.20		C
ATOM	4966	N	THR	X	5	−14.874	92.394	−25.683	1.00	30.86		N
ATOM	4967	CA	THR	X	5	−15.506	93.541	−26.318	1.00	31.01		C
ATOM	4968	C	THR	X	5	−16.635	93.087	−27.228	1.00	32.92		C
ATOM	4969	O	THR	X	5	−16.412	92.301	−28.156	1.00	34.89		O
ATOM	4970	CB	THR	X	5	−14.488	94.361	−27.114	1.00	35.46		C
ATOM	4971	OG1	THR	X	5	−13.373	94.678	−26.280	1.00	37.79		O
ATOM	4972	CG2	THR	X	5	−15.130	95.668	−27.583	1.00	23.38		C
ATOM	4973	N	GLN	X	6	−17.836	93.608	−26.972	1.00	31.00		N
ATOM	4974	CA	GLN	X	6	−19.060	93.406	−27.730	1.00	33.70		C
ATOM	4975	C	GLN	X	6	−19.549	94.756	−28.224	1.00	33.00		C
ATOM	4976	O	GLN	X	6	−19.399	95.759	−27.519	1.00	30.42		O
ATOM	4977	CB	GLN	X	6	−20.188	92.765	−26.892	1.00	30.43		C
ATOM	4978	CG	GLN	X	6	−19.910	91.392	−26.335	1.00	28.80		C
ATOM	4979	CD	GLN	X	6	−21.049	90.852	−25.456	1.00	32.96		C
ATOM	4980	OE1	GLN	X	6	−20.823	90.407	−24.329	1.00	32.89		O
ATOM	4981	NE2	GLN	X	6	−22.266	90.879	−25.978	1.00	26.46		N
ATOM	4982	N	PRO	X	7	−20.179	94.813	−29.392	1.00	28.38		N
ATOM	4983	CA	PRO	X	7	−20.880	96.043	−29.796	1.00	33.26		C
ATOM	4984	C	PRO	X	7	−21.977	96.356	−28.791	1.00	38.21		C
ATOM	4985	O	PRO	X	7	−22.613	95.435	−28.252	1.00	35.17		O
ATOM	4986	CB	PRO	X	7	−21.461	95.693	−31.181	1.00	33.21		C
ATOM	4987	CG	PRO	X	7	−21.607	94.178	−31.146	1.00	34.98		C
ATOM	4988	CD	PRO	X	7	−20.480	93.673	−30.276	1.00	33.91		C
ATOM	4989	N	PRO	X	8	−22.189	97.632	−28.468	1.00	34.91		N
ATOM	4990	CA	PRO	X	8	−23.156	97.962	−27.407	1.00	29.83		C
ATOM	4991	C	PRO	X	8	−24.604	97.731	−27.792	1.00	37.56		C
ATOM	4992	O	PRO	X	8	−25.412	97.420	−26.908	1.00	36.02		O
ATOM	4993	CB	PRO	X	8	−22.879	99.443	−27.119	1.00	28.75		C
ATOM	4994	CG	PRO	X	8	−22.237	99.952	−28.379	1.00	41.44		C
ATOM	4995	CD	PRO	X	8	−21.416	98.803	−28.911	1.00	31.17		C
ATOM	4996	N	SER	X	9	−24.980	97.891	−29.057	1.00	30.64		N
ATOM	4997	CA	SER	X	9	−26.373	97.657	−29.406	1.00	33.12		C
ATOM	4998	C	SER	X	9	−26.487	97.243	−30.864	1.00	36.96		C
ATOM	4999	O	SER	X	9	−25.582	97.451	−31.685	1.00	34.35		O
ATOM	5000	CB	SER	X	9	−27.257	98.873	−29.146	1.00	35.68		C
ATOM	5001	OG	SER	X	9	−26.883	99.958	−29.965	1.00	42.47		O
ATOM	5002	N	VAL	X	10	−27.628	96.644	−31.164	1.00	33.72		N
ATOM	5003	CA	VAL	X	10	−27.851	95.977	−32.431	1.00	34.33		C
ATOM	5004	C	VAL	X	10	−29.358	95.932	−32.642	1.00	34.97		C
ATOM	5005	O	VAL	X	10	−30.118	95.725	−31.688	1.00	36.04		O
ATOM	5006	CB	VAL	X	10	−27.170	94.585	−32.397	1.00	36.02		C
ATOM	5007	CG1	VAL	X	10	−28.071	93.486	−32.875	1.00	38.30		C
ATOM	5008	CG2	VAL	X	10	−25.823	94.625	−33.148	1.00	34.46		C
ATOM	5009	N	SER	X	11	−29.801	96.196	−33.872	1.00	35.57		N
ATOM	5010	CA	SER	X	11	−31.238	96.220	−34.114	1.00	38.43		C
ATOM	5011	C	SER	X	11	−31.565	95.782	−35.531	1.00	38.48		C
ATOM	5012	O	SER	X	11	−30.839	96.101	−36.473	1.00	39.31		O
ATOM	5013	CB	SER	X	11	−31.841	97.609	−33.833	1.00	38.56		C
ATOM	5014	OG	SER	X	11	−31.368	98.589	−34.727	1.00	43.26		O
ATOM	5015	N	ALA	X	12	−32.670	95.054	−35.669	1.00	37.39		N
ATOM	5016	CA	ALA	X	12	−33.132	94.581	−36.965	1.00	35.97		C
ATOM	5017	C	ALA	X	12	−34.610	94.221	−36.869	1.00	39.63		C
ATOM	5018	O	ALA	X	12	−35.144	93.969	−35.782	1.00	37.40		O
ATOM	5019	CB	ALA	X	12	−32.317	93.374	−37.454	1.00	32.40		C
ATOM	5020	N	ALA	X	13	−35.245	94.137	−38.035	1.00	39.79		N
ATOM	5021	CA	ALA	X	13	−36.664	93.835	−38.153	1.00	40.54		C
ATOM	5022	C	ALA	X	13	−36.949	92.341	−37.964	1.00	39.36		C
ATOM	5023	O	ALA	X	13	−36.060	91.493	−38.120	1.00	38.64		O
ATOM	5024	CB	ALA	X	13	−37.170	94.286	−39.518	1.00	26.30		C
ATOM	5025	N	PRO	X	14	−38.182	91.992	−37.606	1.00	39.35		N
ATOM	5026	CA	PRO	X	14	−38.543	90.572	−37.547	1.00	40.01		C
ATOM	5027	C	PRO	X	14	−38.206	89.887	−38.865	1.00	43.81		C
ATOM	5028	O	PRO	X	14	−38.330	90.469	−39.949	1.00	40.74		O
ATOM	5029	CB	PRO	X	14	−40.050	90.596	−37.287	1.00	28.16		C
ATOM	5030	CG	PRO	X	14	−40.292	91.919	−36.614	1.00	38.63		C
ATOM	5031	CD	PRO	X	14	−39.300	92.873	−37.204	1.00	38.01		C
ATOM	5032	N	GLY	X	15	−37.742	88.649	−38.754	1.00	42.53		N
ATOM	5033	CA	GLY	X	15	−37.352	87.856	−39.886	1.00	39.20		C
ATOM	5034	C	GLY	X	15	−35.927	88.040	−40.349	1.00	44.97		C
ATOM	5035	O	GLY	X	15	−35.426	87.186	−41.077	1.00	48.28		O
ATOM	5036	N	GLN	X	16	−35.257	89.115	−39.944	1.00	41.58		N
ATOM	5037	CA	GLN	X	16	−33.915	89.385	−40.433	1.00	43.47		C
ATOM	5038	C	GLN	X	16	−32.862	88.623	−39.621	1.00	47.57		C
ATOM	5039	O	GLN	X	16	−33.167	87.903	−38.664	1.00	46.60		O
ATOM	5040	CB	GLN	X	16	−33.635	90.888	−40.417	1.00	52.99		C
ATOM	5041	CG	GLN	X	16	−34.303	91.702	−41.539	1.00	46.17		C
ATOM	5042	CD	GLN	X	16	−33.566	93.024	−41.807	1.00	74.76		C
ATOM	5043	OE1	GLN	X	16	−33.715	94.021	−41.064	1.00	62.51		O
ATOM	5044	NE2	GLN	X	16	−32.758	93.034	−42.866	1.00	79.00		N
ATOM	5045	N	LYS	X	17	−31.607	88.762	−40.053	1.00	53.20		N
ATOM	5046	CA	LYS	X	17	−30.415	88.195	−39.436	1.00	49.52		C
ATOM	5047	C	LYS	X	17	−29.695	89.254	−38.627	1.00	51.74		C
ATOM	5048	O	LYS	X	17	−29.796	90.454	−38.883	1.00	62.58		O
ATOM	5049	CB	LYS	X	17	−29.417	87.662	−40.469	1.00	49.86		C
ATOM	5050	CG	LYS	X	17	−29.783	86.391	−41.150	1.00	61.26		C
ATOM	5051	CD	LYS	X	17	−28.839	86.137	−42.317	1.00	75.06		C
ATOM	5052	CE	LYS	X	17	−29.295	84.939	−43.148	1.00	82.27		C
ATOM	5053	NZ	LYS	X	17	−28.391	84.723	−44.304	1.00	82.49		N
ATOM	5054	N	VAL	X	18	−28.913	88.785	−37.670	1.00	51.92		N
ATOM	5055	CA	VAL	X	18	−28.083	89.670	−36.876	1.00	47.06		C
ATOM	5056	C	VAL	X	18	−26.882	88.857	−36.416	1.00	42.24		C
ATOM	5057	O	VAL	X	18	−26.969	87.645	−36.210	1.00	39.00		O
ATOM	5058	CB	VAL	X	18	−28.932	90.288	−35.735	1.00	50.43		C
ATOM	5059	CG1	VAL	X	18	−28.437	89.925	−34.363	1.00	44.21		C
ATOM	5060	CG2	VAL	X	18	−29.054	91.783	−35.919	1.00	48.19		C
ATOM	5061	N	THR	X	19	−25.745	89.520	−36.323	1.00	40.09		N
ATOM	5062	CA	THR	X	19	−24.519	88.924	−35.825	1.00	43.49		C
ATOM	5063	C	THR	X	19	−24.005	89.770	−34.672	1.00	39.57		C
ATOM	5064	O	THR	X	19	−24.036	91.000	−34.737	1.00	39.43		O
ATOM	5065	CB	THR	X	19	−23.484	88.816	−36.961	1.00	40.40		C
ATOM	5066	OG1	THR	X	19	−23.352	87.443	−37.322	1.00	51.45		O
ATOM	5067	CG2	THR	X	19	−22.132	89.395	−36.582	1.00	45.74		C
ATOM	5068	N	ILE	X	20	−23.557	89.116	−33.607	1.00	36.67		N
ATOM	5069	CA	ILE	X	20	−23.009	89.805	−32.449	1.00	34.08		C
ATOM	5070	C	ILE	X	20	−21.638	89.219	−32.166	1.00	35.80		C
ATOM	5071	O	ILE	X	20	−21.517	88.008	−31.946	1.00	34.42		O
ATOM	5072	CB	ILE	X	20	−23.917	89.679	−31.210	1.00	36.76		C
ATOM	5073	CG1	ILE	X	20	−25.269	90.345	−31.467	1.00	35.10		C
ATOM	5074	CG2	ILE	X	20	−23.257	90.324	−29.996	1.00	27.82		C
ATOM	5075	CD1	ILE	X	20	−26.276	90.127	−30.364	1.00	28.66		C
ATOM	5076	N	SER	X	21	−20.614	90.068	−32.153	1.00	38.15		N
ATOM	5077	CA	SER	X	21	−19.237	89.614	−31.980	1.00	37.42		C
ATOM	5078	C	SER	X	21	−18.762	89.818	−30.547	1.00	38.58		C
ATOM	5079	O	SER	X	21	−19.344	90.570	−29.762	1.00	39.24		O
ATOM	5080	CB	SER	X	21	−18.290	90.351	−32.932	1.00	30.39		C
ATOM	5081	OG	SER	X	21	−18.312	91.741	−32.656	1.00	45.43		O
ATOM	5082	N	CYS	X	22	−17.662	89.152	−30.226	1.00	31.32		N
ATOM	5083	CA	CYS	X	22	−17.099	89.156	−28.883	1.00	33.00		C
ATOM	5084	C	CYS	X	22	−15.601	88.936	−29.035	1.00	36.67		C
ATOM	5085	O	CYS	X	22	−15.179	87.824	−29.367	1.00	33.05		O
ATOM	5086	CB	CYS	X	22	−17.737	88.067	−28.029	1.00	33.80		C
ATOM	5087	SG	CYS	X	22	−16.950	87.740	−26.422	1.00	49.12		S
ATOM	5088	N	SER	X	23	−14.806	89.986	−28.830	1.00	35.27		N
ATOM	5089	CA	SER	X	23	−13.362	89.917	−29.015	1.00	36.02		C
ATOM	5090	C	SER	X	23	−12.635	89.893	−27.682	1.00	35.20		C
ATOM	5091	O	SER	X	23	−12.961	90.659	−26.765	1.00	32.83		O
ATOM	5092	CB	SER	X	23	−12.847	91.105	−29.824	1.00	34.28		C
ATOM	5093	OG	SER	X	23	−13.487	91.109	−31.082	1.00	60.42		O
ATOM	5094	N	GLY	X	24	−11.631	89.027	−27.600	1.00	29.76		N
ATOM	5095	CA	GLY	X	24	−10.801	88.942	−26.426	1.00	32.74		C
ATOM	5096	C	GLY	X	24	−9.364	88.732	−26.822	1.00	36.96		C
ATOM	5097	O	GLY	X	24	−8.898	89.366	−27.766	1.00	35.74		O
ATOM	5098	N	SER	X	25	−8.666	87.829	−26.132	1.00	34.51		N
ATOM	5099	CA	SER	X	25	−7.238	87.632	−26.326	1.00	35.15		C
ATOM	5100	C	SER	X	25	−6.925	86.161	−26.114	1.00	38.46		C
ATOM	5101	O	SER	X	25	−7.793	85.366	−25.733	1.00	35.89		O
ATOM	5102	CB	SER	X	25	−6.411	88.485	−25.366	1.00	31.48		C
ATOM	5103	OG	SER	X	25	−6.531	87.980	−24.047	1.00	41.73		O
ATOM	5104	N	SER	X	26	−5.656	85.811	−26.338	1.00	32.62		N
ATOM	5105	CA	SER	X	26	−5.255	84.410	−26.269	1.00	40.22		C
ATOM	5106	C	SER	X	26	−5.478	83.825	−24.886	1.00	39.50		C
ATOM	5107	O	SER	X	26	−5.701	82.616	−24.755	1.00	43.16		O
ATOM	5108	CB	SER	X	26	−3.779	84.236	−26.645	1.00	33.65		C
ATOM	5109	OG	SER	X	26	−2.978	85.154	−25.933	1.00	50.17		O
ATOM	5110	N	SER	X	27	−5.442	84.650	−23.847	1.00	37.12		N
ATOM	5111	CA	SER	X	27	−5.564	84.097	−22.504	1.00	35.96		C
ATOM	5112	C	SER	X	27	−7.010	83.927	−22.062	1.00	36.99		C
ATOM	5113	O	SER	X	27	−7.236	83.380	−20.976	1.00	37.69		O
ATOM	5114	CB	SER	X	27	−4.848	84.982	−21.480	1.00	32.77		C
ATOM	5115	OG	SER	X	27	−5.484	86.238	−21.459	1.00	46.10		O
ATOM	5116	N	ASN	X	28	−7.992	84.407	−22.840	1.00	35.46		N
ATOM	5117	CA	ASN	X	28	−9.372	84.080	−22.495	1.00	33.17		C
ATOM	5118	C	ASN	X	28	−10.056	83.327	−23.636	1.00	34.99		C
ATOM	5119	O	ASN	X	28	−10.028	82.089	−23.659	1.00	30.44		O
ATOM	5120	CB	ASN	X	28	−10.161	85.324	−22.072	1.00	29.46		C
ATOM	5121	CG	ASN	X	28	−9.945	86.529	−22.981	1.00	33.39		C
ATOM	5122	OD1	ASN	X	28	−10.325	86.527	−24.163	1.00	33.37		O
ATOM	5123	ND2	ASN	X	28	−9.394	87.594	−22.408	1.00	28.13		N
ATOM	5124	N	ILE	X	29	−10.677	84.041	−24.577	1.00	26.63		N
ATOM	5125	CA	ILE	X	29	−11.370	83.349	−25.660	1.00	33.95		C
ATOM	5126	C	ILE	X	29	−10.423	82.422	−26.417	1.00	37.55		C
ATOM	5127	O	ILE	X	29	−10.814	81.335	−26.857	1.00	33.77		O
ATOM	5128	CB	ILE	X	29	−12.029	84.355	−26.611	1.00	31.78		C
ATOM	5129	CG1	ILE	X	29	−13.165	85.074	−25.894	1.00	37.08		C
ATOM	5130	CG2	ILE	X	29	−12.570	83.634	−27.846	1.00	27.80		C
ATOM	5131	CD1	ILE	X	29	−13.921	85.975	−26.801	1.00	36.60		C
ATOM	5132	N	GLY	X	30	−9.171	82.838	−26.596	1.00	38.13		N
ATOM	5133	CA	GLY	X	30	−8.264	82.044	−27.399	1.00	32.55		C
ATOM	5134	C	GLY	X	30	−7.961	80.683	−26.819	1.00	33.31		C
ATOM	5135	O	GLY	X	30	−7.589	79.781	−27.559	1.00	43.57		O
ATOM	5136	N	ASN	X	31	−8.136	80.495	−25.521	1.00	40.07		N
ATOM	5137	CA	ASN	X	31	−7.797	79.191	−24.968	1.00	37.30		C
ATOM	5138	C	ASN	X	31	−8.808	78.618	−23.980	1.00	36.23		C
ATOM	5139	O	ASN	X	31	−8.500	77.622	−23.324	1.00	37.83		O
ATOM	5140	CB	ASN	X	31	−6.405	79.245	−24.343	1.00	43.50		C
ATOM	5141	CG	ASN	X	31	−5.314	79.117	−25.408	1.00	56.73		C
ATOM	5142	OD1	ASN	X	31	−5.006	78.007	−25.858	1.00	58.50		O
ATOM	5143	ND2	ASN	X	31	−4.764	80.253	−25.851	1.00	48.77		N
ATOM	5144	N	ASN	X	32	−10.015	79.157	−23.886	1.00	33.81		N
ATOM	5145	CA	ASN	X	32	−10.979	78.603	−22.954	1.00	35.74		C
ATOM	5146	C	ASN	X	32	−12.338	78.460	−23.628	1.00	33.34		C
ATOM	5147	O	ASN	X	32	−12.583	79.011	−24.700	1.00	34.66		O
ATOM	5148	CB	ASN	X	32	−11.035	79.466	−21.699	1.00	32.31		C
ATOM	5149	CG	ASN	X	32	−9.711	79.508	−20.983	1.00	33.00		C
ATOM	5150	OD1	ASN	X	32	−9.339	78.559	−20.300	1.00	35.81		O
ATOM	5151	ND2	ASN	X	32	−8.979	80.606	−21.141	1.00	40.72		N
ATOM	5152	N	TYR	X	33	−13.220	77.691	−22.998	1.00	33.41		N
ATOM	5153	CA	TYR	X	33	−14.543	77.451	−23.572	1.00	35.49		C
ATOM	5154	C	TYR	X	33	−15.355	78.735	−23.542	1.00	30.39		C
ATOM	5155	O	TYR	X	33	−15.333	79.455	−22.555	1.00	29.67		O
ATOM	5156	CB	TYR	X	33	−15.281	76.348	−22.793	1.00	28.71		C
ATOM	5157	CG	TYR	X	33	−14.627	74.978	−22.878	1.00	33.53		C
ATOM	5158	CD1	TYR	X	33	−14.513	74.311	−24.098	1.00	27.38		C
ATOM	5159	CD2	TYR	X	33	−14.115	74.356	−21.740	1.00	32.47		C
ATOM	5160	CE1	TYR	X	33	−13.915	73.063	−24.178	1.00	30.49		C
ATOM	5161	CE2	TYR	X	33	−13.514	73.101	−21.813	1.00	31.14		C
ATOM	5162	CZ	TYR	X	33	−13.409	72.468	−23.043	1.00	31.76		C
ATOM	5163	OH	TYR	X	33	−12.815	71.235	−23.121	1.00	31.17		O
ATOM	5164	N	VAL	X	34	−16.106	79.006	−24.602	1.00	29.15		N
ATOM	5165	CA	VAL	X	34	−16.887	80.240	−24.708	1.00	36.08		C
ATOM	5166	C	VAL	X	34	−18.366	79.954	−24.434	1.00	32.87		C
ATOM	5167	O	VAL	X	34	−18.934	79.011	−24.996	1.00	30.79		O
ATOM	5168	CB	VAL	X	34	−16.704	80.865	−26.098	1.00	33.81		C
ATOM	5169	CG1	VAL	X	34	−17.582	82.090	−26.255	1.00	27.19		C
ATOM	5170	CG2	VAL	X	34	−15.243	81.172	−26.332	1.00	32.31		C
ATOM	5171	N	SER	X	35	−19.008	80.798	−23.617	1.00	32.88		N
ATOM	5172	CA	SER	X	35	−20.444	80.696	−23.349	1.00	30.32		C
ATOM	5173	C	SER	X	35	−21.176	81.975	−23.759	1.00	32.72		C
ATOM	5174	O	SER	X	35	−20.616	83.075	−23.709	1.00	28.89		O
ATOM	5175	CB	SER	X	35	−20.725	80.419	−21.869	1.00	28.37		C
ATOM	5176	OG	SER	X	35	−20.265	79.144	−21.480	1.00	28.41		O
ATOM	5177	N	TRP	X	36	−22.446	81.832	−24.154	1.00	28.96		N
ATOM	5178	CA	TRP	X	36	−23.308	82.972	−24.451	1.00	27.19		C
ATOM	5179	C	TRP	X	36	−24.541	82.934	−23.566	1.00	32.55		C
ATOM	5180	O	TRP	X	36	−25.151	81.873	−23.374	1.00	33.96		O
ATOM	5181	CB	TRP	X	36	−23.738	83.010	−25.915	1.00	28.66		C
ATOM	5182	CG	TRP	X	36	−22.661	83.470	−26.893	1.00	32.03		C
ATOM	5183	CD1	TRP	X	36	−21.775	82.676	−27.576	1.00	30.86		C
ATOM	5184	CD2	TRP	X	36	−22.382	84.821	−27.305	1.00	29.58		C
ATOM	5185	NE1	TRP	X	36	−20.965	83.451	−28.377	1.00	29.86		N
ATOM	5186	CE2	TRP	X	36	−21.320	84.767	−28.231	1.00	32.46		C
ATOM	5187	CE3	TRP	X	36	−22.926	86.067	−26.979	1.00	30.71		C
ATOM	5188	CZ2	TRP	X	36	−20.784	85.917	−28.827	1.00	34.25		C
ATOM	5189	CZ3	TRP	X	36	−22.391	87.204	−27.571	1.00	32.12		C
ATOM	5190	CH2	TRP	X	36	−21.329	87.120	−28.480	1.00	31.97		C
ATOM	5191	N	TYR	X	37	−24.909	84.105	−23.040	1.00	34.18		N
ATOM	5192	CA	TYR	X	37	−26.054	84.256	−22.152	1.00	28.55		C
ATOM	5193	C	TYR	X	37	−27.044	85.232	−22.763	1.00	30.63		C
ATOM	5194	O	TYR	X	37	−26.646	86.220	−23.399	1.00	30.08		O
ATOM	5195	CB	TYR	X	37	−25.607	84.731	−20.760	1.00	24.98		C
ATOM	5196	CG	TYR	X	37	−24.567	83.797	−20.195	1.00	29.34		C
ATOM	5197	CD1	TYR	X	37	−24.941	82.601	−19.573	1.00	27.60		C
ATOM	5198	CD2	TYR	X	37	−23.210	84.059	−20.346	1.00	27.93		C
ATOM	5199	CE1	TYR	X	37	−23.978	81.699	−19.056	1.00	30.73		C
ATOM	5200	CE2	TYR	X	37	−22.234	83.172	−19.828	1.00	31.38		C
ATOM	5201	CZ	TYR	X	37	−22.629	81.990	−19.195	1.00	32.90		C
ATOM	5202	OH	TYR	X	37	−21.685	81.119	−18.701	1.00	30.71		O
ATOM	5203	N	GLN	X	38	−28.331	84.926	−22.592	1.00	29.50		N
ATOM	5204	CA	GLN	X	38	−29.430	85.780	−23.026	1.00	30.90		C
ATOM	5205	C	GLN	X	38	−30.211	86.252	−21.807	1.00	31.01		C
ATOM	5206	O	GLN	X	38	−30.612	85.436	−20.970	1.00	29.04		O
ATOM	5207	CB	GLN	X	38	−30.365	85.044	−23.979	1.00	27.81		C
ATOM	5208	CG	GLN	X	38	−31.587	85.851	−24.407	1.00	27.64		C
ATOM	5209	CD	GLN	X	38	−32.640	84.958	−25.007	1.00	34.54		C
ATOM	5210	OE1	GLN	X	38	−33.141	84.043	−24.329	1.00	34.50		O
ATOM	5211	NE2	GLN	X	38	−32.985	85.195	−26.279	1.00	26.87		N
ATOM	5212	N	GLN	X	39	−30.416	87.566	−21.705	1.00	29.58		N
ATOM	5213	CA	GLN	X	39	−31.199	88.157	−20.623	1.00	29.79		C
ATOM	5214	C	GLN	X	39	−32.378	88.907	−21.252	1.00	36.36		C
ATOM	5215	O	GLN	X	39	−32.234	90.040	−21.731	1.00	37.54		O
ATOM	5216	CB	GLN	X	39	−30.341	89.067	−19.749	1.00	26.28		C
ATOM	5217	CG	GLN	X	39	−31.077	89.513	−18.479	1.00	31.07		C
ATOM	5218	CD	GLN	X	39	−30.207	90.302	−17.520	1.00	33.21		C
ATOM	5219	OE1	GLN	X	39	−29.255	90.951	−17.926	1.00	33.77		O
ATOM	5220	NE2	GLN	X	39	−30.542	90.260	−16.241	1.00	34.37		N
ATOM	5221	N	LEU	X	40	−33.539	88.255	−21.271	1.00	32.04		N
ATOM	5222	CA	LEU	X	40	−34.756	88.889	−21.729	1.00	34.90		C
ATOM	5223	C	LEU	X	40	−35.132	90.007	−20.753	1.00	38.54		C
ATOM	5224	O	LEU	X	40	−34.759	89.948	−19.575	1.00	31.68		O
ATOM	5225	CB	LEU	X	40	−35.872	87.851	−21.832	1.00	33.07		C
ATOM	5226	CG	LEU	X	40	−35.490	86.643	−22.697	1.00	39.00		C
ATOM	5227	CD1	LEU	X	40	−36.411	85.450	−22.373	1.00	38.05		C
ATOM	5228	CD2	LEU	X	40	−35.493	86.947	−24.228	1.00	26.12		C
ATOM	5229	N	PRO	X	41	−35.826	91.047	−21.227	1.00	36.64		N
ATOM	5230	CA	PRO	X	41	−36.146	92.208	−20.371	1.00	41.13		C
ATOM	5231	C	PRO	X	41	−36.855	91.770	−19.096	1.00	38.67		C
ATOM	5232	O	PRO	X	41	−37.737	90.913	−19.128	1.00	32.82		O
ATOM	5233	CB	PRO	X	41	−37.079	93.058	−21.246	1.00	36.21		C
ATOM	5234	CG	PRO	X	41	−36.885	92.555	−22.651	1.00	38.84		C
ATOM	5235	CD	PRO	X	41	−36.528	91.097	−22.519	1.00	39.30		C
ATOM	5236	N	GLY	X	42	−36.410	92.308	−17.961	1.00	37.25		N
ATOM	5237	CA	GLY	X	42	−36.981	91.946	−16.678	1.00	39.06		C
ATOM	5238	C	GLY	X	42	−36.772	90.514	−16.194	1.00	47.15		C
ATOM	5239	O	GLY	X	42	−37.474	90.080	−15.269	1.00	47.29		O
ATOM	5240	N	THR	X	43	−35.830	89.759	−16.760	1.00	42.87		N
ATOM	5241	CA	THR	X	43	−35.594	88.390	−16.295	1.00	41.60		C
ATOM	5242	C	THR	X	43	−34.125	88.218	−15.937	1.00	34.86		C
ATOM	5243	O	THR	X	43	−33.283	89.070	−16.225	1.00	35.66		O
ATOM	5244	CB	THR	X	43	−35.966	87.300	−17.340	1.00	38.72		C
ATOM	5245	OG1	THR	X	43	−34.965	87.232	−18.372	1.00	37.04		O
ATOM	5246	CG2	THR	X	43	−37.299	87.578	−18.007	1.00	39.86		C
ATOM	5247	N	ALA	X	44	−33.838	87.056	−15.351	1.00	36.79		N
ATOM	5248	CA	ALA	X	44	−32.495	86.614	−15.069	1.00	33.26		C
ATOM	5249	C	ALA	X	44	−31.804	86.190	−16.368	1.00	34.93		C
ATOM	5250	O	ALA	X	44	−32.466	85.879	−17.358	1.00	32.13		O
ATOM	5251	CB	ALA	X	44	−32.537	85.449	−14.085	1.00	29.97		C
ATOM	5252	N	PRO	X	45	−30.470	86.187	−16.399	1.00	31.73		N
ATOM	5253	CA	PRO	X	45	−29.779	85.591	−17.540	1.00	29.03		C
ATOM	5254	C	PRO	X	45	−30.152	84.124	−17.700	1.00	32.97		C
ATOM	5255	O	PRO	X	45	−30.631	83.455	−16.779	1.00	27.00		O
ATOM	5256	CB	PRO	X	45	−28.294	85.750	−17.187	1.00	29.30		C
ATOM	5257	CG	PRO	X	45	−28.267	86.928	−16.262	1.00	32.14		C
ATOM	5258	CD	PRO	X	45	−29.524	86.784	−15.442	1.00	28.71		C
ATOM	5259	N	LYS	X	46	−29.905	83.624	−18.898	1.00	28.36		N
ATOM	5260	CA	LYS	X	46	−30.155	82.237	−19.238	1.00	34.68		C
ATOM	5261	C	LYS	X	46	−29.009	81.792	−20.131	1.00	35.47		C
ATOM	5262	O	LYS	X	46	−28.503	82.593	−20.930	1.00	27.61		O
ATOM	5263	CB	LYS	X	46	−31.500	82.135	−19.949	1.00	31.10		C
ATOM	5264	CG	LYS	X	46	−31.750	80.915	−20.700	1.00	41.49		C
ATOM	5265	CD	LYS	X	46	−32.725	81.196	−21.858	1.00	47.60		C
ATOM	5266	CE	LYS	X	46	−33.943	81.979	−21.420	1.00	48.37		C
ATOM	5267	NZ	LYS	X	46	−35.081	81.729	−22.345	1.00	49.13		N1+
ATOM	5268	N	LEU	X	47	−28.574	80.539	−19.977	1.00	28.77		N
ATOM	5269	CA	LEU	X	47	−27.546	80.027	−20.872	1.00	24.97		C
ATOM	5270	C	LEU	X	47	−28.138	79.828	−22.264	1.00	32.77		C
ATOM	5271	O	LEU	X	47	−29.190	79.200	−22.426	1.00	29.18		O
ATOM	5272	CB	LEU	X	47	−26.955	78.730	−20.347	1.00	26.07		C
ATOM	5273	CG	LEU	X	47	−25.872	78.105	−21.231	1.00	29.09		C
ATOM	5274	CD1	LEU	X	47	−24.689	79.042	−21.402	1.00	29.03		C
ATOM	5275	CD2	LEU	X	47	−25.420	76.789	−20.647	1.00	27.90		C
ATOM	5276	N	LEU	X	48	−27.482	80.418	−23.260	1.00	30.28		N
ATOM	5277	CA	LEU	X	48	−27.901	80.361	−24.651	1.00	33.70		C
ATOM	5278	C	LEU	X	48	−27.075	79.352	−25.441	1.00	38.84		C
ATOM	5279	O	LEU	X	48	−27.633	78.536	−26.179	1.00	35.80		O
ATOM	5280	CB	LEU	X	48	−27.787	81.757	−25.286	1.00	30.10		C
ATOM	5281	CG	LEU	X	48	−28.388	81.949	−26.684	1.00	36.25		C
ATOM	5282	CD1	LEU	X	48	−29.916	81.905	−26.686	1.00	29.13		C
ATOM	5283	CD2	LEU	X	48	−27.887	83.232	−27.342	1.00	32.77		C
ATOM	5284	N	LEU	X	49	−25.749	79.397	−25.279	1.00	38.10		N
ATOM	5285	CA	LEU	X	49	−24.799	78.535	−25.968	1.00	29.61		C
ATOM	5286	C	LEU	X	49	−23.642	78.253	−25.028	1.00	31.16		C
ATOM	5287	O	LEU	X	49	−23.153	79.160	−24.352	1.00	32.51		O
ATOM	5288	CB	LEU	X	49	−24.241	79.177	−27.235	1.00	29.50		C
ATOM	5289	CG	LEU	X	49	−25.158	79.484	−28.410	1.00	35.20		C
ATOM	5290	CD1	LEU	X	49	−24.385	80.328	−29.434	1.00	32.31		C
ATOM	5291	CD2	LEU	X	49	−25.624	78.172	−29.024	1.00	29.29		C
ATOM	5292	N	TYR	X	50	−23.204	77.003	−24.983	1.00	27.72		N
ATOM	5293	CA	TYR	X	50	−21.976	76.679	−24.285	1.00	28.60		C
ATOM	5294	C	TYR	X	50	−21.037	75.963	−25.242	1.00	30.23		C
ATOM	5295	O	TYR	X	50	−21.429	75.569	−26.346	1.00	31.08		O
ATOM	5296	CB	TYR	X	50	−22.250	75.864	−23.018	1.00	28.65		C
ATOM	5297	CG	TYR	X	50	−22.900	74.531	−23.227	1.00	33.55		C
ATOM	5298	CD1	TYR	X	50	−24.246	74.422	−23.613	1.00	37.48		C
ATOM	5299	CD2	TYR	X	50	−22.196	73.384	−22.985	1.00	29.14		C
ATOM	5300	CE1	TYR	X	50	−24.833	73.183	−23.799	1.00	34.48		C
ATOM	5301	CE2	TYR	X	50	−22.768	72.149	−23.152	1.00	39.17		C
ATOM	5302	CZ	TYR	X	50	−24.076	72.041	−23.550	1.00	38.17		C
ATOM	5303	OH	TYR	X	50	−24.590	70.771	−23.700	1.00	35.08		O
ATOM	5304	N	ASP	X	51	−19.768	75.877	−24.840	1.00	31.56		N
ATOM	5305	CA	ASP	X	51	−18.698	75.390	−25.713	1.00	29.21		C
ATOM	5306	C	ASP	X	51	−18.816	76.000	−27.122	1.00	34.44		C
ATOM	5307	O	ASP	X	51	−18.908	75.308	−28.144	1.00	31.23		O
ATOM	5308	CB	ASP	X	51	−18.699	73.865	−25.753	1.00	30.93		C
ATOM	5309	CG	ASP	X	51	−17.509	73.308	−26.507	1.00	34.52		C
ATOM	5310	OD1	ASP	X	51	−16.467	74.009	−26.589	1.00	38.97		O
ATOM	5311	OD2	ASP	X	51	−17.633	72.187	−27.047	1.00	37.63		O1−
ATOM	5312	N	SER	X	52	−18.882	77.333	−27.151	1.00	29.36		N
ATOM	5313	CA	SER	X	52	−18.957	78.121	−28.379	1.00	32.69		C
ATOM	5314	C	SER	X	52	−20.258	77.970	−29.163	1.00	32.50		C
ATOM	5315	O	SER	X	52	−20.805	78.977	−29.637	1.00	32.67		O
ATOM	5316	CB	SER	X	52	−17.781	77.808	−29.305	1.00	32.99		C
ATOM	5317	OG	SER	X	52	−16.569	78.277	−28.744	1.00	42.26		O
ATOM	5318	N	ASN	X	53	−20.772	76.746	−29.333	1.00	31.33		N
ATOM	5319	CA	ASN	X	53	−21.880	76.604	−30.271	1.00	33.53		C
ATOM	5320	C	ASN	X	53	−22.896	75.532	−29.886	1.00	36.41		C
ATOM	5321	O	ASN	X	53	−23.725	75.172	−30.735	1.00	34.64		O
ATOM	5322	CB	ASN	X	53	−21.326	76.305	−31.671	1.00	29.24		C
ATOM	5323	CG	ASN	X	53	−20.625	74.953	−31.730	1.00	38.39		C
ATOM	5324	OD1	ASN	X	53	−20.519	74.254	−30.721	1.00	35.56		O
ATOM	5325	ND2	ASN	X	53	−20.163	74.573	−32.906	1.00	35.38		N
ATOM	5326	N	LYS	X	54	−22.879	75.013	−28.657	1.00	37.93		N
ATOM	5327	CA	LYS	X	54	−23.821	73.978	−28.239	1.00	37.84		C
ATOM	5328	C	LYS	X	54	−25.063	74.592	−27.605	1.00	33.93		C
ATOM	5329	O	LYS	X	54	−24.957	75.380	−26.656	1.00	33.00		O
ATOM	5330	CB	LYS	X	54	−23.165	73.014	−27.250	1.00	34.82		C
ATOM	5331	CG	LYS	X	54	−24.025	71.814	−26.907	1.00	36.40		C
ATOM	5332	CD	LYS	X	54	−24.191	70.937	−28.131	1.00	37.62		C
ATOM	5333	CE	LYS	X	54	−25.209	69.832	−27.894	1.00	33.30		C
ATOM	5334	NZ	LYS	X	54	−25.145	68.918	−29.053	1.00	47.57		N1+
ATOM	5335	N	AARG	X	55	−26.235	74.212	−28.121	0.50	35.72		N
ATOM	5336	CA	AARG	X	55	−27.511	74.703	−27.600	0.50	37.84		C
ATOM	5337	C	AARG	X	55	−27.955	73.849	−26.418	0.50	37.19		C
ATOM	5338	O	AARG	X	55	−28.052	72.622	−26.555	0.50	39.62		O
ATOM	5339	CB	AARG	X	55	−28.585	74.683	−28.683	0.50	35.53		C
ATOM	5340	CG	AARG	X	55	−28.487	75.808	−29.722	0.50	38.76		C
ATOM	5341	CD	AARG	X	55	−29.610	75.753	−30.781	0.50	37.60		C
ATOM	5342	NE	AARG	X	55	−29.427	74.636	−31.705	0.50	42.24		N
ATOM	5343	CZ	AARG	X	55	−30.198	73.555	−31.759	0.50	40.39		C
ATOM	5344	NH1	AARG	X	55	−29.919	72.598	−32.628	0.50	43.66		N1+
ATOM	5345	NH2	AARG	X	55	−31.248	73.434	−30.961	0.50	39.76		N
ATOM	5346	N	BARG	X	55	−26.235	74.213	−28.110	0.50	35.73		N
ATOM	5347	CA	BARG	X	55	−27.499	74.742	−27.594	0.50	37.86		C
ATOM	5348	C	BARG	X	55	−27.999	73.875	−26.441	0.50	37.17		C
ATOM	5349	O	BARG	X	55	−28.165	72.661	−26.619	0.50	39.65		O
ATOM	5350	CB	BARG	X	55	−28.548	74.810	−28.701	0.50	35.58		C
ATOM	5351	CG	BARG	X	55	−28.335	75.971	−29.695	0.50	38.67		C
ATOM	5352	CD	BARG	X	55	−29.274	75.940	−30.919	0.50	37.26		C
ATOM	5353	NE	BARG	X	55	−28.921	74.866	−31.845	0.50	42.86		N
ATOM	5354	CZ	BARG	X	55	−28.062	74.983	−32.859	0.50	43.30		C
ATOM	5355	NH1	BARG	X	55	−27.465	76.140	−33.108	0.50	28.23		N1+
ATOM	5356	NH2	BARG	X	55	−27.803	73.928	−33.632	0.50	47.26		N
ATOM	5357	N	PRO	X	56	−28.209	74.432	−25.251	1.00	39.61		N
ATOM	5358	CA	PRO	X	56	−28.924	73.683	−24.208	1.00	37.27		C
ATOM	5359	C	PRO	X	56	−30.328	73.384	−24.708	1.00	37.17		C
ATOM	5360	O	PRO	X	56	−30.836	74.048	−25.614	1.00	35.06		O
ATOM	5361	CB	PRO	X	56	−28.960	74.643	−23.020	1.00	32.87		C
ATOM	5362	CG	PRO	X	56	−28.041	75.768	−23.374	1.00	39.79		C
ATOM	5363	CD	PRO	X	56	−27.841	75.794	−24.846	1.00	34.03		C
ATOM	5364	N	SER	X	57	−30.973	72.378	−24.127	1.00	35.37		N
ATOM	5365	CA	SER	X	57	−32.324	72.095	−24.603	1.00	45.77		C
ATOM	5366	C	SER	X	57	−33.240	73.271	−24.286	1.00	39.53		C
ATOM	5367	O	SER	X	57	−33.082	73.960	−23.274	1.00	42.51		O
ATOM	5368	CB	SER	X	57	−32.860	70.777	−24.033	1.00	44.76		C
ATOM	5369	OG	SER	X	57	−32.486	70.611	−22.686	1.00	57.37		O
ATOM	5370	N	GLY	X	58	−34.149	73.551	−25.208	1.00	46.11		N
ATOM	5371	CA	GLY	X	58	−35.017	74.704	−25.108	1.00	38.41		C
ATOM	5372	C	GLY	X	58	−34.575	75.906	−25.915	1.00	46.36		C
ATOM	5373	O	GLY	X	58	−35.360	76.846	−26.056	1.00	47.75		O
ATOM	5374	N	ILE	X	59	−33.356	75.916	−26.442	1.00	38.47		N
ATOM	5375	CA	ILE	X	59	−32.858	77.042	−27.231	1.00	39.45		C
ATOM	5376	C	ILE	X	59	−33.096	76.740	−28.706	1.00	38.36		C
ATOM	5377	O	ILE	X	59	−32.567	75.743	−29.218	1.00	41.39		O
ATOM	5378	CB	ILE	X	59	−31.372	77.301	−26.950	1.00	41.60		C
ATOM	5379	CG1	ILE	X	59	−31.165	77.604	−25.460	1.00	39.46		C
ATOM	5380	CG2	ILE	X	59	−30.858	78.449	−27.839	1.00	36.16		C
ATOM	5381	CD1	ILE	X	59	−31.957	78.855	−24.970	1.00	33.58		C
ATOM	5382	N	PRO	X	60	−33.829	77.583	−29.429	1.00	38.04		N
ATOM	5383	CA	PRO	X	60	−34.124	77.311	−30.841	1.00	40.67		C
ATOM	5384	C	PRO	X	60	−32.877	77.315	−31.712	1.00	41.79		C
ATOM	5385	O	PRO	X	60	−31.899	78.020	−31.439	1.00	39.12		O
ATOM	5386	CB	PRO	X	60	−35.047	78.468	−31.240	1.00	37.50		C
ATOM	5387	CG	PRO	X	60	−35.340	79.184	−30.024	1.00	40.79		C
ATOM	5388	CD	PRO	X	60	−34.325	78.891	−29.004	1.00	41.33		C
ATOM	5389	N	ALA	X	61	−32.956	76.574	−32.821	1.00	41.88		N
ATOM	5390	CA	ALA	X	61	−31.816	76.464	−33.727	1.00	41.28		C
ATOM	5391	C	ALA	X	61	−31.500	77.762	−34.449	1.00	37.80		C
ATOM	5392	O	ALA	X	61	−30.440	77.855	−35.066	1.00	37.27		O
ATOM	5393	CB	ALA	X	61	−32.043	75.362	−34.759	1.00	34.30		C
ATOM	5394	N	ARG	X	62	−32.356	78.779	−34.366	1.00	38.43		N
ATOM	5395	CA	ARG	X	62	−31.978	80.019	−35.031	1.00	42.28		C
ATOM	5396	C	ARG	X	62	−30.888	80.776	−34.273	1.00	39.16		C
ATOM	5397	O	ARG	X	62	−30.360	81.763	−34.795	1.00	42.60		O
ATOM	5398	CB	ARG	X	62	−33.215	80.894	−35.260	1.00	40.18		C
ATOM	5399	CG	ARG	X	62	−33.956	81.319	−34.029	1.00	45.22		C
ATOM	5400	CD	ARG	X	62	−35.169	82.228	−34.403	1.00	57.00		C
ATOM	5401	NE	ARG	X	62	−35.710	82.874	−33.214	1.00	45.98		N
ATOM	5402	CZ	ARG	X	62	−36.485	82.241	−32.345	1.00	47.84		C
ATOM	5403	NH1	ARG	X	62	−36.807	80.976	−32.560	1.00	50.34		N1+
ATOM	5404	NH2	ARG	X	62	−36.923	82.855	−31.261	1.00	51.21		N
ATOM	5405	N	PHE	X	63	−30.522	80.330	−33.074	1.00	40.25		N
ATOM	5406	CA	PHE	X	63	−29.323	80.816	−32.410	1.00	41.09		C
ATOM	5407	C	PHE	X	63	−28.171	79.886	−32.756	1.00	41.66		C
ATOM	5408	O	PHE	X	63	−28.299	78.666	−32.622	1.00	35.82		O
ATOM	5409	CB	PHE	X	63	−29.510	80.887	−30.891	1.00	33.46		C
ATOM	5410	CG	PHE	X	63	−30.586	81.832	−30.473	1.00	36.45		C
ATOM	5411	CD1	PHE	X	63	−30.310	83.184	−30.280	1.00	39.83		C
ATOM	5412	CD2	PHE	X	63	−31.884	81.377	−30.287	1.00	34.93		C
ATOM	5413	CE1	PHE	X	63	−31.325	84.085	−29.906	1.00	36.05		C
ATOM	5414	CE2	PHE	X	63	−32.889	82.251	−29.923	1.00	38.93		C
ATOM	5415	CZ	PHE	X	63	−32.614	83.614	−29.734	1.00	35.26		C
ATOM	5416	N	SER	X	64	−27.053	80.455	−33.207	1.00	33.96		N
ATOM	5417	CA	SER	X	64	−25.866	79.646	−33.436	1.00	36.60		C
ATOM	5418	C	SER	X	64	−24.626	80.455	−33.101	1.00	33.97		C
ATOM	5419	O	SER	X	64	−24.663	81.684	−32.984	1.00	37.04		O
ATOM	5420	CB	SER	X	64	−25.792	79.134	−34.878	1.00	33.50		C
ATOM	5421	OG	SER	X	64	−25.828	80.219	−35.797	1.00	41.55		O
ATOM	5422	N	GLY	X	65	−23.514	79.743	−32.965	1.00	33.67		N
ATOM	5423	CA	GLY	X	65	−22.271	80.366	−32.569	1.00	32.37		C
ATOM	5424	C	GLY	X	65	−21.099	79.800	−33.342	1.00	37.26		C
ATOM	5425	O	GLY	X	65	−21.144	78.694	−33.885	1.00	37.56		O
ATOM	5426	N	SER	X	66	−20.044	80.596	−33.386	1.00	36.95		N
ATOM	5427	CA	SER	X	66	−18.782	80.154	−33.937	1.00	39.89		C
ATOM	5428	C	SER	X	66	−17.675	80.805	−33.137	1.00	38.97		C
ATOM	5429	O	SER	X	66	−17.884	81.794	−32.427	1.00	42.94		O
ATOM	5430	CB	SER	X	66	−18.645	80.521	−35.416	1.00	43.54		C
ATOM	5431	OG	SER	X	66	−18.842	81.914	−35.579	1.00	44.16		O
ATOM	5432	N	LYS	X	67	−16.493	80.236	−33.268	1.00	37.88		N
ATOM	5433	CA	LYS	X	67	−15.318	80.724	−32.578	1.00	38.71		C
ATOM	5434	C	LYS	X	67	−14.182	80.683	−33.584	1.00	41.62		C
ATOM	5435	O	LYS	X	67	−14.049	79.712	−34.332	1.00	36.78		O
ATOM	5436	CB	LYS	X	67	−14.996	79.866	−31.337	1.00	34.63		C
ATOM	5437	CG	LYS	X	67	−13.718	80.278	−30.577	1.00	39.36		C
ATOM	5438	CD	LYS	X	67	−13.483	79.408	−29.335	1.00	43.58		C
ATOM	5439	CE	LYS	X	67	−12.029	79.470	−28.865	1.00	49.06		C
ATOM	5440	NZ	LYS	X	67	−11.798	78.829	−27.509	1.00	45.19		N1+
ATOM	5441	N	SER	X	68	−13.372	81.733	−33.603	1.00	32.64		N
ATOM	5442	CA	SER	X	68	−12.213	81.766	−34.484	1.00	39.05		C
ATOM	5443	C	SER	X	68	−11.107	82.533	−33.774	1.00	44.53		C
ATOM	5444	O	SER	X	68	−11.196	83.760	−33.617	1.00	37.82		O
ATOM	5445	CB	SER	X	68	−12.578	82.412	−35.816	1.00	40.60		C
ATOM	5446	OG	SER	X	68	−11.432	82.493	−36.637	1.00	69.58		O
ATOM	5447	N	GLY	X	69	−10.073	81.825	−33.344	1.00	41.45		N
ATOM	5448	CA	GLY	X	69	−8.973	82.520	−32.683	1.00	38.45		C
ATOM	5449	C	GLY	X	69	−9.424	83.162	−31.382	1.00	38.09		C
ATOM	5450	O	GLY	X	69	−9.944	82.493	−30.485	1.00	40.05		O
ATOM	5451	N	THR	X	70	−9.248	84.479	−31.260	1.00	38.95		N
ATOM	5452	CA	THR	X	70	−9.575	85.191	−30.033	1.00	31.37		C
ATOM	5453	C	THR	X	70	−10.914	85.919	−30.101	1.00	36.24		C
ATOM	5454	O	THR	X	70	−11.192	86.796	−29.271	1.00	37.77		O
ATOM	5455	CB	THR	X	70	−8.458	86.171	−29.692	1.00	36.81		C
ATOM	5456	OG1	THR	X	70	−8.349	87.134	−30.744	1.00	30.74		O
ATOM	5457	CG2	THR	X	70	−7.134	85.414	−29.544	1.00	25.19		C
ATOM	5458	N	SER	X	71	−11.765	85.574	−31.048	1.00	37.57		N
ATOM	5459	CA	SER	X	71	−13.081	86.175	−31.072	1.00	38.07		C
ATOM	5460	C	SER	X	71	−14.125	85.082	−31.262	1.00	38.54		C
ATOM	5461	O	SER	X	71	−13.834	83.992	−31.759	1.00	37.91		O
ATOM	5462	CB	SER	X	71	−13.185	87.249	−32.162	1.00	40.23		C
ATOM	5463	OG	SER	X	71	−13.241	86.662	−33.448	1.00	48.33		O
ATOM	5464	N	ALA	X	72	−15.344	85.387	−30.821	1.00	30.70		N
ATOM	5465	CA	ALA	X	72	−16.491	84.505	−30.944	1.00	32.65		C
ATOM	5466	C	ALA	X	72	−17.649	85.344	−31.464	1.00	33.91		C
ATOM	5467	O	ALA	X	72	−17.724	86.538	−31.199	1.00	35.37		O
ATOM	5468	CB	ALA	X	72	−16.847	83.861	−29.596	1.00	28.85		C
ATOM	5469	N	ATHR	X	73	−18.543	84.722	−32.219	0.60	34.81		N
ATOM	5470	CA	ATHR	X	73	−19.686	85.428	−32.781	0.60	36.26		C
ATOM	5471	C	ATHR	X	73	−20.968	84.644	−32.530	0.60	38.23		C
ATOM	5472	O	ATHR	X	73	−21.021	83.423	−32.730	0.60	36.94		O
ATOM	5473	CB	ATHR	X	73	−19.528	85.662	−34.285	0.60	37.26		C
ATOM	5474	OG1	ATHR	X	73	−19.317	84.403	−34.929	0.60	39.56		O
ATOM	5475	CG2	ATHR	X	73	−18.350	86.575	−34.575	0.60	38.40		C
ATOM	5476	N	BTHR	X	73	−18.549	84.710	−32.211	0.40	34.91		N
ATOM	5477	CA	BTHR	X	73	−19.684	85.400	−32.812	0.40	36.39		C
ATOM	5478	C	BTHR	X	73	−20.970	84.636	−32.529	0.40	38.11		C
ATOM	5479	O	BTHR	X	73	−21.026	83.413	−32.708	0.40	36.77		O
ATOM	5480	CB	BTHR	X	73	−19.509	85.557	−34.327	0.40	37.24		C
ATOM	5481	OG1	BTHR	X	73	−18.230	86.138	−34.608	0.40	37.63		O
ATOM	5482	CG2	BTHR	X	73	−20.620	86.434	−34.910	0.40	32.90		C
ATOM	5483	N	LEU	X	74	−21.997	85.359	−32.097	1.00	35.38		N
ATOM	5484	CA	LEU	X	74	−23.326	84.804	−31.943	1.00	34.79		C
ATOM	5485	C	LEU	X	74	−24.147	85.205	−33.156	1.00	36.97		C
ATOM	5486	O	LEU	X	74	−24.156	86.379	−33.545	1.00	33.92		O
ATOM	5487	CB	LEU	X	74	−23.986	85.314	−30.665	1.00	32.61		C
ATOM	5488	CG	LEU	X	74	−25.507	85.206	−30.626	1.00	31.72		C
ATOM	5489	CD1	LEU	X	74	−25.882	83.725	−30.473	1.00	30.32		C
ATOM	5490	CD2	LEU	X	74	−26.036	86.026	−29.454	1.00	27.99		C
ATOM	5491	N	GLY	X	75	−24.840	84.247	−33.745	1.00	36.52		N
ATOM	5492	CA	GLY	X	75	−25.703	84.512	−34.884	1.00	34.24		C
ATOM	5493	C	GLY	X	75	−27.148	84.242	−34.527	1.00	37.87		C
ATOM	5494	O	GLY	X	75	−27.451	83.245	−33.871	1.00	37.63		O
ATOM	5495	N	ILE	X	76	−28.035	85.141	−34.957	1.00	39.75		N
ATOM	5496	CA	ILE	X	76	−29.479	84.985	−34.802	1.00	41.67		C
ATOM	5497	C	ILE	X	76	−30.121	85.182	−36.168	1.00	42.37		C
ATOM	5498	O	ILE	X	76	−30.094	86.290	−36.715	1.00	44.35		O
ATOM	5499	CB	ILE	X	76	−30.078	85.974	−33.790	1.00	40.33		C
ATOM	5500	CG1	ILE	X	76	−29.186	86.075	−32.552	1.00	41.66		C
ATOM	5501	CG2	ILE	X	76	−31.481	85.526	−33.397	1.00	35.42		C
ATOM	5502	CD1	ILE	X	76	−29.726	86.959	−31.465	1.00	37.72		C
ATOM	5503	N	THR	X	77	−30.686	84.119	−36.725	1.00	43.91		N
ATOM	5504	CA	THR	X	77	−31.472	84.236	−37.948	1.00	48.21		C
ATOM	5505	C	THR	X	77	−32.958	84.232	−37.615	1.00	43.41		C
ATOM	5506	O	THR	X	77	−33.376	83.754	−36.561	1.00	53.87		O
ATOM	5507	CB	THR	X	77	−31.176	83.090	−38.915	1.00	48.60		C
ATOM	5508	OG1	THR	X	77	−31.675	81.879	−38.346	1.00	50.81		O
ATOM	5509	CG2	THR	X	77	−29.695	82.947	−39.136	1.00	39.95		C
ATOM	5510	N	GLY	X	78	−33.757	84.758	−38.536	1.00	46.47		N
ATOM	5511	CA	GLY	X	78	−35.202	84.734	−38.389	1.00	39.22		C
ATOM	5512	C	GLY	X	78	−35.720	85.391	−37.128	1.00	45.27		C
ATOM	5513	O	GLY	X	78	−36.522	84.791	−36.407	1.00	43.17		O
ATOM	5514	N	LEU	X	79	−35.270	86.624	−36.870	1.00	46.54		N
ATOM	5515	CA	LEU	X	79	−35.555	87.331	−35.624	1.00	38.18		C
ATOM	5516	C	LEU	X	79	−37.039	87.325	−35.285	1.00	35.99		C
ATOM	5517	O	LEU	X	79	−37.888	87.609	−36.131	1.00	36.59		O
ATOM	5518	CB	LEU	X	79	−35.059	88.776	−35.730	1.00	39.04		C
ATOM	5519	CG	LEU	X	79	−33.807	89.295	−34.996	1.00	40.52		C
ATOM	5520	CD1	LEU	X	79	−33.440	88.520	−33.740	1.00	39.26		C
ATOM	5521	CD2	LEU	X	79	−32.618	89.397	−35.910	1.00	54.14		C
ATOM	5522	N	GLN	X	80	−37.345	87.044	−34.026	1.00	38.14		N
ATOM	5523	CA	GLN	X	80	−38.697	87.144	−33.497	1.00	39.98		C
ATOM	5524	C	GLN	X	80	−38.700	88.184	−32.389	1.00	41.62		C
ATOM	5525	O	GLN	X	80	−37.668	88.422	−31.753	1.00	36.20		O
ATOM	5526	CB	GLN	X	80	−39.186	85.813	−32.942	1.00	33.25		C
ATOM	5527	CG	GLN	X	80	−39.044	84.680	−33.904	1.00	43.46		C
ATOM	5528	CD	GLN	X	80	−39.580	83.358	−33.355	1.00	50.00		C
ATOM	5529	OE1	GLN	X	80	−39.521	82.335	−34.031	1.00	49.67		O
ATOM	5530	NE2	GLN	X	80	−40.101	83.378	−32.131	1.00	47.24		N
ATOM	5531	N	THR	X	81	−39.865	88.806	−32.161	1.00	42.32		N
ATOM	5532	CA	THR	X	81	−39.935	89.865	−31.159	1.00	40.35		C
ATOM	5533	C	THR	X	81	−39.450	89.373	−29.794	1.00	36.41		C
ATOM	5534	O	THR	X	81	−38.817	90.132	−29.050	1.00	35.09		O
ATOM	5535	CB	THR	X	81	−41.369	90.415	−31.067	1.00	40.85		C
ATOM	5536	OG1	THR	X	81	−42.261	89.347	−30.772	1.00	57.82		O
ATOM	5537	CG2	THR	X	81	−41.798	90.998	−32.377	1.00	43.15		C
ATOM	5538	N	GLY	X	82	−39.684	88.094	−29.474	1.00	36.68		N
ATOM	5539	CA	GLY	X	82	−39.232	87.486	−28.236	1.00	28.64		C
ATOM	5540	C	GLY	X	82	−37.724	87.287	−28.129	1.00	37.77		C
ATOM	5541	O	GLY	X	82	−37.248	86.752	−27.124	1.00	34.17		O
ATOM	5542	N	ASP	X	83	−36.959	87.652	−29.150	1.00	30.06		N
ATOM	5543	CA	ASP	X	83	−35.509	87.630	−29.043	1.00	32.84		C
ATOM	5544	C	ASP	X	83	−34.923	88.941	−28.517	1.00	34.01		C
ATOM	5545	O	ASP	X	83	−33.729	88.984	−28.208	1.00	31.84		O
ATOM	5546	CB	ASP	X	83	−34.907	87.303	−30.404	1.00	31.73		C
ATOM	5547	CG	ASP	X	83	−35.427	85.990	−30.952	1.00	41.54		C
ATOM	5548	OD1	ASP	X	83	−35.746	85.088	−30.133	1.00	36.80		O
ATOM	5549	OD2	ASP	X	83	−35.522	85.868	−32.194	1.00	42.52		O1−
ATOM	5550	N	GLU	X	84	−35.724	90.002	−28.424	1.00	31.24		N
ATOM	5551	CA	GLU	X	84	−35.262	91.272	−27.871	1.00	37.59		C
ATOM	5552	C	GLU	X	84	−34.719	91.031	−26.459	1.00	32.26		C
ATOM	5553	O	GLU	X	84	−35.402	90.452	−25.609	1.00	35.56		O
ATOM	5554	CB	GLU	X	84	−36.416	92.283	−27.890	1.00	30.20		C
ATOM	5555	CG	GLU	X	84	−36.070	93.629	−27.345	1.00	45.30		C
ATOM	5556	CD	GLU	X	84	−36.947	94.775	−27.890	1.00	45.92		C
ATOM	5557	OE1	GLU	X	84	−37.343	95.625	−27.064	1.00	55.26		O
ATOM	5558	OE2	GLU	X	84	−37.238	94.832	−29.112	1.00	39.84		O1−
ATOM	5559	N	ALA	X	85	−33.455	91.385	−26.241	1.00	33.55		N
ATOM	5560	CA	ALA	X	85	−32.741	90.944	−25.047	1.00	30.96		C
ATOM	5561	C	ALA	X	85	−31.361	91.575	−25.034	1.00	28.54		C
ATOM	5562	O	ALA	X	85	−30.916	92.168	−26.021	1.00	32.81		O
ATOM	5563	CB	ALA	X	85	−32.594	89.409	−24.997	1.00	30.64		C
ATOM	5564	N	ASP	X	86	−30.680	91.413	−23.903	1.00	29.41		N
ATOM	5565	CA	ASP	X	86	−29.249	91.647	−23.793	1.00	31.96		C
ATOM	5566	C	ASP	X	86	−28.504	90.322	−23.884	1.00	32.23		C
ATOM	5567	O	ASP	X	86	−28.925	89.318	−23.303	1.00	33.09		O
ATOM	5568	CB	ASP	X	86	−28.907	92.357	−22.482	1.00	33.01		C
ATOM	5569	CG	ASP	X	86	−29.599	93.708	−22.367	1.00	39.16		C
ATOM	5570	OD1	ASP	X	86	−29.651	94.437	−23.368	1.00	40.13		O
ATOM	5571	OD2	ASP	X	86	−30.101	94.037	−21.280	1.00	48.35		O1−
ATOM	5572	N	TYR	X	87	−27.386	90.329	−24.599	1.00	31.45		N
ATOM	5573	CA	TYR	X	87	−26.601	89.129	−24.842	1.00	28.71		C
ATOM	5574	C	TYR	X	87	−25.182	89.374	−24.358	1.00	32.26		C
ATOM	5575	O	TYR	X	87	−24.609	90.435	−24.628	1.00	31.02		O
ATOM	5576	CB	TYR	X	87	−26.621	88.762	−26.326	1.00	26.11		C
ATOM	5577	CG	TYR	X	87	−28.002	88.352	−26.816	1.00	30.12		C
ATOM	5578	CD1	TYR	X	87	−28.925	89.305	−27.224	1.00	29.60		C
ATOM	5579	CD2	TYR	X	87	−28.378	87.014	−26.863	1.00	28.20		C
ATOM	5580	CE1	TYR	X	87	−30.188	88.932	−27.678	1.00	34.26		C
ATOM	5581	CE2	TYR	X	87	−29.626	86.630	−27.320	1.00	32.08		C
ATOM	5582	CZ	TYR	X	87	−30.527	87.596	−27.726	1.00	34.03		C
ATOM	5583	OH	TYR	X	87	−31.777	87.223	−28.150	1.00	31.35		O
ATOM	5584	N	TYR	X	88	−24.632	88.394	−23.642	1.00	29.11		N
ATOM	5585	CA	TYR	X	88	−23.311	88.458	−23.036	1.00	28.65		C
ATOM	5586	C	TYR	X	88	−22.534	87.201	−23.398	1.00	32.64		C
ATOM	5587	O	TYR	X	88	−23.054	86.084	−23.241	1.00	32.58		O
ATOM	5588	CB	TYR	X	88	−23.408	88.547	−21.508	1.00	27.95		C
ATOM	5589	CG	TYR	X	88	−24.118	89.757	−20.959	1.00	30.42		C
ATOM	5590	CD1	TYR	X	88	−25.501	89.759	−20.792	1.00	28.19		C
ATOM	5591	CD2	TYR	X	88	−23.401	90.890	−20.574	1.00	31.06		C
ATOM	5592	CE1	TYR	X	88	−26.162	90.867	−20.275	1.00	27.13		C
ATOM	5593	CE2	TYR	X	88	−24.041	92.005	−20.067	1.00	32.77		C
ATOM	5594	CZ	TYR	X	88	−25.424	91.989	−19.920	1.00	36.54		C
ATOM	5595	OH	TYR	X	88	−26.055	93.090	−19.405	1.00	30.95		O
ATOM	5596	N	CYS	X	89	−21.287	87.372	−23.833	1.00	28.04		N
ATOM	5597	CA	CYS	X	89	−20.334	86.269	−23.902	1.00	28.74		C
ATOM	5598	C	CYS	X	89	−19.528	86.212	−22.607	1.00	32.37		C
ATOM	5599	O	CYS	X	89	−19.378	87.212	−21.902	1.00	35.41		O
ATOM	5600	CB	CYS	X	89	−19.378	86.436	−25.082	1.00	33.37		C
ATOM	5601	SG	CYS	X	89	−18.463	88.060	−25.073	1.00	43.75		S
ATOM	5602	N	GLY	X	90	−19.005	85.032	−22.303	1.00	32.61		N
ATOM	5603	CA	GLY	X	90	−18.237	84.821	−21.083	1.00	31.53		C
ATOM	5604	C	GLY	X	90	−17.235	83.695	−21.244	1.00	33.08		C
ATOM	5605	O	GLY	X	90	−17.445	82.767	−22.030	1.00	35.81		O
ATOM	5606	N	THR	X	91	−16.107	83.816	−20.531	1.00	25.99		N
ATOM	5607	CA	THR	X	91	−15.089	82.778	−20.428	1.00	29.82		C
ATOM	5608	C	THR	X	91	−14.309	82.951	−19.143	1.00	31.29		C
ATOM	5609	O	THR	X	91	−14.533	83.878	−18.365	1.00	34.63		O
ATOM	5610	CB	THR	X	91	−13.968	82.816	−21.479	1.00	38.46		C
ATOM	5611	OG1	THR	X	91	−14.245	83.717	−22.547	1.00	45.88		O
ATOM	5612	CG2	THR	X	91	−13.680	81.476	−21.973	1.00	27.98		C
ATOM	5613	N	TRP	X	92	−13.306	82.097	−19.016	1.00	27.25		N
ATOM	5614	CA	TRP	X	92	−12.219	82.230	−18.077	1.00	29.16		C
ATOM	5615	C	TRP	X	92	−11.070	83.003	−18.714	1.00	32.78		C
ATOM	5616	O	TRP	X	92	−10.800	82.873	−19.912	1.00	30.90		O
ATOM	5617	CB	TRP	X	92	−11.757	80.836	−17.670	1.00	27.36		C
ATOM	5618	CG	TRP	X	92	−10.715	80.810	−16.612	1.00	35.33		C
ATOM	5619	CD1	TRP	X	92	−9.392	80.455	−16.757	1.00	34.95		C
ATOM	5620	CD2	TRP	X	92	−10.900	81.116	−15.227	1.00	34.91		C
ATOM	5621	NE1	TRP	X	92	−8.751	80.510	−15.535	1.00	33.88		N
ATOM	5622	CE2	TRP	X	92	−9.647	80.927	−14.584	1.00	35.68		C
ATOM	5623	CE3	TRP	X	92	−11.998	81.527	−14.465	1.00	29.27		C
ATOM	5624	CZ2	TRP	X	92	−9.471	81.141	−13.221	1.00	32.90		C
ATOM	5625	CZ3	TRP	X	92	−11.821	81.740	−13.107	1.00	30.95		C
ATOM	5626	CH2	TRP	X	92	−10.571	81.542	−12.498	1.00	36.18		C
ATOM	5627	N	ASP	X	93	−10.389	83.802	−17.915	1.00	34.71		N
ATOM	5628	CA	ASP	X	93	−9.143	84.431	−18.340	1.00	35.49		C
ATOM	5629	C	ASP	X	93	−8.004	83.809	−17.537	1.00	35.61		C
ATOM	5630	O	ASP	X	93	−7.912	84.013	−16.322	1.00	38.60		O
ATOM	5631	CB	ASP	X	93	−9.192	85.940	−18.151	1.00	30.03		C
ATOM	5632	CG	ASP	X	93	−8.045	86.639	−18.857	1.00	39.44		C
ATOM	5633	OD1	ASP	X	93	−6.878	86.282	−18.573	1.00	37.16		O1−
ATOM	5634	OD2	ASP	X	93	−8.317	87.531	−19.701	1.00	32.36		O
ATOM	5635	N	SER	X	94	−7.137	83.061	−18.223	1.00	33.93		N
ATOM	5636	CA	SER	X	94	−6.072	82.302	−17.571	1.00	37.23		C
ATOM	5637	C	SER	X	94	−5.010	83.199	−16.958	1.00	43.27		C
ATOM	5638	O	SER	X	94	−4.321	82.779	−16.024	1.00	47.17		O
ATOM	5639	CB	SER	X	94	−5.415	81.337	−18.557	1.00	35.59		C
ATOM	5640	OG	SER	X	94	−6.349	80.369	−19.056	1.00	47.61		O
ATOM	5641	N	SER	X	95	−4.851	84.415	−17.456	1.00	36.82		N
ATOM	5642	CA	SER	X	95	−3.842	85.284	−16.877	1.00	40.13		C
ATOM	5643	C	SER	X	95	−4.390	86.199	−15.784	1.00	43.12		C
ATOM	5644	O	SER	X	95	−3.652	86.546	−14.858	1.00	44.13		O
ATOM	5645	CB	SER	X	95	−3.177	86.104	−17.979	1.00	38.64		C
ATOM	5646	OG	SER	X	95	−3.953	87.241	−18.283	1.00	52.16		O
ATOM	5647	N	LEU	X	96	−5.653	86.623	−15.858	1.00	49.30		N
ATOM	5648	CA	LEU	X	96	−6.260	87.359	−14.750	1.00	41.53		C
ATOM	5649	C	LEU	X	96	−6.849	86.436	−13.685	1.00	36.33		C
ATOM	5650	O	LEU	X	96	−7.332	86.925	−12.663	1.00	40.59		O
ATOM	5651	CB	LEU	X	96	−7.345	88.299	−15.263	1.00	31.21		C
ATOM	5652	CG	LEU	X	96	−6.975	89.345	−16.315	1.00	35.69		C
ATOM	5653	CD1	LEU	X	96	−8.257	89.972	−16.878	1.00	32.73		C
ATOM	5654	CD2	LEU	X	96	−6.072	90.443	−15.740	1.00	33.32		C
ATOM	5655	N	ASN	X	97	−6.819	85.128	−13.908	1.00	33.69		N
ATOM	5656	CA	ASN	X	97	−7.457	84.113	−13.054	1.00	40.52		C
ATOM	5657	C	ASN	X	97	−8.862	84.515	−12.585	1.00	37.02		C
ATOM	5658	O	ASN	X	97	−9.170	84.528	−11.394	1.00	38.37		O
ATOM	5659	CB	ASN	X	97	−6.566	83.762	−11.863	1.00	40.15		C
ATOM	5660	CG	ASN	X	97	−5.793	82.485	−12.103	1.00	56.68		C
ATOM	5661	OD1	ASN	X	97	−6.057	81.431	−11.474	1.00	58.82		O
ATOM	5662	ND2	ASN	X	97	−4.866	82.541	−13.069	1.00	45.20		N
ATOM	5663	N	THR	X	98	−9.736	84.807	−13.551	1.00	33.40		N
ATOM	5664	CA	THR	X	98	−11.086	85.225	−13.198	1.00	36.45		C
ATOM	5665	C	THR	X	98	−12.042	84.934	−14.345	1.00	31.02		C
ATOM	5666	O	THR	X	98	−11.637	84.809	−15.497	1.00	29.12		O
ATOM	5667	CB	THR	X	98	−11.138	86.713	−12.830	1.00	32.72		C
ATOM	5668	OG1	THR	X	98	−12.455	87.038	−12.382	1.00	37.61		O
ATOM	5669	CG2	THR	X	98	−10.840	87.569	−14.031	1.00	32.00		C
ATOM	5670	N	VAL	X	99	−13.326	84.815	−14.005	1.00	30.06		N
ATOM	5671	CA	VAL	X	99	−14.358	84.769	−15.027	1.00	24.45		C
ATOM	5672	C	VAL	X	99	−14.563	86.160	−15.611	1.00	29.75		C
ATOM	5673	O	VAL	X	99	−14.620	87.174	−14.897	1.00	26.93		O
ATOM	5674	CB	VAL	X	99	−15.680	84.233	−14.460	1.00	28.00		C
ATOM	5675	CG1	VAL	X	99	−16.739	84.291	−15.532	1.00	26.99		C
ATOM	5676	CG2	VAL	X	99	−15.525	82.801	−13.869	1.00	29.57		C
ATOM	5677	N	VAL	X	100	−14.775	86.208	−16.906	1.00	29.21		N
ATOM	5678	CA	VAL	X	100	−14.748	87.464	−17.623	1.00	28.67		C
ATOM	5679	C	VAL	X	100	−15.948	87.512	−18.574	1.00	32.26		C
ATOM	5680	O	VAL	X	100	−16.225	86.546	−19.296	1.00	33.30		O
ATOM	5681	CB	VAL	X	100	−13.355	87.559	−18.285	1.00	34.89		C
ATOM	5682	CG1	VAL	X	100	−13.294	87.188	−19.773	1.00	28.07		C
ATOM	5683	CG2	VAL	X	100	−12.657	88.799	−17.889	1.00	30.67		C
ATOM	5684	N	PHE	X	101	−16.709	88.599	−18.512	1.00	29.76		N
ATOM	5685	CA	PHE	X	101	−17.876	88.803	−19.365	1.00	37.29		C
ATOM	5686	C	PHE	X	101	−17.634	89.939	−20.348	1.00	33.64		C
ATOM	5687	O	PHE	X	101	−16.940	90.913	−20.039	1.00	36.04		O
ATOM	5688	CB	PHE	X	101	−19.138	89.186	−18.567	1.00	33.79		C
ATOM	5689	CG	PHE	X	101	−19.780	88.069	−17.808	1.00	32.73		C
ATOM	5690	CD1	PHE	X	101	−20.482	87.064	−18.464	1.00	38.68		C
ATOM	5691	CD2	PHE	X	101	−19.729	88.057	−16.407	1.00	31.51		C
ATOM	5692	CE1	PHE	X	101	−21.114	86.044	−17.743	1.00	34.99		C
ATOM	5693	CE2	PHE	X	101	−20.345	87.044	−15.674	1.00	28.97		C
ATOM	5694	CZ	PHE	X	101	−21.040	86.028	−16.349	1.00	30.18		C
ATOM	5695	N	GLY	X	102	−18.283	89.846	−21.507	1.00	31.53		N
ATOM	5696	CA	GLY	X	102	−18.420	91.004	−22.354	1.00	30.93		C
ATOM	5697	C	GLY	X	102	−19.343	92.039	−21.708	1.00	38.01		C
ATOM	5698	O	GLY	X	102	−20.047	91.780	−20.724	1.00	32.78		O
ATOM	5699	N	GLY	X	103	−19.311	93.246	−22.272	1.00	29.12		N
ATOM	5700	CA	GLY	X	103	−20.117	94.353	−21.794	1.00	29.37		C
ATOM	5701	C	GLY	X	103	−21.583	94.244	−22.120	1.00	33.08		C
ATOM	5702	O	GLY	X	103	−22.376	95.015	−21.576	1.00	35.44		O
ATOM	5703	N	GLY	X	104	−21.964	93.300	−22.974	1.00	34.27		N
ATOM	5704	CA	GLY	X	104	−23.358	93.149	−23.326	1.00	29.50		C
ATOM	5705	C	GLY	X	104	−23.731	93.836	−24.619	1.00	29.53		C
ATOM	5706	O	GLY	X	104	−23.197	94.891	−24.951	1.00	32.35		O
ATOM	5707	N	THR	X	105	−24.636	93.220	−25.369	1.00	34.88		N
ATOM	5708	CA	THR	X	105	−25.182	93.780	−26.591	1.00	32.20		C
ATOM	5709	C	THR	X	105	−26.689	93.826	−26.424	1.00	34.52		C
ATOM	5710	O	THR	X	105	−27.326	92.787	−26.221	1.00	32.97		O
ATOM	5711	CB	THR	X	105	−24.791	92.943	−27.812	1.00	30.26		C
ATOM	5712	OG1	THR	X	105	−23.367	92.949	−27.935	1.00	36.62		O
ATOM	5713	CG2	THR	X	105	−25.397	93.520	−29.084	1.00	27.38		C
ATOM	5714	N	LYS	X	106	−27.246	95.027	−26.490	1.00	33.22		N
ATOM	5715	CA	LYS	X	106	−28.686	95.209	−26.472	1.00	35.13		C
ATOM	5716	C	LYS	X	106	−29.210	94.955	−27.877	1.00	32.47		C
ATOM	5717	O	LYS	X	106	−28.824	95.647	−28.822	1.00	37.14		O
ATOM	5718	CB	LYS	X	106	−29.035	96.619	−26.001	1.00	33.00		C
ATOM	5719	CG	LYS	X	106	−30.515	96.974	−26.093	1.00	40.50		C
ATOM	5720	CD	LYS	X	106	−30.760	98.406	−25.536	1.00	50.00		C
ATOM	5721	CE	LYS	X	106	−32.202	98.919	−25.776	1.00	54.95		C
ATOM	5722	NZ	LYS	X	106	−33.307	98.040	−25.259	1.00	53.87		N1+
ATOM	5723	N	LEU	X	107	−30.039	93.941	−28.022	1.00	31.69		N
ATOM	5724	CA	LEU	X	107	−30.702	93.641	−29.282	1.00	35.95		C
ATOM	5725	C	LEU	X	107	−32.109	94.195	−29.217	1.00	34.06		C
ATOM	5726	O	LEU	X	107	−32.890	93.810	−28.335	1.00	36.06		O
ATOM	5727	CB	LEU	X	107	−30.764	92.135	−29.542	1.00	29.30		C
ATOM	5728	CG	LEU	X	107	−31.101	91.566	−30.925	1.00	36.45		C
ATOM	5729	CD1	LEU	X	107	−31.582	90.117	−30.792	1.00	47.08		C
ATOM	5730	CD2	LEU	X	107	−32.108	92.310	−31.732	1.00	35.75		C
ATOM	5731	N	ATHR	X	108	−32.447	95.068	−30.150	0.50	29.34		N
ATOM	5732	CA	ATHR	X	108	−33.819	95.519	−30.281	0.50	34.47		C
ATOM	5733	C	ATHR	X	108	−34.372	94.993	−31.598	0.50	34.43		C
ATOM	5734	O	ATHR	X	108	−33.730	95.114	−32.645	0.50	33.84		O
ATOM	5735	CB	ATHR	X	108	−33.929	97.050	−30.167	0.50	35.43		C
ATOM	5736	OG1	ATHR	X	108	−34.721	97.575	−31.244	0.50	39.77		O
ATOM	5737	CG2	ATHR	X	108	−32.553	97.713	−30.114	0.50	36.64		C
ATOM	5738	N	BTHR	X	108	−32.435	95.083	−30.149	0.50	28.73		N
ATOM	5739	CA	BTHR	X	108	−33.795	95.559	−30.334	0.50	34.59		C
ATOM	5740	C	BTHR	X	108	−34.344	94.934	−31.610	0.50	34.22		C
ATOM	5741	O	BTHR	X	108	−33.682	94.959	−32.651	0.50	33.77		O
ATOM	5742	CB	BTHR	X	108	−33.864	97.095	−30.407	0.50	35.40		C
ATOM	5743	OG1	BTHR	X	108	−33.311	97.671	−29.217	0.50	29.14		O
ATOM	5744	CG2	BTHR	X	108	−35.332	97.571	−30.561	0.50	36.81		C
ATOM	5745	N	VAL	X	109	−35.533	94.354	−31.521	1.00	34.56		N
ATOM	5746	CA	VAL	X	109	−36.242	93.847	−32.687	1.00	37.76		C
ATOM	5747	C	VAL	X	109	−37.211	94.947	−33.124	1.00	37.56		C
ATOM	5748	O	VAL	X	109	−38.195	95.233	−32.435	1.00	39.51		O
ATOM	5749	CB	VAL	X	109	−36.957	92.526	−32.370	1.00	36.89		C
ATOM	5750	CG1	VAL	X	109	−37.657	91.986	−33.592	1.00	37.00		C
ATOM	5751	CG2	VAL	X	109	−35.944	91.498	−31.854	1.00	35.12		C
ATOM	5752	N	LEU	X	110	−36.903	95.596	−34.249	1.00	40.19		N
ATOM	5753	CA	LEU	X	110	−37.598	96.804	−34.693	1.00	37.97		C
ATOM	5754	C	LEU	X	110	−39.089	96.596	−34.915	1.00	42.37		C
ATOM	5755	O	LEU	X	110	−39.492	95.862	−35.816	1.00	42.06		O
ATOM	5756	CB	LEU	X	110	−36.952	97.330	−35.974	1.00	32.89		C
ATOM	5757	CG	LEU	X	110	−35.483	97.738	−35.777	1.00	44.78		C
ATOM	5758	CD1	LEU	X	110	−34.740	97.954	−37.095	1.00	36.15		C
ATOM	5759	CD2	LEU	X	110	−35.451	98.999	−34.936	1.00	37.61		C
ATOM	5760	N	SER	X	111	−39.923	97.222	−34.090	1.00	44.41		N
ATOM	5761	CA	SER	X	111	−41.366	97.119	−34.268	1.00	50.21		C
ATOM	5762	C	SER	X	111	−42.007	98.460	−34.601	1.00	49.69		C
ATOM	5763	O	SER	X	111	−43.235	98.560	−34.605	1.00	52.76		O
ATOM	5764	CB	SER	X	111	−42.017	96.500	−33.028	1.00	44.40		C
ATOM	5765	OG	SER	X	111	−41.726	97.270	−31.878	1.00	60.88		O
ATOM	5766	N	GLN	X	112	−41.211	99.487	−34.878	1.00	47.15		N
ATOM	5767	CA	GLN	X	112	−41.707	100.757	−35.390	1.00	48.33		C
ATOM	5768	C	GLN	X	112	−40.538	101.473	−36.048	1.00	46.20		C
ATOM	5769	O	GLN	X	112	−39.389	101.022	−35.937	1.00	50.86		O
ATOM	5770	CB	GLN	X	112	−42.328	101.613	−34.268	1.00	45.44		C
ATOM	5771	CG	GLN	X	112	−41.332	102.017	−33.210	1.00	54.29		C
ATOM	5772	CD	GLN	X	112	−41.921	102.957	−32.174	1.00	55.17		C
ATOM	5773	OE1	GLN	X	112	−42.268	102.535	−31.064	1.00	50.12		O
ATOM	5774	NE2	GLN	X	112	−42.016	104.247	−32.523	1.00	51.29		N
ATOM	5775	N	PRO	X	113	−40.791	102.573	−36.760	1.00	47.86	GZ00	N
ATOM	5776	CA	PRO	X	113	−39.684	103.305	−37.392	1.00	44.33	GZ00	C
ATOM	5777	C	PRO	X	113	−38.722	103.861	−36.360	1.00	47.98	GZ00	C
ATOM	5778	O	PRO	X	113	−39.099	104.165	−35.229	1.00	51.31	GZ00	O
ATOM	5779	CB	PRO	X	113	−40.386	104.439	−38.148	1.00	44.96	GZ00	C
ATOM	5780	CG	PRO	X	113	−41.754	103.943	−38.377	1.00	46.92	GZ00	C
ATOM	5781	CD	PRO	X	113	−42.098	103.123	−37.162	1.00	47.64	GZ00	C
ATOM	5782	N	LYS	X	114	−37.464	104.002	−36.764	1.00	48.55	GZ00	N
ATOM	5783	CA	LYS	X	114	−36.492	104.609	−35.876	1.00	42.68	GZ00	C
ATOM	5784	C	LYS	X	114	−36.864	106.065	−35.628	1.00	49.83	GZ00	C
ATOM	5785	O	LYS	X	114	−37.429	106.739	−36.491	1.00	52.51	GZ00	O
ATOM	5786	CB	LYS	X	114	−35.082	104.485	−36.457	1.00	45.63	GZ00	C
ATOM	5787	CG	LYS	X	114	−34.596	103.034	−36.553	1.00	50.09	GZ00	C
ATOM	5788	CD	LYS	X	114	−33.151	102.950	−37.039	1.00	58.16	GZ00	C
ATOM	5789	CE	LYS	X	114	−32.468	101.608	−36.704	1.00	40.47	GZ00	C
ATOM	5790	NZ	LYS	X	114	−30.975	101.802	−36.780	1.00	37.72	GZ00	N1+
ATOM	5791	N	ALA	X	115	−36.559	106.540	−34.424	1.00	48.82	GZ00	N
ATOM	5792	CA	ALA	X	115	−36.951	107.875	−33.987	1.00	42.61	GZ00	C
ATOM	5793	C	ALA	X	115	−35.771	108.535	−33.298	1.00	43.87	GZ00	C
ATOM	5794	O	ALA	X	115	−35.255	108.014	−32.302	1.00	42.55	GZ00	O
ATOM	5795	CB	ALA	X	115	−38.151	107.809	−33.040	1.00	37.00	GZ00	C
ATOM	5796	N	ALA	X	116	−35.349	109.676	−33.825	1.00	42.05	GZ00	N
ATOM	5797	CA	ALA	X	116	−34.281	110.428	−33.189	1.00	51.37	GZ00	C
ATOM	5798	C	ALA	X	116	−34.776	111.034	−31.871	1.00	46.85	GZ00	C
ATOM	5799	O	ALA	X	116	−35.976	111.217	−31.674	1.00	42.99	GZ00	O
ATOM	5800	CB	ALA	X	116	−33.779	111.525	−34.121	1.00	48.36	GZ00	C
ATOM	5801	N	PRO	X	117	−33.881	111.279	−30.922	1.00	47.49	GZ00	N
ATOM	5802	CA	PRO	X	117	−34.320	111.846	−29.642	1.00	49.41	GZ00	C
ATOM	5803	C	PRO	X	117	−34.616	113.337	−29.751	1.00	53.03	GZ00	C
ATOM	5804	O	PRO	X	117	−33.903	114.088	−30.426	1.00	49.88	GZ00	O
ATOM	5805	CB	PRO	X	117	−33.120	111.582	−28.721	1.00	48.21	GZ00	C
ATOM	5806	CG	PRO	X	117	−31.929	111.617	−29.651	1.00	40.15	GZ00	C
ATOM	5807	CD	PRO	X	117	−32.431	110.999	−30.939	1.00	47.80	GZ00	C
ATOM	5808	N	SER	X	118	−35.660	113.776	−29.048	1.00	43.61	GZ00	N
ATOM	5809	CA	SER	X	118	−35.846	115.206	−28.812	1.00	49.92	GZ00	C
ATOM	5810	C	SER	X	118	−35.152	115.555	−27.504	1.00	43.16	GZ00	C
ATOM	5811	O	SER	X	118	−35.266	114.824	−26.515	1.00	50.92	GZ00	O
ATOM	5812	CB	SER	X	118	−37.325	115.608	−28.770	1.00	47.75	GZ00	C
ATOM	5813	OG	SER	X	118	−37.961	115.002	−27.671	1.00	58.79	GZ00	O
ATOM	5814	N	VAL	X	119	−34.377	116.627	−27.528	1.00	41.52	GZ00	N
ATOM	5815	CA	VAL	X	119	−33.512	117.022	−26.426	1.00	44.89	GZ00	C
ATOM	5816	C	VAL	X	119	−33.886	118.439	−26.021	1.00	52.97	GZ00	C
ATOM	5817	O	VAL	X	119	−33.914	119.338	−26.869	1.00	55.14	GZ00	O
ATOM	5818	CB	VAL	X	119	−32.030	116.957	−26.837	1.00	42.97	GZ00	C
ATOM	5819	CG1	VAL	X	119	−31.122	117.319	−25.668	1.00	42.13	GZ00	C
ATOM	5820	CG2	VAL	X	119	−31.694	115.590	−27.416	1.00	46.14	GZ00	C
ATOM	5821	N	THR	X	120	−34.183	118.644	−24.741	1.00	53.84	GZ00	N
ATOM	5822	CA	THR	X	120	−34.297	119.997	−24.223	1.00	52.90	GZ00	C
ATOM	5823	C	THR	X	120	−33.396	120.136	−23.000	1.00	49.02	GZ00	C
ATOM	5824	O	THR	X	120	−33.365	119.257	−22.135	1.00	44.38	GZ00	O
ATOM	5825	CB	THR	X	120	−35.779	120.402	−23.935	1.00	46.21	GZ00	C
ATOM	5826	OG1	THR	X	120	−35.982	120.611	−22.536	1.00	53.27	GZ00	O
ATOM	5827	CG2	THR	X	120	−36.767	119.365	−24.468	1.00	51.58	GZ00	C
ATOM	5828	N	LEU	X	121	−32.652	121.246	−22.960	1.00	49.59	GZ00	N
ATOM	5829	CA	LEU	X	121	−31.580	121.506	−22.006	1.00	46.69	GZ00	C
ATOM	5830	C	LEU	X	121	−31.926	122.718	−21.147	1.00	49.22	GZ00	C
ATOM	5831	O	LEU	X	121	−32.183	123.802	−21.676	1.00	57.48	GZ00	O
ATOM	5832	CB	LEU	X	121	−30.282	121.762	−22.756	1.00	42.85	GZ00	C
ATOM	5833	CG	LEU	X	121	−28.925	121.456	−22.159	1.00	49.09	GZ00	C
ATOM	5834	CD1	LEU	X	121	−27.908	122.373	−22.827	1.00	42.63	GZ00	C
ATOM	5835	CD2	LEU	X	121	−28.888	121.557	−20.653	1.00	50.57	GZ00	C
ATOM	5836	N	PHE	X	122	−31.952	122.534	−19.834	1.00	51.49	GZ00	N
ATOM	5837	CA	PHE	X	122	−32.197	123.630	−18.917	1.00	48.21	GZ00	C
ATOM	5838	C	PHE	X	122	−30.914	124.009	−18.215	1.00	52.42	GZ00	C
ATOM	5839	O	PHE	X	122	−30.201	123.122	−17.727	1.00	47.78	GZ00	O
ATOM	5840	CB	PHE	X	122	−33.245	123.263	−17.872	1.00	44.54	GZ00	C
ATOM	5841	CG	PHE	X	122	−34.637	123.136	−18.419	1.00	55.06	GZ00	C
ATOM	5842	CD1	PHE	X	122	−35.407	124.269	−18.664	1.00	49.10	GZ00	C
ATOM	5843	CD2	PHE	X	122	−35.197	121.885	−18.648	1.00	51.91	GZ00	C
ATOM	5844	CE1	PHE	X	122	−36.697	124.155	−19.151	1.00	52.05	GZ00	C
ATOM	5845	CE2	PHE	X	122	−36.487	121.766	−19.133	1.00	44.48	GZ00	C
ATOM	5846	CZ	PHE	X	122	−37.238	122.899	−19.385	1.00	49.83	GZ00	C
ATOM	5847	N	PRO	X	123	−30.613	125.302	−18.116	1.00	55.21	GZ00	N
ATOM	5848	CA	PRO	X	123	−29.470	125.760	−17.316	1.00	49.75	GZ00	C
ATOM	5849	C	PRO	X	123	−29.834	125.768	−15.844	1.00	49.06	GZ00	C
ATOM	5850	O	PRO	X	123	−31.016	125.607	−15.493	1.00	43.82	GZ00	O
ATOM	5851	CB	PRO	X	123	−29.233	127.183	−17.842	1.00	55.50	GZ00	C
ATOM	5852	CG	PRO	X	123	−30.612	127.648	−18.178	1.00	51.07	GZ00	C
ATOM	5853	CD	PRO	X	123	−31.353	126.426	−18.710	1.00	47.80	GZ00	C
ATOM	5854	N	PRO	X	124	−28.866	125.964	−14.950	1.00	48.22	GZ00	N
ATOM	5855	CA	PRO	X	124	−29.212	126.031	−13.526	1.00	50.20	GZ00	C
ATOM	5856	C	PRO	X	124	−30.040	127.272	−13.245	1.00	49.48	GZ00	C
ATOM	5857	O	PRO	X	124	−29.819	128.331	−13.832	1.00	60.15	GZ00	O
ATOM	5858	CB	PRO	X	124	−27.850	126.075	−12.822	1.00	45.39	GZ00	C
ATOM	5859	CG	PRO	X	124	−26.917	126.606	−13.838	1.00	51.55	GZ00	C
ATOM	5860	CD	PRO	X	124	−27.423	126.159	−15.178	1.00	47.41	GZ00	C
ATOM	5861	N	SER	X	125	−31.021	127.122	−12.367	1.00	47.01	GZ00	N
ATOM	5862	CA	SER	X	125	−31.863	128.243	−11.982	1.00	52.47	GZ00	C
ATOM	5863	C	SER	X	125	−31.107	129.183	−11.033	1.00	58.92	GZ00	C
ATOM	5864	O	SER	X	125	−30.113	128.806	−10.387	1.00	46.42	GZ00	O
ATOM	5865	CB	SER	X	125	−33.156	127.749	−11.322	1.00	46.03	GZ00	C
ATOM	5866	OG	SER	X	125	−32.890	127.191	−10.049	1.00	47.81	GZ00	O
ATOM	5867	N	SER	X	126	−31.591	130.436	−10.966	1.00	57.48	GZ00	N
ATOM	5868	CA	SER	X	126	−30.955	131.426	−10.096	1.00	51.60	GZ00	C
ATOM	5869	C	SER	X	126	−31.069	131.029	−8.631	1.00	45.30	GZ00	C
ATOM	5870	O	SER	X	126	−30.103	131.177	−7.870	1.00	56.73	GZ00	O
ATOM	5871	CB	SER	X	126	−31.552	132.818	−10.327	1.00	46.73	GZ00	C
ATOM	5872	OG	SER	X	126	−32.956	132.793	−10.192	1.00	64.48	GZ00	O
ATOM	5873	N	GLU	X	127	−32.222	130.484	−8.219	1.00	49.07	GZ00	N
ATOM	5874	CA	GLU	X	127	−32.347	130.017	−6.839	1.00	53.87	GZ00	C
ATOM	5875	C	GLU	X	127	−31.302	128.962	−6.507	1.00	55.39	GZ00	C
ATOM	5876	O	GLU	X	127	−30.761	128.948	−5.394	1.00	53.30	GZ00	O
ATOM	5877	CB	GLU	X	127	−33.733	129.444	−6.558	1.00	46.74	GZ00	C
ATOM	5878	CG	GLU	X	127	−34.909	130.267	−7.005	1.00	50.20	GZ00	C
ATOM	5879	CD	GLU	X	127	−36.221	129.697	−6.458	1.00	67.37	GZ00	C
ATOM	5880	OE1	GLU	X	127	−36.163	128.878	−5.501	1.00	58.54	GZ00	O
ATOM	5881	OE2	GLU	X	127	−37.303	130.059	−6.988	1.00	72.90	GZ00	O1−
ATOM	5882	N	GLU	X	128	−30.978	128.088	−7.466	1.00	52.88	GZ00	N
ATOM	5883	CA	GLU	X	128	−30.012	127.035	−7.162	1.00	58.48	GZ00	C
ATOM	5884	C	GLU	X	128	−28.600	127.593	−7.114	1.00	54.84	GZ00	C
ATOM	5885	O	GLU	X	128	−27.778	127.141	−6.305	1.00	50.17	GZ00	O
ATOM	5886	CB	GLU	X	128	−30.100	125.882	−8.171	1.00	51.98	GZ00	C
ATOM	5887	CG	GLU	X	128	−29.266	124.683	−7.739	1.00	50.39	GZ00	C
ATOM	5888	CD	GLU	X	128	−29.022	123.641	−8.841	1.00	56.66	GZ00	C
ATOM	5889	OE1	GLU	X	128	−28.576	122.533	−8.481	1.00	51.79	GZ00	O
ATOM	5890	OE2	GLU	X	128	−29.257	123.912	−10.044	1.00	50.04	GZ00	O1−
ATOM	5891	N	LEU	X	129	−28.300	128.569	−7.971	1.00	51.67	GZ00	N
ATOM	5892	CA	LEU	X	129	−27.020	129.247	−7.835	1.00	57.61	GZ00	C
ATOM	5893	C	LEU	X	129	−26.899	129.856	−6.440	1.00	54.69	GZ00	C
ATOM	5894	O	LEU	X	129	−25.876	129.685	−5.768	1.00	56.10	GZ00	O
ATOM	5895	CB	LEU	X	129	−26.861	130.296	−8.938	1.00	51.14	GZ00	C
ATOM	5896	CG	LEU	X	129	−26.749	129.691	−10.350	1.00	59.65	GZ00	C
ATOM	5897	CD1	LEU	X	129	−26.772	130.745	−11.454	1.00	51.42	GZ00	C
ATOM	5898	CD2	LEU	X	129	−25.537	128.778	−10.502	1.00	48.62	GZ00	C
ATOM	5899	N	GLN	X	130	−27.979	130.476	−5.947	1.00	51.64	GZ00	N
ATOM	5900	CA	GLN	X	130	−27.987	131.040	−4.600	1.00	54.55	GZ00	C
ATOM	5901	C	GLN	X	130	−27.717	130.007	−3.525	1.00	57.65	GZ00	C
ATOM	5902	O	GLN	X	130	−27.308	130.384	−2.425	1.00	62.14	GZ00	O
ATOM	5903	CB	GLN	X	130	−29.325	131.707	−4.308	1.00	49.30	GZ00	C
ATOM	5904	CG	GLN	X	130	−29.494	133.013	−5.001	1.00	55.98	GZ00	C
ATOM	5905	CD	GLN	X	130	−29.020	134.140	−4.135	1.00	68.65	GZ00	C
ATOM	5906	OE1	GLN	X	130	−27.848	134.527	−4.169	1.00	64.86	GZ00	O
ATOM	5907	NE2	GLN	X	130	−29.925	134.657	−3.313	1.00	63.69	GZ00	N
ATOM	5908	N	ALA	X	131	−27.980	128.727	−3.788	1.00	58.30	GZ00	N
ATOM	5909	CA	ALA	X	131	−27.635	127.669	−2.849	1.00	53.42	GZ00	C
ATOM	5910	C	ALA	X	131	−26.223	127.155	−3.057	1.00	55.16	GZ00	C
ATOM	5911	O	ALA	X	131	−25.840	126.154	−2.444	1.00	55.67	GZ00	O
ATOM	5912	CB	ALA	X	131	−28.629	126.517	−2.951	1.00	53.39	GZ00	C
ATOM	5913	N	ASN	X	132	−25.445	127.820	−3.909	1.00	57.80	GZ00	N
ATOM	5914	CA	ASN	X	132	−24.062	127.430	−4.188	1.00	65.38	GZ00	C
ATOM	5915	C	ASN	X	132	−23.983	126.038	−4.819	1.00	64.86	GZ00	C
ATOM	5916	O	ASN	X	132	−23.125	125.221	−4.474	1.00	58.78	GZ00	O
ATOM	5917	CB	ASN	X	132	−23.198	127.502	−2.930	1.00	57.21	GZ00	C
ATOM	5918	CG	ASN	X	132	−21.742	127.673	−3.259	1.00	66.70	GZ00	C
ATOM	5919	OD1	ASN	X	132	−21.389	128.368	−4.221	1.00	68.31	GZ00	O
ATOM	5920	ND2	ASN	X	132	−20.880	127.021	−2.485	1.00	71.71	GZ00	N
ATOM	5921	N	LYS	X	133	−24.891	125.766	−5.750	1.00	63.21	GZ00	N
ATOM	5922	CA	LYS	X	133	−24.866	124.558	−6.558	1.00	55.69	GZ00	C
ATOM	5923	C	LYS	X	133	−25.304	124.950	−7.959	1.00	58.70	GZ00	C
ATOM	5924	O	LYS	X	133	−25.800	126.057	−8.195	1.00	60.57	GZ00	O
ATOM	5925	CB	LYS	X	133	−25.778	123.468	−5.978	1.00	57.74	GZ00	C
ATOM	5926	CG	LYS	X	133	−25.404	122.972	−4.574	1.00	60.29	GZ00	C
ATOM	5927	CD	LYS	X	133	−26.528	122.090	−3.989	1.00	77.16	GZ00	C
ATOM	5928	CE	LYS	X	133	−26.295	121.712	−2.516	1.00	67.68	GZ00	C
ATOM	5929	NZ	LYS	X	133	−27.578	121.494	−1.757	1.00	61.53	GZ00	N1+
ATOM	5930	N	ALA	X	134	−25.128	124.033	−8.899	1.00	57.91	GZ00	N
ATOM	5931	CA	ALA	X	134	−25.550	124.292	−10.273	1.00	57.46	GZ00	C
ATOM	5932	C	ALA	X	134	−25.676	122.951	−10.970	1.00	58.56	GZ00	C
ATOM	5933	O	ALA	X	134	−24.715	122.173	−10.980	1.00	56.94	GZ00	O
ATOM	5934	CB	ALA	X	134	−24.546	125.194	−10.994	1.00	46.64	GZ00	C
ATOM	5935	N	THR	X	135	−26.850	122.650	−11.519	1.00	55.26	GZ00	N
ATOM	5936	CA	THR	X	135	−26.986	121.434	−12.308	1.00	47.36	GZ00	C
ATOM	5937	C	THR	X	135	−27.631	121.778	−13.640	1.00	45.07	GZ00	C
ATOM	5938	O	THR	X	135	−28.602	122.540	−13.693	1.00	43.66	GZ00	O
ATOM	5939	CB	THR	X	135	−27.779	120.335	−11.579	1.00	46.59	GZ00	C
ATOM	5940	OG1	THR	X	135	−29.174	120.523	−11.787	1.00	60.99	GZ00	O
ATOM	5941	CG2	THR	X	135	−27.487	120.331	−10.088	1.00	40.51	GZ00	C
ATOM	5942	N	LEU	X	136	−27.050	121.251	−14.711	1.00	43.91	GZ00	N
ATOM	5943	CA	LEU	X	136	−27.635	121.315	−16.036	1.00	42.15	GZ00	C
ATOM	5944	C	LEU	X	136	−28.501	120.080	−16.231	1.00	50.30	GZ00	C
ATOM	5945	O	LEU	X	136	−28.140	118.976	−15.812	1.00	46.46	GZ00	O
ATOM	5946	CB	LEU	X	136	−26.544	121.383	−17.101	1.00	46.62	GZ00	C
ATOM	5947	CG	LEU	X	136	−25.574	122.574	−17.036	1.00	48.02	GZ00	C
ATOM	5948	CD1	LEU	X	136	−24.445	122.431	−18.044	1.00	53.43	GZ00	C
ATOM	5949	CD2	LEU	X	136	−26.330	123.797	−17.372	1.00	47.48	GZ00	C
ATOM	5950	N	VAL	X	137	−29.654	120.270	−16.849	1.00	48.09	GZ00	N
ATOM	5951	CA	VAL	X	137	−30.643	119.214	−16.962	1.00	49.70	GZ00	C
ATOM	5952	C	VAL	X	137	−30.865	118.972	−18.443	1.00	47.78	GZ00	C
ATOM	5953	O	VAL	X	137	−31.364	119.852	−19.156	1.00	46.56	GZ00	O
ATOM	5954	CB	VAL	X	137	−31.951	119.574	−16.249	1.00	41.53	GZ00	C
ATOM	5955	CG1	VAL	X	137	−32.927	118.433	−16.354	1.00	38.78	GZ00	C
ATOM	5956	CG2	VAL	X	137	−31.677	119.926	−14.782	1.00	37.08	GZ00	C
ATOM	5957	N	CYS	X	138	−30.480	117.787	−18.905	1.00	41.44	GZ00	N
ATOM	5958	CA	CYS	X	138	−30.653	117.371	−20.292	1.00	44.75	GZ00	C
ATOM	5959	C	CYS	X	138	−31.717	116.286	−20.316	1.00	42.51	GZ00	C
ATOM	5960	O	CYS	X	138	−31.459	115.150	−19.904	1.00	45.75	GZ00	O
ATOM	5961	CB	CYS	X	138	−29.341	116.850	−20.872	1.00	41.85	GZ00	C
ATOM	5962	SG	CYS	X	138	−29.335	116.711	−22.686	1.00	48.77	GZ00	S
ATOM	5963	N	LEU	X	139	−32.904	116.627	−20.803	1.00	40.25	GZ00	N
ATOM	5964	CA	LEU	X	139	−33.998	115.670	−20.918	1.00	44.13	GZ00	C
ATOM	5965	C	LEU	X	139	−34.091	115.164	−22.348	1.00	48.33	GZ00	C
ATOM	5966	O	LEU	X	139	−34.096	115.956	−23.296	1.00	49.49	GZ00	O
ATOM	5967	CB	LEU	X	139	−35.323	116.286	−20.469	1.00	40.97	GZ00	C
ATOM	5968	CG	LEU	X	139	−35.163	116.830	−19.046	1.00	45.88	GZ00	C
ATOM	5969	CD1	LEU	X	139	−34.991	118.304	−19.121	1.00	55.62	GZ00	C
ATOM	5970	CD2	LEU	X	139	−36.336	116.513	−18.183	1.00	56.00	GZ00	C
ATOM	5971	N	ILE	X	140	−34.185	113.843	−22.489	1.00	43.98	GZ00	N
ATOM	5972	CA	ILE	X	140	−34.065	113.151	−23.763	1.00	39.00	GZ00	C
ATOM	5973	C	ILE	X	140	−35.287	112.261	−23.897	1.00	41.08	GZ00	C
ATOM	5974	O	ILE	X	140	−35.562	111.453	−23.003	1.00	45.21	GZ00	O
ATOM	5975	CB	ILE	X	140	−32.776	112.314	−23.820	1.00	38.23	GZ00	C
ATOM	5976	CG1	ILE	X	140	−31.593	113.141	−23.326	1.00	38.68	GZ00	C
ATOM	5977	CG2	ILE	X	140	−32.517	111.813	−25.212	1.00	37.81	GZ00	C
ATOM	5978	CD1	ILE	X	140	−30.465	112.309	−22.831	1.00	36.60	GZ00	C
ATOM	5979	N	SER	X	141	−36.037	112.410	−24.986	1.00	38.32	GZ00	N
ATOM	5980	CA	SER	X	141	−37.296	111.688	−25.062	1.00	41.71	GZ00	C
ATOM	5981	C	SER	X	141	−37.616	111.305	−26.496	1.00	42.47	GZ00	C
ATOM	5982	O	SER	X	141	−37.050	111.841	−27.451	1.00	41.57	GZ00	O
ATOM	5983	CB	SER	X	141	−38.442	112.523	−24.495	1.00	41.65	GZ00	C
ATOM	5984	OG	SER	X	141	−38.508	113.735	−25.214	1.00	44.00	GZ00	O
ATOM	5985	N	ASP	X	142	−38.557	110.367	−26.620	1.00	46.32	GZ00	N
ATOM	5986	CA	ASP	X	142	−39.150	109.987	−27.901	1.00	48.85	GZ00	C
ATOM	5987	C	ASP	X	142	−38.129	109.382	−28.860	1.00	51.47	GZ00	C
ATOM	5988	O	ASP	X	142	−38.175	109.623	−30.072	1.00	44.48	GZ00	O
ATOM	5989	CB	ASP	X	142	−39.846	111.179	−28.546	1.00	47.17	GZ00	C
ATOM	5990	CG	ASP	X	142	−41.165	111.502	−27.888	1.00	60.06	GZ00	C
ATOM	5991	OD1	ASP	X	142	−41.856	110.559	−27.429	1.00	53.08	GZ00	O
ATOM	5992	OD2	ASP	X	142	−41.509	112.706	−27.833	1.00	72.08	GZ00	O1−
ATOM	5993	N	PHE	X	143	−37.183	108.607	−28.329	1.00	42.34	GZ00	N
ATOM	5994	CA	PHE	X	143	−36.209	107.975	−29.202	1.00	50.27	GZ00	C
ATOM	5995	C	PHE	X	143	−36.431	106.471	−29.275	1.00	46.86	GZ00	C
ATOM	5996	O	PHE	X	143	−36.969	105.852	−28.352	1.00	43.04	GZ00	O
ATOM	5997	CB	PHE	X	143	−34.773	108.296	−28.793	1.00	38.71	GZ00	C
ATOM	5998	CG	PHE	X	143	−34.426	107.944	−27.388	1.00	40.75	GZ00	C
ATOM	5999	CD1	PHE	X	143	−33.898	106.698	−27.084	1.00	36.49	GZ00	C
ATOM	6000	CD2	PHE	X	143	−34.537	108.889	−26.377	1.00	38.84	GZ00	C
ATOM	6001	CE1	PHE	X	143	−33.510	106.389	−25.788	1.00	41.99	GZ00	C
ATOM	6002	CE2	PHE	X	143	−34.161	108.588	−25.078	1.00	39.59	GZ00	C
ATOM	6003	CZ	PHE	X	143	−33.645	107.330	−24.777	1.00	38.14	GZ00	C
ATOM	6004	N	TYR	X	144	−36.071	105.909	−30.422	1.00	41.60	GZ00	N
ATOM	6005	CA	TYR	X	144	−36.247	104.485	−30.675	1.00	40.98	GZ00	C
ATOM	6006	C	TYR	X	144	−35.290	104.053	−31.769	1.00	46.46	GZ00	C
ATOM	6007	O	TYR	X	144	−35.237	104.680	−32.843	1.00	42.13	GZ00	O
ATOM	6008	CB	TYR	X	144	−37.685	104.146	−31.067	1.00	43.87	GZ00	C
ATOM	6009	CG	TYR	X	144	−37.912	102.658	−31.265	1.00	41.93	GZ00	C
ATOM	6010	CD1	TYR	X	144	−38.183	101.821	−30.184	1.00	44.51	GZ00	C
ATOM	6011	CD2	TYR	X	144	−37.838	102.090	−32.527	1.00	35.71	GZ00	C
ATOM	6012	CE1	TYR	X	144	−38.379	100.445	−30.358	1.00	40.63	GZ00	C
ATOM	6013	CE2	TYR	X	144	−38.050	100.733	−32.717	1.00	40.34	GZ00	C
ATOM	6014	CZ	TYR	X	144	−38.309	99.912	−31.631	1.00	41.12	GZ00	C
ATOM	6015	OH	TYR	X	144	−38.511	98.567	−31.831	1.00	40.40	GZ00	O
ATOM	6016	N	PRO	X	145	−34.530	102.974	−31.511	1.00	40.55	GZ00	N
ATOM	6017	CA	PRO	X	145	−34.563	102.164	−30.284	1.00	43.72	GZ00	C
ATOM	6018	C	PRO	X	145	−33.998	102.849	−29.028	1.00	43.96	GZ00	C
ATOM	6019	O	PRO	X	145	−33.489	103.965	−29.115	1.00	40.33	GZ00	O
ATOM	6020	CB	PRO	X	145	−33.699	100.937	−30.644	1.00	43.12	GZ00	C
ATOM	6021	CG	PRO	X	145	−32.956	101.292	−31.849	1.00	42.92	GZ00	C
ATOM	6022	CD	PRO	X	145	−33.714	102.356	−32.570	1.00	40.02	GZ00	C
ATOM	6023	N	GLY	X	146	−34.102	102.165	−27.884	1.00	38.67	GZ00	N
ATOM	6024	CA	GLY	X	146	−33.811	102.737	−26.584	1.00	36.90	GZ00	C
ATOM	6025	C	GLY	X	146	−32.366	102.660	−26.134	1.00	38.27	GZ00	C
ATOM	6026	O	GLY	X	146	−32.068	102.118	−25.070	1.00	42.45	GZ00	O
ATOM	6027	N	ALA	X	147	−31.462	103.201	−26.930	1.00	33.88	GZ00	N
ATOM	6028	CA	ALA	X	147	−30.063	103.278	−26.560	1.00	36.10	GZ00	C
ATOM	6029	C	ALA	X	147	−29.541	104.597	−27.083	1.00	33.68	GZ00	C
ATOM	6030	O	ALA	X	147	−29.858	105.007	−28.203	1.00	39.90	GZ00	O
ATOM	6031	CB	ALA	X	147	−29.225	102.121	−27.118	1.00	29.64	GZ00	C
ATOM	6032	N	VAL	X	148	−28.712	105.231	−26.263	1.00	33.29	GZ00	N
ATOM	6033	CA	VAL	X	148	−28.309	106.608	−26.467	1.00	34.38	GZ00	C
ATOM	6034	C	VAL	X	148	−27.005	106.806	−25.702	1.00	44.52	GZ00	C
ATOM	6035	O	VAL	X	148	−26.787	106.191	−24.652	1.00	39.89	GZ00	O
ATOM	6036	CB	VAL	X	148	−29.464	107.518	−25.970	1.00	40.00	GZ00	C
ATOM	6037	CG1	VAL	X	148	−28.993	108.560	−25.020	1.00	41.53	GZ00	C
ATOM	6038	CG2	VAL	X	148	−30.271	108.073	−27.138	1.00	35.87	GZ00	C
ATOM	6039	N	THR	X	149	−26.133	107.663	−26.213	1.00	36.77	GZ00	N
ATOM	6040	CA	THR	X	149	−24.987	108.051	−25.409	1.00	38.57	GZ00	C
ATOM	6041	C	THR	X	149	−24.960	109.563	−25.294	1.00	44.30	GZ00	C
ATOM	6042	O	THR	X	149	−25.353	110.287	−26.217	1.00	42.08	GZ00	O
ATOM	6043	CB	THR	X	149	−23.650	107.565	−25.975	1.00	48.56	GZ00	C
ATOM	6044	OG1	THR	X	149	−23.455	108.130	−27.276	1.00	56.60	GZ00	O
ATOM	6045	CG2	THR	X	149	−23.624	106.035	−26.054	1.00	37.17	GZ00	C
ATOM	6046	N	VAL	X	150	−24.503	110.036	−24.146	1.00	43.54	GZ00	N
ATOM	6047	CA	VAL	X	150	−24.564	111.452	−23.836	1.00	47.15	GZ00	C
ATOM	6048	C	VAL	X	150	−23.160	111.946	−23.536	1.00	46.29	GZ00	C
ATOM	6049	O	VAL	X	150	−22.484	111.422	−22.642	1.00	44.10	GZ00	O
ATOM	6050	CB	VAL	X	150	−25.519	111.726	−22.663	1.00	42.61	GZ00	C
ATOM	6051	CG1	VAL	X	150	−25.584	113.212	−22.388	1.00	45.14	GZ00	C
ATOM	6052	CG2	VAL	X	150	−26.919	111.152	−22.975	1.00	37.35	GZ00	C
ATOM	6053	N	ALA	X	151	−22.741	112.977	−24.260	1.00	43.99	GZ00	N
ATOM	6054	CA	ALA	X	151	−21.484	113.665	−24.002	1.00	55.42	GZ00	C
ATOM	6055	C	ALA	X	151	−21.769	115.133	−23.706	1.00	56.11	GZ00	C
ATOM	6056	O	ALA	X	151	−22.614	115.758	−24.361	1.00	51.73	GZ00	O
ATOM	6057	CB	ALA	X	151	−20.528	113.545	−25.190	1.00	47.91	GZ00	C
ATOM	6058	N	TRP	X	152	−21.091	115.665	−22.693	1.00	48.76	GZ00	N
ATOM	6059	CA	TRP	X	152	−21.207	117.064	−22.312	1.00	52.98	GZ00	C
ATOM	6060	C	TRP	X	152	−19.957	117.821	−22.742	1.00	62.60	GZ00	C
ATOM	6061	O	TRP	X	152	−18.840	117.307	−22.638	1.00	63.13	GZ00	O
ATOM	6062	CB	TRP	X	152	−21.402	117.202	−20.798	1.00	54.47	GZ00	C
ATOM	6063	CG	TRP	X	152	−22.732	116.706	−20.310	1.00	55.93	GZ00	C
ATOM	6064	CD1	TRP	X	152	−23.070	115.415	−20.021	1.00	50.45	GZ00	C
ATOM	6065	CD2	TRP	X	152	−23.908	117.493	−20.059	1.00	54.33	GZ00	C
ATOM	6066	NE1	TRP	X	152	−24.380	115.350	−19.603	1.00	45.37	GZ00	N
ATOM	6067	CE2	TRP	X	152	−24.919	116.608	−19.624	1.00	49.73	GZ00	C
ATOM	6068	CE3	TRP	X	152	−24.205	118.856	−20.162	1.00	49.64	GZ00	C
ATOM	6069	CZ2	TRP	X	152	−26.201	117.046	−19.286	1.00	49.17	GZ00	C
ATOM	6070	CZ3	TRP	X	152	−25.488	119.290	−19.834	1.00	47.92	GZ00	C
ATOM	6071	CH2	TRP	X	152	−26.464	118.390	−19.400	1.00	49.61	GZ00	C
ATOM	6072	N	LYS	X	153	−20.141	119.053	−23.204	1.00	65.10	GZ00	N
ATOM	6073	CA	LYS	X	153	−19.019	119.883	−23.602	1.00	62.17	GZ00	C
ATOM	6074	C	LYS	X	153	−19.122	121.266	−22.971	1.00	70.98	GZ00	C
ATOM	6075	O	LYS	X	153	−20.213	121.849	−22.883	1.00	60.73	GZ00	O
ATOM	6076	CB	LYS	X	153	−18.918	119.968	−25.133	1.00	62.97	GZ00	C
ATOM	6077	CG	LYS	X	153	−18.343	118.679	−25.728	1.00	71.97	GZ00	C
ATOM	6078	CD	LYS	X	153	−18.093	118.773	−27.212	1.00	76.62	GZ00	C
ATOM	6079	CE	LYS	X	153	−17.488	117.483	−27.757	1.00	78.74	GZ00	C
ATOM	6080	NZ	LYS	X	153	−17.470	117.510	−29.257	1.00	82.65	GZ00	N1+
ATOM	6081	N	ALA	X	154	−17.966	121.767	−22.517	1.00	68.61	GZ00	N
ATOM	6082	CA	ALA	X	154	−17.783	123.138	−22.053	1.00	70.61	GZ00	C
ATOM	6083	C	ALA	X	154	−16.988	123.883	−23.122	1.00	76.84	GZ00	C
ATOM	6084	O	ALA	X	154	−15.785	123.645	−23.282	1.00	70.93	GZ00	O
ATOM	6085	CB	ALA	X	154	−17.057	123.158	−20.709	1.00	58.77	GZ00	C
ATOM	6086	N	ASP	X	155	−17.672	124.765	−23.853	1.00	75.44	GZ00	N
ATOM	6087	CA	ASP	X	155	−17.137	125.491	−25.013	1.00	86.60	GZ00	C
ATOM	6088	C	ASP	X	155	−16.167	124.618	−25.821	1.00	88.28	GZ00	C
ATOM	6089	O	ASP	X	155	−14.980	124.919	−25.980	1.00	92.56	GZ00	O
ATOM	6090	CB	ASP	X	155	−16.529	126.864	−24.643	1.00	93.75	GZ00	C
ATOM	6091	CG	ASP	X	155	−15.592	126.838	−23.429	1.00	92.88	GZ00	C
ATOM	6092	OD2	ASP	X	155	−15.842	127.652	−22.504	1.00	84.61	GZ00	O1−
ATOM	6093	OD1	ASP	X	155	−14.599	126.064	−23.414	1.00	88.83	GZ00	O
ATOM	6094	N	SER	X	156	−16.707	123.493	−26.297	1.00	79.32	GZ00	N
ATOM	6095	CA	SER	X	156	−16.051	122.520	−27.174	1.00	78.60	GZ00	C
ATOM	6096	C	SER	X	156	−14.971	121.688	−26.498	1.00	74.64	GZ00	C
ATOM	6097	O	SER	X	156	−14.249	120.963	−27.189	1.00	84.36	GZ00	O
ATOM	6098	CB	SER	X	156	−15.436	123.186	−28.416	1.00	73.87	GZ00	C
ATOM	6099	OG	SER	X	156	−16.405	123.895	−29.165	1.00	81.66	GZ00	O
ATOM	6100	N	SER	X	157	−14.854	121.728	−25.183	1.00	69.01	GZ00	N
ATOM	6101	CA	SER	X	157	−13.979	120.769	−24.541	1.00	69.77	GZ00	C
ATOM	6102	C	SER	X	157	−14.813	119.693	−23.873	1.00	80.18	GZ00	C
ATOM	6103	O	SER	X	157	−15.795	120.013	−23.189	1.00	78.55	GZ00	O
ATOM	6104	CB	SER	X	157	−13.084	121.447	−23.505	1.00	71.70	GZ00	C
ATOM	6105	OG	SER	X	157	−12.182	122.329	−24.136	1.00	83.37	GZ00	O
ATOM	6106	N	PRO	X	158	−14.476	118.419	−24.062	1.00	82.78	GZ00	N
ATOM	6107	CA	PRO	X	158	−15.228	117.349	−23.395	1.00	76.46	GZ00	C
ATOM	6108	C	PRO	X	158	−15.217	117.510	−21.881	1.00	71.70	GZ00	C
ATOM	6109	O	PRO	X	158	−14.185	117.812	−21.277	1.00	72.61	GZ00	O
ATOM	6110	CB	PRO	X	158	−14.501	116.072	−23.839	1.00	73.01	GZ00	C
ATOM	6111	CG	PRO	X	158	−13.220	116.534	−24.487	1.00	79.70	GZ00	C
ATOM	6112	CD	PRO	X	158	−13.513	117.891	−25.037	1.00	80.30	GZ00	C
ATOM	6113	N	VAL	X	159	−16.375	117.266	−21.266	1.00	66.35	GZ00	N
ATOM	6114	CA	VAL	X	159	−16.548	117.386	−19.823	1.00	62.00	GZ00	C
ATOM	6115	C	VAL	X	159	−16.401	116.006	−19.204	1.00	69.04	GZ00	C
ATOM	6116	O	VAL	X	159	−17.189	115.099	−19.491	1.00	77.71	GZ00	O
ATOM	6117	CB	VAL	X	159	−17.910	117.997	−19.467	1.00	64.97	GZ00	C
ATOM	6118	CG1	VAL	X	159	−18.084	118.013	−17.959	1.00	62.71	GZ00	C
ATOM	6119	CG2	VAL	X	159	−18.059	119.400	−20.075	1.00	59.52	GZ00	C
ATOM	6120	N	LYS	X	160	−15.413	115.857	−18.328	1.00	74.85	GZ00	N
ATOM	6121	CA	LYS	X	160	−14.967	114.550	−17.867	1.00	79.58	GZ00	C
ATOM	6122	C	LYS	X	160	−15.580	114.124	−16.535	1.00	75.16	GZ00	C
ATOM	6123	O	LYS	X	160	−15.412	112.964	−16.143	1.00	82.11	GZ00	O
ATOM	6124	CB	LYS	X	160	−13.429	114.543	−17.758	1.00	85.50	GZ00	C
ATOM	6125	CG	LYS	X	160	−12.723	113.330	−18.377	1.00	89.99	GZ00	C
ATOM	6126	CD	LYS	X	160	−12.558	113.438	−19.900	1.00	91.72	GZ00	C
ATOM	6127	CE	LYS	X	160	−11.807	112.217	−20.463	1.00	101.89	GZ00	C
ATOM	6128	NZ	LYS	X	160	−11.786	112.147	−21.960	1.00	92.33	GZ00	N1+
ATOM	6129	N	ALA	X	161	−16.284	115.011	−15.833	1.00	64.13	GZ00	N
ATOM	6130	CA	ALA	X	161	−16.778	114.677	−14.503	1.00	64.11	GZ00	C
ATOM	6131	C	ALA	X	161	−18.053	115.454	−14.206	1.00	60.81	GZ00	C
ATOM	6132	O	ALA	X	161	−18.346	116.472	−14.836	1.00	59.19	GZ00	O
ATOM	6133	CB	ALA	X	161	−15.728	114.953	−13.424	1.00	61.76	GZ00	C
ATOM	6134	N	GLY	X	162	−18.809	114.954	−13.231	1.00	53.42	GZ00	N
ATOM	6135	CA	GLY	X	162	−20.048	115.575	−12.823	1.00	55.17	GZ00	C
ATOM	6136	C	GLY	X	162	−21.273	115.133	−13.595	1.00	59.06	GZ00	C
ATOM	6137	O	GLY	X	162	−22.353	115.706	−13.396	1.00	55.42	GZ00	O
ATOM	6138	N	VAL	X	163	−21.147	114.128	−14.458	1.00	52.82	GZ00	N
ATOM	6139	CA	VAL	X	163	−22.234	113.680	−15.316	1.00	48.37	GZ00	C
ATOM	6140	C	VAL	X	163	−22.874	112.455	−14.689	1.00	49.71	GZ00	C
ATOM	6141	O	VAL	X	163	−22.179	111.511	−14.296	1.00	50.43	GZ00	O
ATOM	6142	CB	VAL	X	163	−21.738	113.364	−16.737	1.00	45.16	GZ00	C
ATOM	6143	CG1	VAL	X	163	−22.863	112.761	−17.564	1.00	41.69	GZ00	C
ATOM	6144	CG2	VAL	X	163	−21.220	114.622	−17.401	1.00	46.72	GZ00	C
ATOM	6145	N	GLU	X	164	−24.197	112.468	−14.599	1.00	47.13	GZ00	N
ATOM	6146	CA	GLU	X	164	−24.964	111.300	−14.201	1.00	53.09	GZ00	C
ATOM	6147	C	GLU	X	164	−26.115	111.140	−15.178	1.00	46.61	GZ00	C
ATOM	6148	O	GLU	X	164	−26.815	112.113	−15.471	1.00	51.75	GZ00	O
ATOM	6149	CB	GLU	X	164	−25.447	111.448	−12.757	1.00	51.29	GZ00	C
ATOM	6150	CG	GLU	X	164	−24.369	110.989	−11.771	1.00	66.35	GZ00	C
ATOM	6151	CD	GLU	X	164	−24.588	111.481	−10.349	1.00	80.34	GZ00	C
ATOM	6152	OE1	GLU	X	164	−25.618	112.153	−10.090	1.00	84.11	GZ00	O
ATOM	6153	OE2	GLU	X	164	−23.723	111.189	−9.486	1.00	74.82	GZ00	O1−
ATOM	6154	N	THR	X	165	−26.291	109.923	−15.699	1.00	44.17	GZ00	N
ATOM	6155	CA	THR	X	165	−27.216	109.646	−16.791	1.00	41.22	GZ00	C
ATOM	6156	C	THR	X	165	−28.051	108.419	−16.450	1.00	43.11	GZ00	C
ATOM	6157	O	THR	X	165	−27.536	107.449	−15.891	1.00	46.87	GZ00	O
ATOM	6158	CB	THR	X	165	−26.455	109.433	−18.098	1.00	41.49	GZ00	C
ATOM	6159	OG1	THR	X	165	−25.742	110.625	−18.421	1.00	41.60	GZ00	O
ATOM	6160	CG2	THR	X	165	−27.397	109.091	−19.242	1.00	40.37	GZ00	C
ATOM	6161	N	THR	X	166	−29.352	108.492	−16.715	1.00	45.39	GZ00	N
ATOM	6162	CA	THR	X	166	−30.228	107.356	−16.466	1.00	48.92	GZ00	C
ATOM	6163	C	THR	X	166	−30.165	106.353	−17.611	1.00	43.82	GZ00	C
ATOM	6164	O	THR	X	166	−29.861	106.689	−18.756	1.00	48.48	GZ00	O
ATOM	6165	CB	THR	X	166	−31.684	107.786	−16.285	1.00	42.46	GZ00	C
ATOM	6166	OG1	THR	X	166	−32.133	108.501	−17.446	1.00	42.85	GZ00	O
ATOM	6167	CG2	THR	X	166	−31.833	108.639	−15.075	1.00	49.93	GZ00	C
ATOM	6168	N	VAL	X	167	−30.481	105.109	−17.287	1.00	43.83	GZ00	N
ATOM	6169	CA	VAL	X	167	−30.761	104.109	−18.306	1.00	47.99	GZ00	C
ATOM	6170	C	VAL	X	167	−32.044	104.535	−19.004	1.00	43.14	GZ00	C
ATOM	6171	O	VAL	X	167	−32.921	105.146	−18.381	1.00	51.16	GZ00	O
ATOM	6172	CB	VAL	X	167	−30.905	102.716	−17.689	1.00	47.80	GZ00	C
ATOM	6173	CG1	VAL	X	167	−29.736	102.444	−16.786	1.00	37.96	GZ00	C
ATOM	6174	CG2	VAL	X	167	−32.215	102.646	−16.913	1.00	51.34	GZ00	C
ATOM	6175	N	PRO	X	168	−32.201	104.266	−20.280	1.00	44.56	GZ00	N
ATOM	6176	CA	PRO	X	168	−33.464	104.616	−20.934	1.00	41.00	GZ00	C
ATOM	6177	C	PRO	X	168	−34.607	103.782	−20.385	1.00	47.02	GZ00	C
ATOM	6178	O	PRO	X	168	−34.429	102.648	−19.941	1.00	49.69	GZ00	O
ATOM	6179	CB	PRO	X	168	−33.202	104.334	−22.419	1.00	43.99	GZ00	C
ATOM	6180	CG	PRO	X	168	−31.908	103.574	−22.452	1.00	46.78	GZ00	C
ATOM	6181	CD	PRO	X	168	−31.141	103.904	−21.227	1.00	39.42	GZ00	C
ATOM	6182	N	SER	X	169	−35.784	104.384	−20.368	1.00	47.67	GZ00	N
ATOM	6183	CA	SER	X	169	−36.987	103.723	−19.907	1.00	50.31	GZ00	C
ATOM	6184	C	SER	X	169	−38.095	103.966	−20.920	1.00	49.36	GZ00	C
ATOM	6185	O	SER	X	169	−38.168	105.022	−21.563	1.00	43.92	GZ00	O
ATOM	6186	CB	SER	X	169	−37.417	104.225	−18.517	1.00	43.96	GZ00	C
ATOM	6187	OG	SER	X	169	−37.708	105.604	−18.594	1.00	55.02	GZ00	O
ATOM	6188	N	LYS	X	170	−38.955	102.967	−21.057	1.00	52.10	GZ00	N
ATOM	6189	CA	LYS	X	170	−39.974	102.986	−22.090	1.00	53.24	GZ00	C
ATOM	6190	C	LYS	X	170	−41.088	103.939	−21.683	1.00	52.61	GZ00	C
ATOM	6191	O	LYS	X	170	−41.529	103.938	−20.531	1.00	55.96	GZ00	O
ATOM	6192	CB	LYS	X	170	−40.491	101.563	−22.339	1.00	57.92	GZ00	C
ATOM	6193	CG	LYS	X	170	−41.220	101.352	−23.678	1.00	61.39	GZ00	C
ATOM	6194	CD	LYS	X	170	−41.730	99.902	−23.841	1.00	60.71	GZ00	C
ATOM	6195	CE	LYS	X	170	−40.545	98.928	−24.020	1.00	68.36	GZ00	C
ATOM	6196	NZ	LYS	X	170	−40.911	97.510	−24.330	1.00	76.29	GZ00	N1+
ATOM	6197	N	GLN	X	171	−41.485	104.794	−22.619	1.00	49.96	GZ00	N
ATOM	6198	CA	GLN	X	171	−42.633	105.668	−22.499	1.00	48.46	GZ00	C
ATOM	6199	C	GLN	X	171	−43.897	104.888	−22.851	1.00	55.64	GZ00	C
ATOM	6200	O	GLN	X	171	−43.843	103.749	−23.324	1.00	58.51	GZ00	O
ATOM	6201	CB	GLN	X	171	−42.474	106.880	−23.422	1.00	47.95	GZ00	C
ATOM	6202	CG	GLN	X	171	−41.214	107.699	−23.166	1.00	44.29	GZ00	C
ATOM	6203	CD	GLN	X	171	−40.919	108.737	−24.253	1.00	49.84	GZ00	C
ATOM	6204	OE1	GLN	X	171	−40.035	109.590	−24.090	1.00	47.77	GZ00	O
ATOM	6205	NE2	GLN	X	171	−41.651	108.667	−25.365	1.00	49.40	GZ00	N
ATOM	6206	N	SER	X	172	−45.052	105.506	−22.605	1.00	61.57	GZ00	N
ATOM	6207	CA	SER	X	172	−46.313	104.841	−22.927	1.00	67.22	GZ00	C
ATOM	6208	C	SER	X	172	−46.410	104.535	−24.419	1.00	65.89	GZ00	C
ATOM	6209	O	SER	X	172	−46.922	103.477	−24.808	1.00	65.81	GZ00	O
ATOM	6210	CB	SER	X	172	−47.491	105.696	−22.460	1.00	55.65	GZ00	C
ATOM	6211	OG	SER	X	172	−47.391	106.989	−23.016	1.00	65.82	GZ00	O
ATOM	6212	N	ASN	X	173	−45.891	105.434	−25.268	1.00	64.43	GZ00	N
ATOM	6213	CA	ASN	X	173	−45.898	105.274	−26.722	1.00	55.79	GZ00	C
ATOM	6214	C	ASN	X	173	−44.815	104.319	−27.236	1.00	60.52	GZ00	C
ATOM	6215	O	ASN	X	173	−44.548	104.300	−28.446	1.00	58.94	GZ00	O
ATOM	6216	CB	ASN	X	173	−45.762	106.634	−27.419	1.00	56.26	GZ00	C
ATOM	6217	CG	ASN	X	173	−44.404	107.291	−27.198	1.00	62.34	GZ00	C
ATOM	6218	OD1	ASN	X	173	−43.536	106.762	−26.496	1.00	55.11	GZ00	O
ATOM	6219	ND2	ASN	X	173	−44.207	108.450	−27.834	1.00	61.15	GZ00	N
ATOM	6220	N	ASN	X	174	−44.162	103.573	−26.348	1.00	57.78	GZ00	N
ATOM	6221	CA	ASN	X	174	−43.139	102.573	−26.649	1.00	62.92	GZ00	C
ATOM	6222	C	ASN	X	174	−41.849	103.159	−27.207	1.00	62.49	GZ00	C
ATOM	6223	O	ASN	X	174	−40.923	102.390	−27.512	1.00	56.92	GZ00	O
ATOM	6224	CB	ASN	X	174	−43.647	101.485	−27.598	1.00	64.96	GZ00	C
ATOM	6225	CG	ASN	X	174	−44.491	100.463	−26.877	1.00	72.73	GZ00	C
ATOM	6226	OD1	ASN	X	174	−44.329	100.265	−25.673	1.00	66.54	GZ00	O
ATOM	6227	ND2	ASN	X	174	−45.394	99.809	−27.599	1.00	78.95	GZ00	N
ATOM	6228	N	LYS	X	175	−41.738	104.481	−27.328	1.00	58.39	GZ00	N
ATOM	6229	CA	LYS	X	175	−40.429	105.092	−27.468	1.00	52.42	GZ00	C
ATOM	6230	C	LYS	X	175	−39.796	105.219	−26.086	1.00	49.60	GZ00	C
ATOM	6231	O	LYS	X	175	−40.366	104.789	−25.077	1.00	48.97	GZ00	O
ATOM	6232	CB	LYS	X	175	−40.537	106.429	−28.183	1.00	49.13	GZ00	C
ATOM	6233	CG	LYS	X	175	−41.199	106.317	−29.545	1.00	48.64	GZ00	C
ATOM	6234	CD	LYS	X	175	−41.226	107.678	−30.217	1.00	55.03	GZ00	C
ATOM	6235	CE	LYS	X	175	−42.052	107.683	−31.482	1.00	50.14	GZ00	C
ATOM	6236	NZ	LYS	X	175	−41.863	108.996	−32.147	1.00	65.58	GZ00	N
ATOM	6237	N	TYR	X	176	−38.595	105.789	−26.028	1.00	45.23	GZ00	N
ATOM	6238	CA	TYR	X	176	−37.810	105.757	−24.803	1.00	46.64	GZ00	C
ATOM	6239	C	TYR	X	176	−37.405	107.159	−24.375	1.00	46.24	GZ00	C
ATOM	6240	O	TYR	X	176	−37.332	108.091	−25.185	1.00	42.79	GZ00	O
ATOM	6241	CB	TYR	X	176	−36.559	104.893	−24.956	1.00	40.24	GZ00	C
ATOM	6242	CG	TYR	X	176	−36.865	103.419	−25.082	1.00	46.22	GZ00	C
ATOM	6243	CD1	TYR	X	176	−37.356	102.882	−26.276	1.00	40.78	GZ00	C
ATOM	6244	CD2	TYR	X	176	−36.683	102.567	−24.006	1.00	47.03	GZ00	C
ATOM	6245	CE1	TYR	X	176	−37.628	101.537	−26.389	1.00	43.89	GZ00	C
ATOM	6246	CE2	TYR	X	176	−36.965	101.215	−24.107	1.00	51.38	GZ00	C
ATOM	6247	CZ	TYR	X	176	−37.439	100.706	−25.294	1.00	52.19	GZ00	C
ATOM	6248	OH	TYR	X	176	−37.713	99.359	−25.380	1.00	57.66	GZ00	O
ATOM	6249	N	ALA	X	177	−37.152	107.290	−23.072	1.00	42.19	GZ00	N
ATOM	6250	CA	ALA	X	177	−36.737	108.543	−22.464	1.00	42.58	GZ00	C
ATOM	6251	C	ALA	X	177	−35.553	108.309	−21.543	1.00	39.64	GZ00	C
ATOM	6252	O	ALA	X	177	−35.393	107.231	−20.966	1.00	43.45	GZ00	O
ATOM	6253	CB	ALA	X	177	−37.873	109.197	−21.673	1.00	36.73	GZ00	C
ATOM	6254	N	ALA	X	178	−34.735	109.339	−21.397	1.00	35.05	GZ00	N
ATOM	6255	CA	ALA	X	178	−33.635	109.306	−20.451	1.00	41.99	GZ00	C
ATOM	6256	C	ALA	X	178	−33.310	110.743	−20.087	1.00	37.98	GZ00	C
ATOM	6257	O	ALA	X	178	−33.750	111.681	−20.751	1.00	42.02	GZ00	O
ATOM	6258	CB	ALA	X	178	−32.406	108.580	−21.021	1.00	32.61	GZ00	C
ATOM	6259	N	SER	X	179	−32.574	110.910	−18.999	1.00	43.75	GZ00	N
ATOM	6260	CA	SER	X	179	−32.093	112.230	−18.639	1.00	42.28	GZ00	C
ATOM	6261	C	SER	X	179	−30.654	112.109	−18.170	1.00	40.65	GZ00	C
ATOM	6262	O	SER	X	179	−30.220	111.051	−17.713	1.00	48.12	GZ00	O
ATOM	6263	CB	SER	X	179	−32.956	112.897	−17.572	1.00	35.06	GZ00	C
ATOM	6264	OG	SER	X	179	−33.250	112.013	−16.525	1.00	37.63	GZ00	O
ATOM	6265	N	SER	X	180	−29.921	113.202	−18.326	1.00	41.05	GZ00	N
ATOM	6266	CA	SER	X	180	−28.523	113.321	−17.950	1.00	41.22	GZ00	C
ATOM	6267	C	SER	X	180	−28.336	114.625	−17.185	1.00	47.40	GZ00	C
ATOM	6268	O	SER	X	180	−28.846	115.667	−17.606	1.00	38.98	GZ00	O
ATOM	6269	CB	SER	X	180	−27.628	113.305	−19.187	1.00	42.77	GZ00	C
ATOM	6270	OG	SER	X	180	−26.270	113.291	−18.824	1.00	40.90	GZ00	O
ATOM	6271	N	TYR	X	181	−27.616	114.556	−16.062	1.00	49.96	GZ00	N
ATOM	6272	CA	TYR	X	181	−27.366	115.685	−15.179	1.00	43.04	GZ00	C
ATOM	6273	C	TYR	X	181	−25.872	115.961	−15.084	1.00	48.60	GZ00	C
ATOM	6274	O	TYR	X	181	−25.089	115.054	−14.778	1.00	50.29	GZ00	O
ATOM	6275	CB	TYR	X	181	−27.922	115.419	−13.778	1.00	32.89	GZ00	C
ATOM	6276	CG	TYR	X	181	−29.417	115.274	−13.722	1.00	40.29	GZ00	C
ATOM	6277	CD2	TYR	X	181	−30.224	116.358	−13.413	1.00	36.67	GZ00	C
ATOM	6278	CD1	TYR	X	181	−30.030	114.053	−13.999	1.00	41.31	GZ00	C
ATOM	6279	CE2	TYR	X	181	−31.614	116.238	−13.366	1.00	40.95	GZ00	C
ATOM	6280	CE1	TYR	X	181	−31.402	113.909	−13.951	1.00	38.36	GZ00	C
ATOM	6281	CZ	TYR	X	181	−32.195	115.000	−13.636	1.00	46.60	GZ00	C
ATOM	6282	OH	TYR	X	181	−33.561	114.845	−13.591	1.00	40.50	GZ00	O
ATOM	6283	N	LEU	X	182	−25.488	117.220	−15.298	1.00	46.12	GZ00	N
ATOM	6284	CA	LEU	X	182	−24.119	117.692	−15.092	1.00	47.69	GZ00	C
ATOM	6285	C	LEU	X	182	−24.094	118.629	−13.889	1.00	50.67	GZ00	C
ATOM	6286	O	LEU	X	182	−24.748	119.679	−13.906	1.00	45.67	GZ00	O
ATOM	6287	CB	LEU	X	182	−23.582	118.410	−16.332	1.00	50.05	GZ00	C
ATOM	6288	CG	LEU	X	182	−22.207	119.070	−16.145	1.00	51.24	GZ00	C
ATOM	6289	CD1	LEU	X	182	−21.143	118.063	−15.726	1.00	46.82	GZ00	C
ATOM	6290	CD2	LEU	X	182	−21.779	119.815	−17.399	1.00	48.62	GZ00	C
ATOM	6291	N	SER	X	183	−23.382	118.231	−12.839	1.00	44.73	GZ00	N
ATOM	6292	CA	SER	X	183	−23.218	119.066	−11.658	1.00	53.81	GZ00	C
ATOM	6293	C	SER	X	183	−21.967	119.928	−11.797	1.00	58.46	GZ00	C
ATOM	6294	O	SER	X	183	−20.896	119.430	−12.152	1.00	65.34	GZ00	O
ATOM	6295	CB	SER	X	183	−23.124	118.218	−10.393	1.00	46.16	GZ00	C
ATOM	6296	OG	SER	X	183	−24.237	117.370	−10.277	1.00	53.51	GZ00	O
ATOM	6297	N	LEU	X	184	−22.104	121.208	−11.480	1.00	52.70	GZ00	N
ATOM	6298	CA	LEU	X	184	−21.025	122.174	−11.566	1.00	59.11	GZ00	C
ATOM	6299	C	LEU	X	184	−21.049	123.030	−10.308	1.00	62.24	GZ00	C
ATOM	6300	O	LEU	X	184	−22.011	123.007	−9.537	1.00	61.48	GZ00	O
ATOM	6301	CB	LEU	X	184	−21.178	123.079	−12.796	1.00	57.83	GZ00	C
ATOM	6302	CG	LEU	X	184	−21.196	122.468	−14.189	1.00	57.44	GZ00	C
ATOM	6303	CD1	LEU	X	184	−21.426	123.563	−15.208	1.00	52.24	GZ00	C
ATOM	6304	CD2	LEU	X	184	−19.901	121.740	−14.475	1.00	62.82	GZ00	C
ATOM	6305	N	THR	X	185	−19.978	123.805	−10.106	1.00	64.47	GZ00	N
ATOM	6306	CA	THR	X	185	−20.070	124.923	−9.176	1.00	60.49	GZ00	C
ATOM	6307	C	THR	X	185	−20.580	126.161	−9.899	1.00	61.60	GZ00	C
ATOM	6308	O	THR	X	185	−20.455	126.279	−11.129	1.00	56.95	GZ00	O
ATOM	6309	CB	THR	X	185	−18.710	125.225	−8.555	1.00	61.74	GZ00	C
ATOM	6310	OG1	THR	X	185	−17.813	125.690	−9.577	1.00	64.33	GZ00	O
ATOM	6311	CG2	THR	X	185	−18.149	124.005	−7.840	1.00	49.10	GZ00	C
ATOM	6312	N	PRO	X	186	−21.194	127.094	−9.165	1.00	63.67	GZ00	N
ATOM	6313	CA	PRO	X	186	−21.536	128.392	−9.774	1.00	66.91	GZ00	C
ATOM	6314	C	PRO	X	186	−20.364	129.034	−10.512	1.00	66.84	GZ00	C
ATOM	6315	O	PRO	X	186	−20.570	129.710	−11.529	1.00	66.08	GZ00	O
ATOM	6316	CB	PRO	X	186	−21.974	129.227	−8.564	1.00	55.91	GZ00	C
ATOM	6317	CG	PRO	X	186	−22.496	128.215	−7.584	1.00	54.51	GZ00	C
ATOM	6318	CD	PRO	X	186	−21.625	127.004	−7.757	1.00	56.56	GZ00	C
ATOM	6319	N	GLU	X	187	−19.133	128.818	−10.030	1.00	69.10	GZ00	N
ATOM	6320	CA	GLU	X	187	−17.938	129.365	−10.676	1.00	76.90	GZ00	C
ATOM	6321	C	GLU	X	187	−17.718	128.740	−12.049	1.00	75.85	GZ00	C
ATOM	6322	O	GLU	X	187	−17.599	129.450	−13.059	1.00	69.16	GZ00	O
ATOM	6323	CB	GLU	X	187	−16.708	129.124	−9.791	1.00	78.07	GZ00	C
ATOM	6324	CG	GLU	X	187	−17.004	128.966	−8.297	1.00	81.84	GZ00	C
ATOM	6325	CD	GLU	X	187	−17.761	130.158	−7.714	1.00	100.11	GZ00	C
ATOM	6326	OE1	GLU	X	187	−17.435	131.317	−8.086	1.00	95.34	GZ00	O
ATOM	6327	OE2	GLU	X	187	−18.692	129.930	−6.901	1.00	102.20	GZ00	O1−
ATOM	6328	N	GLN	X	188	−17.652	127.402	−12.095	1.00	68.87	GZ00	N
ATOM	6329	CA	GLN	X	188	−17.499	126.699	−13.361	1.00	62.65	GZ00	C
ATOM	6330	C	GLN	X	188	−18.597	127.093	−14.333	1.00	65.88	GZ00	C
ATOM	6331	O	GLN	X	188	−18.350	127.252	−15.533	1.00	66.09	GZ00	O
ATOM	6332	CB	GLN	X	188	−17.540	125.195	−13.127	1.00	65.71	GZ00	C
ATOM	6333	CG	GLN	X	188	−16.451	124.635	−12.256	1.00	60.72	GZ00	C
ATOM	6334	CD	GLN	X	188	−16.821	123.252	−11.764	1.00	66.14	GZ00	C
ATOM	6335	OE1	GLN	X	188	−17.996	122.941	−11.617	1.00	70.69	GZ00	O
ATOM	6336	NE2	GLN	X	188	−15.827	122.419	−11.504	1.00	73.28	GZ00	N
ATOM	6337	N	TRP	X	189	−19.821	127.251	−13.828	1.00	60.70	GZ00	N
ATOM	6338	CA	TRP	X	189	−20.941	127.588	−14.695	1.00	61.89	GZ00	C
ATOM	6339	C	TRP	X	189	−20.728	128.932	−15.381	1.00	66.39	GZ00	C
ATOM	6340	O	TRP	X	189	−20.889	129.048	−16.601	1.00	69.50	GZ00	O
ATOM	6341	CB	TRP	X	189	−22.233	127.581	−13.880	1.00	53.09	GZ00	C
ATOM	6342	CG	TRP	X	189	−23.388	128.262	−14.520	1.00	48.26	GZ00	C
ATOM	6343	CD1	TRP	X	189	−24.099	129.288	−13.998	1.00	54.93	GZ00	C
ATOM	6344	CD2	TRP	X	189	−23.972	127.976	−15.799	1.00	53.12	GZ00	C
ATOM	6345	NE1	TRP	X	189	−25.102	129.665	−14.859	1.00	60.99	GZ00	N
ATOM	6346	CE2	TRP	X	189	−25.047	128.878	−15.976	1.00	52.94	GZ00	C
ATOM	6347	CE3	TRP	X	189	−23.704	127.040	−16.803	1.00	54.03	GZ00	C
ATOM	6348	CZ2	TRP	X	189	−25.861	128.873	−17.116	1.00	55.81	GZ00	C
ATOM	6349	CZ3	TRP	X	189	−24.512	127.036	−17.944	1.00	57.95	GZ00	C
ATOM	6350	CH2	TRP	X	189	−25.577	127.953	−18.090	1.00	55.87	GZ00	C
ATOM	6351	N	LYS	X	190	−20.337	129.957	−14.619	1.00	75.20	GZ00	N
ATOM	6352	CA	LYS	X	190	−20.232	131.302	−15.184	1.00	80.83	GZ00	C
ATOM	6353	C	LYS	X	190	−18.940	131.535	−15.962	1.00	78.13	GZ00	C
ATOM	6354	O	LYS	X	190	−18.891	132.458	−16.786	1.00	75.06	GZ00	O
ATOM	6355	CB	LYS	X	190	−20.398	132.357	−14.081	1.00	73.65	GZ00	C
ATOM	6356	CG	LYS	X	190	−21.825	132.394	−13.491	1.00	81.54	GZ00	C
ATOM	6357	CD	LYS	X	190	−21.973	133.326	−12.286	1.00	80.94	GZ00	C
ATOM	6358	CE	LYS	X	190	−23.413	133.330	−11.769	1.00	79.11	GZ00	C
ATOM	6359	NZ	LYS	X	190	−23.602	134.127	−10.516	1.00	82.23	GZ00	N1+
ATOM	6360	N	SER	X	191	−17.917	130.698	−15.765	1.00	70.70	GZ00	N
ATOM	6361	CA	SER	X	191	−16.625	130.963	−16.388	1.00	77.12	GZ00	C
ATOM	6362	C	SER	X	191	−16.645	130.672	−17.891	1.00	80.54	GZ00	C
ATOM	6363	O	SER	X	191	−16.183	131.494	−18.691	1.00	90.60	GZ00	O
ATOM	6364	CB	SER	X	191	−15.528	130.163	−15.676	1.00	70.51	GZ00	C
ATOM	6365	OG	SER	X	191	−15.673	128.776	−15.878	1.00	73.70	GZ00	O
ATOM	6366	N	HIS	X	192	−17.193	129.529	−18.303	1.00	79.21	GZ00	N
ATOM	6367	CA	HIS	X	192	−17.144	129.148	−19.709	1.00	68.99	GZ00	C
ATOM	6368	C	HIS	X	192	−18.216	129.880	−20.503	1.00	68.52	GZ00	C
ATOM	6369	O	HIS	X	192	−19.228	130.326	−19.959	1.00	75.08	GZ00	O
ATOM	6370	CB	HIS	X	192	−17.328	127.646	−19.858	1.00	67.33	GZ00	C
ATOM	6371	CG	HIS	X	192	−16.211	126.849	−19.270	1.00	72.96	GZ00	C
ATOM	6372	ND1	HIS	X	192	−16.133	126.565	−17.924	1.00	69.38	GZ00	N
ATOM	6373	CD2	HIS	X	192	−15.134	126.260	−19.844	1.00	69.24	GZ00	C
ATOM	6374	CE1	HIS	X	192	−15.051	125.843	−17.690	1.00	77.85	GZ00	C
ATOM	6375	NE2	HIS	X	192	−14.427	125.644	−18.839	1.00	78.93	GZ00	N
ATOM	6376	N	ARG	X	193	−17.980	130.015	−21.811	1.00	67.36	GZ00	N
ATOM	6377	CA	ARG	X	193	−18.945	130.743	−22.627	1.00	70.06	GZ00	C
ATOM	6378	C	ARG	X	193	−20.261	129.998	−22.711	1.00	73.81	GZ00	C
ATOM	6379	O	ARG	X	193	−21.329	130.620	−22.671	1.00	71.37	GZ00	O
ATOM	6380	CB	ARG	X	193	−18.411	131.013	−24.033	1.00	83.17	GZ00	C
ATOM	6381	CG	ARG	X	193	−17.125	131.815	−24.098	1.00	91.89	GZ00	C
ATOM	6382	CD	ARG	X	193	−16.644	131.932	−25.540	1.00	98.59	GZ00	C
ATOM	6383	NE	ARG	X	193	−15.566	132.909	−25.682	1.00	110.88	GZ00	N
ATOM	6384	CZ	ARG	X	193	−14.801	133.031	−26.763	1.00	111.56	GZ00	C
ATOM	6385	NH1	ARG	X	193	−13.838	133.947	−26.798	1.00	100.02	GZ00	N1+
ATOM	6386	NH2	ARG	X	193	−15.019	132.260	−27.824	1.00	112.85	GZ00	N
ATOM	6387	N	SER	X	194	−20.207	128.670	−22.831	1.00	80.31	GZ00	N
ATOM	6388	CA	SER	X	194	−21.414	127.865	−22.991	1.00	74.11	GZ00	C
ATOM	6389	C	SER	X	194	−21.137	126.416	−22.618	1.00	71.90	GZ00	C
ATOM	6390	O	SER	X	194	−19.991	125.955	−22.604	1.00	68.02	GZ00	O
ATOM	6391	CB	SER	X	194	−21.945	127.911	−24.425	1.00	69.53	GZ00	C
ATOM	6392	OG	SER	X	194	−21.159	127.065	−25.246	1.00	67.74	GZ00	O
ATOM	6393	N	TYR	X	195	−22.224	125.690	−22.382	1.00	67.26	GZ00	N
ATOM	6394	CA	TYR	X	195	−22.180	124.258	−22.168	1.00	63.57	GZ00	C
ATOM	6395	C	TYR	X	195	−23.120	123.573	−23.142	1.00	64.49	GZ00	C
ATOM	6396	O	TYR	X	195	−24.117	124.154	−23.584	1.00	56.47	GZ00	O
ATOM	6397	CB	TYR	X	195	−22.572	123.889	−20.766	1.00	57.00	GZ00	C
ATOM	6398	CG	TYR	X	195	−21.519	124.195	−19.752	1.00	60.50	GZ00	C
ATOM	6399	CD1	TYR	X	195	−21.344	125.486	−19.268	1.00	63.71	GZ00	C
ATOM	6400	CD2	TYR	X	195	−20.712	123.184	−19.254	1.00	60.86	GZ00	C
ATOM	6401	CE1	TYR	X	195	−20.383	125.757	−18.319	1.00	66.00	GZ00	C
ATOM	6402	CE2	TYR	X	195	−19.756	123.440	−18.310	1.00	67.49	GZ00	C
ATOM	6403	CZ	TYR	X	195	−19.588	124.727	−17.850	1.00	65.78	GZ00	C
ATOM	6404	OH	TYR	X	195	−18.626	124.963	−16.906	1.00	71.05	GZ00	O
ATOM	6405	N	SER	X	196	−22.786	122.326	−23.470	1.00	62.79	GZ00	N
ATOM	6406	CA	SER	X	196	−23.538	121.568	−24.453	1.00	61.48	GZ00	C
ATOM	6407	C	SER	X	196	−23.826	120.160	−23.952	1.00	61.15	GZ00	C
ATOM	6408	O	SER	X	196	−23.001	119.525	−23.279	1.00	54.07	GZ00	O
ATOM	6409	CB	SER	X	196	−22.791	121.504	−25.783	1.00	63.75	GZ00	C
ATOM	6410	OG	SER	X	196	−22.721	122.789	−26.372	1.00	69.20	GZ00	O
ATOM	6411	N	CYS	X	197	−25.014	119.690	−24.294	1.00	52.83	GZ00	N
ATOM	6412	CA	CYS	X	197	−25.428	118.315	−24.085	1.00	51.91	GZ00	C
ATOM	6413	C	CYS	X	197	−25.524	117.683	−25.463	1.00	55.35	GZ00	C
ATOM	6414	O	CYS	X	197	−26.303	118.149	−26.305	1.00	55.75	GZ00	O
ATOM	6415	CB	CYS	X	197	−26.772	118.256	−23.354	1.00	51.31	GZ00	C
ATOM	6416	SG	CYS	X	197	−27.349	116.579	−23.083	1.00	51.29	GZ00	S
ATOM	6417	N	GLN	X	198	−24.716	116.655	−25.704	1.00	49.43	GZ00	N
ATOM	6418	CA	GLN	X	198	−24.668	115.979	−26.996	1.00	53.99	GZ00	C
ATOM	6419	C	GLN	X	198	−25.193	114.555	−26.839	1.00	53.90	GZ00	C
ATOM	6420	O	GLN	X	198	−24.579	113.736	−26.139	1.00	49.13	GZ00	O
ATOM	6421	CB	GLN	X	198	−23.245	115.967	−27.554	1.00	51.29	GZ00	C
ATOM	6422	CG	GLN	X	198	−22.782	117.315	−28.078	1.00	67.46	GZ00	C
ATOM	6423	CD	GLN	X	198	−21.293	117.357	−28.388	1.00	69.14	GZ00	C
ATOM	6424	OE1	GLN	X	198	−20.565	116.404	−28.128	1.00	72.78	GZ00	O
ATOM	6425	NE2	GLN	X	198	−20.838	118.470	−28.943	1.00	73.70	GZ00	N
ATOM	6426	N	VAL	X	199	−26.299	114.256	−27.519	1.00	45.97	GZ00	N
ATOM	6427	CA	VAL	X	199	−26.970	112.961	−27.422	1.00	47.62	GZ00	C
ATOM	6428	C	VAL	X	199	−26.780	112.222	−28.743	1.00	49.39	GZ00	C
ATOM	6429	O	VAL	X	199	−27.294	112.648	−29.786	1.00	43.67	GZ00	O
ATOM	6430	CB	VAL	X	199	−28.465	113.117	−27.091	1.00	38.03	GZ00	C
ATOM	6431	CG1	VAL	X	199	−29.116	111.753	−26.854	1.00	36.64	GZ00	C
ATOM	6432	CG2	VAL	X	199	−28.642	114.009	−25.881	1.00	43.16	GZ00	C
ATOM	6433	N	THR	X	200	−26.069	111.100	−28.699	1.00	44.37	GZ00	N
ATOM	6434	CA	THR	X	200	−25.870	110.288	−29.888	1.00	47.13	GZ00	C
ATOM	6435	C	THR	X	200	−26.837	109.107	−29.884	1.00	46.93	GZ00	C
ATOM	6436	O	THR	X	200	−26.959	108.389	−28.886	1.00	37.31	GZ00	O
ATOM	6437	CB	THR	X	200	−24.426	109.819	−29.990	1.00	47.07	GZ00	C
ATOM	6438	OG1	THR	X	200	−23.583	110.975	−30.046	1.00	49.61	GZ00	O
ATOM	6439	CG2	THR	X	200	−24.222	108.955	−31.246	1.00	48.16	GZ00	C
ATOM	6440	N	HIS	X	201	−27.533	108.936	−31.002	1.00	40.95	GZ00	N
ATOM	6441	CA	HIS	X	201	−28.533	107.899	−31.163	1.00	45.21	GZ00	C
ATOM	6442	C	HIS	X	201	−28.414	107.309	−32.559	1.00	45.62	GZ00	C
ATOM	6443	O	HIS	X	201	−28.609	108.023	−33.549	1.00	41.52	GZ00	O
ATOM	6444	CB	HIS	X	201	−29.928	108.468	−30.953	1.00	37.81	GZ00	C
ATOM	6445	CG	HIS	X	201	−31.009	107.472	−31.174	1.00	40.25	GZ00	C
ATOM	6446	ND1	HIS	X	201	−31.717	107.395	−32.354	1.00	39.48	GZ00	N
ATOM	6447	CD2	HIS	X	201	−31.492	106.492	−30.372	1.00	32.60	GZ00	C
ATOM	6448	CE1	HIS	X	201	−32.614	106.425	−32.257	1.00	41.48	GZ00	C
ATOM	6449	NE2	HIS	X	201	−32.500	105.865	−31.063	1.00	36.04	GZ00	N
ATOM	6450	N	GLU	X	202	−28.100	106.014	−32.636	1.00	40.07	GZ00	N
ATOM	6451	CA	GLU	X	202	−27.996	105.307	−33.916	1.00	39.77	GZ00	C
ATOM	6452	C	GLU	X	202	−27.068	106.042	−34.889	1.00	44.82	GZ00	C
ATOM	6453	O	GLU	X	202	−27.387	106.247	−36.062	1.00	40.88	GZ00	O
ATOM	6454	CB	GLU	X	202	−29.376	105.095	−34.535	1.00	36.52	GZ00	C
ATOM	6455	CG	GLU	X	202	−30.307	104.272	−33.669	1.00	41.95	GZ00	C
ATOM	6456	CD	GLU	X	202	−29.852	102.821	−33.573	1.00	51.67	GZ00	C
ATOM	6457	OE1	GLU	X	202	−29.603	102.188	−34.631	1.00	51.18	GZ00	O
ATOM	6458	OE2	GLU	X	202	−29.735	102.316	−32.433	1.00	49.62	GZ00	O1−
ATOM	6459	N	GLY	X	203	−25.911	106.464	−34.381	1.00	41.22	GZ00	N
ATOM	6460	CA	GLY	X	203	−24.926	107.146	−35.193	1.00	42.73	GZ00	C
ATOM	6461	C	GLY	X	203	−25.235	108.578	−35.586	1.00	47.72	GZ00	C
ATOM	6462	O	GLY	X	203	−24.445	109.169	−36.321	1.00	53.27	GZ00	O
ATOM	6463	N	SER	X	206	−26.322	109.176	−35.101	1.00	52.11	GZ00	N
ATOM	6464	CA	SER	X	206	−26.642	110.577	−35.375	1.00	50.86	GZ00	C
ATOM	6465	C	SER	X	206	−26.773	111.328	−34.056	1.00	52.21	GZ00	C
ATOM	6466	O	SER	X	206	−27.448	110.853	−33.136	1.00	52.48	GZ00	O
ATOM	6467	CB	SER	X	206	−27.944	110.707	−36.167	1.00	47.57	GZ00	C
ATOM	6468	OG	SER	X	206	−27.838	110.125	−37.454	1.00	59.00	GZ00	O
ATOM	6469	N	THR	X	207	−26.128	112.488	−33.953	1.00	50.76	GZ00	N
ATOM	6470	CA	THR	X	207	−26.108	113.241	−32.704	1.00	55.87	GZ00	C
ATOM	6471	C	THR	X	207	−27.025	114.462	−32.764	1.00	57.12	GZ00	C
ATOM	6472	O	THR	X	207	−27.074	115.180	−33.767	1.00	57.64	GZ00	O
ATOM	6473	CB	THR	X	207	−24.696	113.690	−32.344	1.00	48.26	GZ00	C
ATOM	6474	OG1	THR	X	207	−24.359	114.813	−33.157	1.00	73.99	GZ00	O
ATOM	6475	CG2	THR	X	207	−23.702	112.580	−32.600	1.00	47.46	GZ00	C
ATOM	6476	N	VAL	X	208	−27.777	114.659	−31.690	1.00	49.79	GZ00	N
ATOM	6477	CA	VAL	X	208	−28.598	115.842	−31.472	1.00	52.71	GZ00	C
ATOM	6478	C	VAL	X	208	−27.951	116.636	−30.343	1.00	55.59	GZ00	C
ATOM	6479	O	VAL	X	208	−27.557	116.063	−29.317	1.00	52.08	GZ00	O
ATOM	6480	CB	VAL	X	208	−30.047	115.452	−31.131	1.00	51.79	GZ00	C
ATOM	6481	CG1	VAL	X	208	−30.880	116.672	−30.802	1.00	49.77	GZ00	C
ATOM	6482	CG2	VAL	X	208	−30.666	114.651	−32.276	1.00	48.08	GZ00	C
ATOM	6483	N	GLU	X	209	−27.787	117.939	−30.547	1.00	56.25	GZ00	N
ATOM	6484	CA	GLU	X	209	−27.107	118.778	−29.571	1.00	56.90	GZ00	C
ATOM	6485	C	GLU	X	209	−27.976	119.957	−29.174	1.00	58.39	GZ00	C
ATOM	6486	O	GLU	X	209	−28.692	120.525	−30.005	1.00	55.14	GZ00	O
ATOM	6487	CB	GLU	X	209	−25.772	119.293	−30.087	1.00	57.63	GZ00	C
ATOM	6488	CG	GLU	X	209	−25.088	120.229	−29.113	1.00	64.92	GZ00	C
ATOM	6489	CD	GLU	X	209	−23.766	120.754	−29.630	1.00	76.32	GZ00	C
ATOM	6490	OE1	GLU	X	209	−22.869	119.942	−29.932	1.00	78.95	GZ00	O
ATOM	6491	OE2	GLU	X	209	−23.636	121.986	−29.766	1.00	85.57	GZ00	O1−
ATOM	6492	N	LYS	X	210	−27.935	120.282	−27.886	1.00	62.74	GZ00	N
ATOM	6493	CA	LYS	X	210	−28.467	121.522	−27.345	1.00	53.79	GZ00	C
ATOM	6494	C	LYS	X	210	−27.379	122.171	−26.505	1.00	56.56	GZ00	C
ATOM	6495	O	LYS	X	210	−26.616	121.476	−25.823	1.00	56.28	GZ00	O
ATOM	6496	CB	LYS	X	210	−29.711	121.279	−26.513	1.00	53.44	GZ00	C
ATOM	6497	CG	LYS	X	210	−30.907	120.841	−27.324	1.00	54.02	GZ00	C
ATOM	6498	CD	LYS	X	210	−31.098	121.748	−28.509	1.00	54.29	GZ00	C
ATOM	6499	CE	LYS	X	210	−32.343	121.367	−29.282	1.00	55.10	GZ00	C
ATOM	6500	NZ	LYS	X	210	−33.545	121.832	−28.528	1.00	61.72	GZ00	N1+
ATOM	6501	N	THR	X	211	−27.270	123.498	−26.592	1.00	59.32	GZ00	N
ATOM	6502	CA	THR	X	211	−26.267	124.229	−25.828	1.00	59.32	GZ00	C
ATOM	6503	C	THR	X	211	−26.946	125.341	−25.039	1.00	55.85	GZ00	C
ATOM	6504	O	THR	X	211	−27.984	125.869	−25.443	1.00	52.37	GZ00	O
ATOM	6505	CB	THR	X	211	−25.177	124.830	−26.725	1.00	59.58	GZ00	C
ATOM	6506	OG1	THR	X	211	−25.586	126.134	−27.141	1.00	68.27	GZ00	O
ATOM	6507	CG2	THR	X	211	−24.975	123.970	−27.975	1.00	57.88	GZ00	C
ATOM	6508	N	VAL	X	212	−26.348	125.706	−23.911	1.00	52.69	GZ00	N
ATOM	6509	CA	VAL	X	212	−26.936	126.709	−23.035	1.00	63.41	GZ00	C
ATOM	6510	C	VAL	X	212	−25.825	127.640	−22.548	1.00	67.46	GZ00	C
ATOM	6511	O	VAL	X	212	−24.665	127.233	−22.408	1.00	65.23	GZ00	O
ATOM	6512	CB	VAL	X	212	−27.702	126.029	−21.866	1.00	57.88	GZ00	C
ATOM	6513	CG1	VAL	X	212	−26.783	125.712	−20.700	1.00	44.64	GZ00	C
ATOM	6514	CG2	VAL	X	212	−28.897	126.846	−21.442	1.00	65.99	GZ00	C
ATOM	6515	N	ALA	X	213	−26.174	128.916	−22.332	1.00	65.82	GZ00	N
ATOM	6516	CA	ALA	X	213	−25.166	129.919	−21.988	1.00	71.28	GZ00	C
ATOM	6517	C	ALA	X	213	−25.503	130.667	−20.702	1.00	73.86	GZ00	C
ATOM	6518	O	ALA	X	213	−26.677	130.982	−20.445	1.00	75.77	GZ00	O
ATOM	6519	CB	ALA	X	213	−25.003	130.928	−23.133	1.00	69.34	GZ00	C
ATOM	6520	N	PRO	X	214	−24.486	130.994	−19.889	1.00	70.92	GZ00	N
ATOM	6521	CA	PRO	X	214	−24.746	131.692	−18.614	1.00	72.76	GZ00	C
ATOM	6522	C	PRO	X	214	−25.314	133.090	−18.773	1.00	82.62	GZ00	C
ATOM	6523	O	PRO	X	214	−25.933	133.596	−17.827	1.00	89.01	GZ00	O
ATOM	6524	CB	PRO	X	214	−23.366	131.732	−17.943	1.00	66.71	GZ00	C
ATOM	6525	CG	PRO	X	214	−22.637	130.585	−18.525	1.00	65.72	GZ00	C
ATOM	6526	CD	PRO	X	214	−23.119	130.445	−19.944	1.00	70.60	GZ00	C
ATOM	6527	N	THR	X	215	−25.149	133.725	−19.928	1.00	84.77	GZ00	N
ATOM	6528	CA	THR	X	215	−25.832	134.986	−20.202	1.00	96.30	GZ00	C
ATOM	6529	C	THR	X	215	−27.332	134.702	−20.252	1.00	95.28	GZ00	C
ATOM	6530	O	THR	X	215	−27.859	134.231	−21.265	1.00	91.48	GZ00	O
ATOM	6531	CB	THR	X	215	−25.328	135.593	−21.510	1.00	97.14	GZ00	C
ATOM	6532	OG1	THR	X	215	−25.743	134.773	−22.612	1.00	87.67	GZ00	O
ATOM	6533	CG2	THR	X	215	−23.793	135.691	−21.507	1.00	90.01	GZ00	C
ATOM	6534	N	GLU	X	216	−28.027	134.994	−19.152	1.00	96.06	GZ00	N
ATOM	6535	CA	GLU	X	216	−29.446	134.662	−19.010	1.00	98.88	GZ00	C
ATOM	6536	C	GLU	X	216	−30.325	135.917	−18.923	1.00	99.86	GZ00	C
ATOM	6537	O	GLU	X	216	−31.553	135.830	−18.821	1.00	94.58	GZ00	O
ATOM	6538	CB	GLU	X	216	−29.662	133.791	−17.762	1.00	104.37	GZ00	C
ATOM	6539	CG	GLU	X	216	−29.007	132.394	−17.811	1.00	103.51	GZ00	C
ATOM	6540	CD	GLU	X	216	−29.281	131.561	−16.556	1.00	100.31	GZ00	C
ATOM	6541	OE1	GLU	X	216	−30.463	131.201	−16.329	1.00	98.05	GZ00	O
ATOM	6542	OE2	GLU	X	216	−28.323	131.288	−15.788	1.00	94.94	GZ00	O1−
TER
ATOM	6543	N	THR	E	152	−7.503	113.907	0.585	1.00	78.03	B000	N
ATOM	6544	CA	THR	E	152	−7.804	113.632	1.990	1.00	91.98	B000	C
ATOM	6545	C	THR	E	152	−6.989	112.446	2.537	1.00	87.18	B000	C
ATOM	6546	O	THR	E	152	−5.914	112.642	3.113	1.00	87.17	B000	O
ATOM	6547	CB	THR	E	152	−9.331	113.377	2.199	1.00	99.46	B000	C
ATOM	6548	OG1	THR	E	152	−9.547	112.614	3.396	1.00	103.56	B000	O
ATOM	6549	CG2	THR	E	152	−9.959	112.661	0.997	1.00	88.04	B000	C
ATOM	6550	N	CYS	E	153	−7.511	111.230	2.378	1.00	83.15	B000	N
ATOM	6551	CA	CYS	E	153	−6.804	109.997	2.699	1.00	86.88	B000	C
ATOM	6552	C	CYS	E	153	−6.722	109.106	1.463	1.00	80.76	B000	C
ATOM	6553	O	CYS	E	153	−7.463	109.278	0.486	1.00	71.27	B000	O
ATOM	6554	CB	CYS	E	153	−7.471	109.227	3.860	1.00	86.61	B000	C
ATOM	6555	SG	CYS	E	153	−6.738	109.471	5.513	1.00	90.81	B000	S
ATOM	6556	N	CYS	E	154	−5.817	108.133	1.525	1.00	72.71	B000	N
ATOM	6557	CA	CYS	E	154	−5.632	107.218	0.411	1.00	64.86	B000	C
ATOM	6558	C	CYS	E	154	−6.850	106.311	0.243	1.00	66.48	B000	C
ATOM	6559	O	CYS	E	154	−7.564	106.023	1.210	1.00	66.73	B000	O
ATOM	6560	CB	CYS	E	154	−4.385	106.373	0.626	1.00	57.69	B000	C
ATOM	6561	SG	CYS	E	154	−2.833	107.296	0.371	1.00	72.69	B000	S
ATOM	6562	N	PRO	E	155	−7.115	105.854	−0.978	1.00	56.60	B000	N
ATOM	6563	CA	PRO	E	155	−8.220	104.914	−1.192	1.00	57.19	B000	C
ATOM	6564	C	PRO	E	155	−8.052	103.661	−0.345	1.00	62.02	B000	C
ATOM	6565	O	PRO	E	155	−7.012	103.404	0.267	1.00	60.28	B000	O
ATOM	6566	CB	PRO	E	155	−8.143	104.589	−2.687	1.00	52.85	B000	C
ATOM	6567	CG	PRO	E	155	−7.332	105.677	−3.277	1.00	56.95	B000	C
ATOM	6568	CD	PRO	E	155	−6.392	106.158	−2.220	1.00	54.57	B000	C
ATOM	6569	N	VAL	E	156	−9.123	102.871	−0.306	1.00	64.34	B000	N
ATOM	6570	CA	VAL	E	156	−9.121	101.644	0.477	1.00	62.48	B000	C
ATOM	6571	C	VAL	E	156	−8.013	100.726	−0.021	1.00	57.31	B000	C
ATOM	6572	O	VAL	E	156	−7.843	100.536	−1.235	1.00	55.79	B000	O
ATOM	6573	CB	VAL	E	156	−10.498	100.968	0.373	1.00	58.69	B000	C
ATOM	6574	CG1	VAL	E	156	−10.628	99.853	1.400	1.00	62.99	B000	C
ATOM	6575	CG2	VAL	E	156	−11.612	102.013	0.508	1.00	72.16	B000	C
ATOM	6576	N	ASN	E	157	−7.244	100.163	0.915	1.00	49.37	B000	N
ATOM	6577	CA	ASN	E	157	−6.142	99.218	0.687	1.00	55.22	B000	C
ATOM	6578	C	ASN	E	157	−4.871	99.882	0.162	1.00	52.64	B000	C
ATOM	6579	O	ASN	E	157	−3.871	99.180	−0.036	1.00	49.46	B000	O
ATOM	6580	CB	ASN	E	157	−6.513	98.075	−0.276	1.00	51.75	B000	C
ATOM	6581	CG	ASN	E	157	−7.713	97.282	0.202	1.00	58.73	B000	C
ATOM	6582	OD1	ASN	E	157	−7.839	97.001	1.392	1.00	60.67	B000	O
ATOM	6583	ND2	ASN	E	157	−8.609	96.935	−0.720	1.00	58.30	B000	N
ATOM	6584	N	TRP	E	158	−4.868	101.187	−0.082	1.00	49.22	B000	N
ATOM	6585	CA	TRP	E	158	−3.644	101.885	−0.433	1.00	45.78	B000	C
ATOM	6586	C	TRP	E	158	−2.983	102.464	0.818	1.00	47.63	B000	C
ATOM	6587	O	TRP	E	158	−3.618	102.655	1.855	1.00	53.96	B000	O
ATOM	6588	CB	TRP	E	158	−3.933	102.979	−1.453	1.00	48.76	B000	C
ATOM	6589	CG	TRP	E	158	−4.381	102.473	−2.793	1.00	40.31	B000	C
ATOM	6590	CD1	TRP	E	158	−5.498	101.731	−3.072	1.00	46.46	B000	C
ATOM	6591	CD2	TRP	E	158	−3.718	102.683	−4.043	1.00	35.79	B000	C
ATOM	6592	NE1	TRP	E	158	−5.573	101.465	−4.432	1.00	39.86	B000	N
ATOM	6593	CE2	TRP	E	158	−4.495	102.050	−5.047	1.00	45.74	B000	C
ATOM	6594	CE3	TRP	E	158	−2.548	103.355	−4.417	1.00	40.22	B000	C
ATOM	6595	CZ2	TRP	E	158	−4.132	102.067	−6.395	1.00	41.97	B000	C
ATOM	6596	CZ3	TRP	E	158	−2.193	103.378	−5.764	1.00	41.46	B000	C
ATOM	6597	CH2	TRP	E	158	−2.980	102.727	−6.732	1.00	40.39	B000	C
ATOM	6598	N	VAL	E	159	−1.689	102.734	0.702	1.00	44.22	B000	N
ATOM	6599	CA	VAL	E	159	−0.837	103.172	1.800	1.00	48.43	B000	C
ATOM	6600	C	VAL	E	159	−0.297	104.558	1.461	1.00	58.07	B000	C
ATOM	6601	O	VAL	E	159	0.103	104.818	0.318	1.00	55.09	B000	O
ATOM	6602	CB	VAL	E	159	0.330	102.189	2.039	1.00	52.63	B000	C
ATOM	6603	CG1	VAL	E	159	1.251	102.704	3.126	1.00	54.92	B000	C
ATOM	6604	CG2	VAL	E	159	−0.184	100.818	2.407	1.00	53.05	B000	C
ATOM	6605	N	GLU	E	160	−0.275	105.443	2.456	1.00	57.15	B000	N
ATOM	6606	CA	GLU	E	160	0.120	106.833	2.256	1.00	59.51	B000	C
ATOM	6607	C	GLU	E	160	1.577	107.054	2.654	1.00	55.30	B000	C
ATOM	6608	O	GLU	E	160	2.043	106.531	3.673	1.00	50.50	B000	O
ATOM	6609	CB	GLU	E	160	−0.809	107.756	3.046	1.00	51.43	B000	C
ATOM	6610	CG	GLU	E	160	−0.440	109.219	3.035	1.00	65.54	B000	C
ATOM	6611	CD	GLU	E	160	−1.336	110.058	3.952	1.00	77.96	B000	C
ATOM	6612	OE1	GLU	E	160	−2.418	109.568	4.357	1.00	79.30	B000	O
ATOM	6613	OE2	GLU	E	160	−0.951	111.203	4.281	1.00	75.66	B000	O1−
ATOM	6614	N	HIS	E	161	2.304	107.801	1.822	1.00	53.62	B000	N
ATOM	6615	CA	HIS	E	161	3.658	108.222	2.177	1.00	53.50	B000	C
ATOM	6616	C	HIS	E	161	4.013	109.474	1.393	1.00	61.66	B000	C
ATOM	6617	O	HIS	E	161	3.896	109.472	0.159	1.00	55.60	B000	O
ATOM	6618	CB	HIS	E	161	4.656	107.120	1.884	1.00	50.97	B000	C
ATOM	6619	CG	HIS	E	161	6.076	107.514	2.135	1.00	58.56	B000	C
ATOM	6620	ND1	HIS	E	161	6.845	108.173	1.196	1.00	62.19	B000	N
ATOM	6621	CD2	HIS	E	161	6.877	107.322	3.213	1.00	53.33	B000	C
ATOM	6622	CE1	HIS	E	161	8.056	108.376	1.687	1.00	63.04	B000	C
ATOM	6623	NE2	HIS	E	161	8.102	107.869	2.909	1.00	61.41	B000	N
ATOM	6624	N	GLU	E	162	4.410	110.541	2.112	1.00	61.25	B000	N
ATOM	6625	CA	GLU	E	162	4.767	111.850	1.561	1.00	55.02	B000	C
ATOM	6626	C	GLU	E	162	3.975	112.247	0.322	1.00	62.64	B000	C
ATOM	6627	O	GLU	E	162	4.537	112.301	−0.778	1.00	75.86	B000	O
ATOM	6628	CB	GLU	E	162	6.267	111.936	1.225	1.00	60.44	B000	C
ATOM	6629	CG	GLU	E	162	7.223	111.633	2.366	1.00	61.24	B000	C
ATOM	6630	CD	GLU	E	162	8.697	111.610	1.933	1.00	86.98	B000	C
ATOM	6631	OE1	GLU	E	162	9.025	111.099	0.822	1.00	83.67	B000	O
ATOM	6632	OE2	GLU	E	162	9.538	112.097	2.725	1.00	95.90	B000	O1−
ATOM	6633	N	ARG	E	163	2.679	112.496	0.469	1.00	55.87	B000	N
ATOM	6634	CA	ARG	E	163	1.819	113.000	−0.602	1.00	76.66	B000	C
ATOM	6635	C	ARG	E	163	1.554	112.012	−1.738	1.00	68.88	B000	C
ATOM	6636	O	ARG	E	163	0.922	112.388	−2.739	1.00	65.44	B000	O
ATOM	6637	CB	ARG	E	163	2.398	114.288	−1.215	1.00	89.70	B000	C
ATOM	6638	CG	ARG	E	163	2.928	115.328	−0.208	1.00	98.04	B000	C
ATOM	6639	CD	ARG	E	163	3.983	116.257	−0.835	1.00	106.40	B000	C
ATOM	6640	NE	ARG	E	163	3.452	117.044	−1.950	1.00	124.58	B000	N
ATOM	6641	CZ	ARG	E	163	3.588	116.723	−3.236	1.00	120.88	B000	C
ATOM	6642	NH1	ARG	E	163	4.245	115.622	−3.585	1.00	111.66	B000	N1+
ATOM	6643	NH2	ARG	E	163	3.063	117.503	−4.176	1.00	118.93	B000	N
ATOM	6644	N	SER	E	164	1.973	110.758	−1.622	1.00	63.49	B000	N
ATOM	6645	CA	SER	E	164	1.606	109.768	−2.620	1.00	57.22	B000	C
ATOM	6646	C	SER	E	164	0.888	108.601	−1.952	1.00	52.22	B000	C
ATOM	6647	O	SER	E	164	1.071	108.329	−0.761	1.00	49.98	B000	O
ATOM	6648	CB	SER	E	164	2.823	109.290	−3.411	1.00	56.71	B000	C
ATOM	6649	OG	SER	E	164	3.161	110.233	−4.411	1.00	65.04	B000	O
ATOM	6650	N	CYS	E	165	0.066	107.913	−2.740	1.00	50.88	B000	N
ATOM	6651	CA	CYS	E	165	−0.614	106.691	−2.322	1.00	53.42	B000	C
ATOM	6652	C	CYS	E	165	−0.042	105.497	−3.076	1.00	50.12	B000	C
ATOM	6653	O	CYS	E	165	0.124	105.555	−4.300	1.00	46.54	B000	O
ATOM	6654	CB	CYS	E	165	−2.118	106.793	−2.576	1.00	56.64	B000	C
ATOM	6655	SG	CYS	E	165	−2.945	108.028	−1.541	1.00	67.86	B000	S
ATOM	6656	N	TYR	E	166	0.226	104.410	−2.350	1.00	52.80	B000	N
ATOM	6657	CA	TYR	E	166	0.904	103.231	−2.882	1.00	48.23	B000	C
ATOM	6658	C	TYR	E	166	0.064	101.984	−2.650	1.00	48.96	B000	C
ATOM	6659	O	TYR	E	166	−0.538	101.821	−1.584	1.00	46.07	B000	O
ATOM	6660	CB	TYR	E	166	2.265	103.033	−2.222	1.00	45.49	B000	C
ATOM	6661	CG	TYR	E	166	3.196	104.186	−2.406	1.00	51.14	B000	C
ATOM	6662	CD1	TYR	E	166	3.000	105.382	−1.709	1.00	50.78	B000	C
ATOM	6663	CD2	TYR	E	166	4.296	104.081	−3.249	1.00	49.21	B000	C
ATOM	6664	CE1	TYR	E	166	3.859	106.442	−1.867	1.00	52.01	B000	C
ATOM	6665	CE2	TYR	E	166	5.175	105.138	−3.408	1.00	52.82	B000	C
ATOM	6666	CZ	TYR	E	166	4.954	106.317	−2.714	1.00	56.72	B000	C
ATOM	6667	OH	TYR	E	166	5.829	107.368	−2.874	1.00	55.75	B000	O
ATOM	6668	N	TRP	E	167	0.064	101.085	−3.634	1.00	43.75	B000	N
ATOM	6669	CA	TRP	E	167	−0.639	99.813	−3.539	1.00	41.16	B000	C
ATOM	6670	C	TRP	E	167	0.346	98.684	−3.794	1.00	42.24	B000	C
ATOM	6671	O	TRP	E	167	1.054	98.693	−4.804	1.00	37.42	B000	O
ATOM	6672	CB	TRP	E	167	−1.804	99.743	−4.530	1.00	42.53	B000	C
ATOM	6673	CG	TRP	E	167	−2.599	98.467	−4.395	1.00	46.44	B000	C
ATOM	6674	CD1	TRP	E	167	−3.662	98.242	−3.560	1.00	49.81	B000	C
ATOM	6675	CD2	TRP	E	167	−2.395	97.251	−5.116	1.00	43.13	B000	C
ATOM	6676	NE1	TRP	E	167	−4.114	96.955	−3.706	1.00	51.07	B000	N
ATOM	6677	CE2	TRP	E	167	−3.366	96.330	−4.665	1.00	46.50	B000	C
ATOM	6678	CE3	TRP	E	167	−1.491	96.852	−6.103	1.00	40.37	B000	C
ATOM	6679	CZ2	TRP	E	167	−3.455	95.041	−5.165	1.00	36.86	B000	C
ATOM	6680	CZ3	TRP	E	167	−1.587	95.579	−6.604	1.00	39.69	B000	C
ATOM	6681	CH2	TRP	E	167	−2.554	94.682	−6.133	1.00	42.15	B000	C
ATOM	6682	N	PHE	E	168	0.377	97.709	−2.891	1.00	42.39	B000	N
ATOM	6683	CA	PHE	E	168	1.369	96.645	−2.921	1.00	39.44	B000	C
ATOM	6684	C	PHE	E	168	0.718	95.320	−3.300	1.00	41.71	B000	C
ATOM	6685	O	PHE	E	168	−0.056	94.762	−2.515	1.00	39.56	B000	O
ATOM	6686	CB	PHE	E	168	2.054	96.539	−1.567	1.00	33.24	B000	C
ATOM	6687	CG	PHE	E	168	2.834	97.745	−1.209	1.00	45.15	B000	C
ATOM	6688	CD1	PHE	E	168	4.165	97.858	−1.603	1.00	43.49	B000	C
ATOM	6689	CD2	PHE	E	168	2.251	98.776	−0.472	1.00	43.18	B000	C
ATOM	6690	CE1	PHE	E	168	4.917	98.991	−1.279	1.00	48.63	B000	C
ATOM	6691	CE2	PHE	E	168	2.986	99.913	−0.135	1.00	49.01	B000	C
ATOM	6692	CZ	PHE	E	168	4.326	100.026	−0.541	1.00	48.19	B000	C
ATOM	6693	N	SER	E	169	1.081	94.788	−4.469	1.00	34.62	B000	N
ATOM	6694	CA	SER	E	169	0.586	93.478	−4.863	1.00	37.57	B000	C
ATOM	6695	C	SER	E	169	1.143	92.402	−3.936	1.00	34.54	B000	C
ATOM	6696	O	SER	E	169	2.169	92.574	−3.280	1.00	36.05	B000	O
ATOM	6697	CB	SER	E	169	0.978	93.141	−6.308	1.00	33.43	B000	C
ATOM	6698	OG	SER	E	169	2.306	92.629	−6.362	1.00	34.63	B000	O
ATOM	6699	N	ARG	E	170	0.449	91.272	−3.899	1.00	35.37	B000	N
ATOM	6700	CA	ARG	E	170	0.918	90.093	−3.184	1.00	37.90	B000	C
ATOM	6701	C	ARG	E	170	0.997	88.896	−4.131	1.00	35.62	B000	C
ATOM	6702	O	ARG	E	170	0.924	87.742	−3.715	1.00	37.12	B000	O
ATOM	6703	CB	ARG	E	170	0.028	89.827	−1.967	1.00	36.19	B000	C
ATOM	6704	CG	ARG	E	170	0.216	90.900	−0.870	1.00	40.70	B000	C
ATOM	6705	CD	ARG	E	170	−0.749	90.780	0.304	1.00	45.71	B000	C
ATOM	6706	NE	ARG	E	170	−2.082	91.308	−0.011	1.00	51.47	B000	N
ATOM	6707	CZ	ARG	E	170	−3.156	91.221	0.782	1.00	53.18	B000	C
ATOM	6708	NH1	ARG	E	170	−3.089	90.606	1.963	1.00	52.87	B000	N1+
ATOM	6709	NH2	ARG	E	170	−4.315	91.737	0.384	1.00	52.00	B000	N
ATOM	6710	N	SER	E	171	1.194	89.177	−5.414	1.00	34.01	B000	N
ATOM	6711	CA	SER	E	171	1.334	88.153	−6.435	1.00	37.47	B000	C
ATOM	6712	C	SER	E	171	2.092	88.761	−7.607	1.00	36.87	B000	C
ATOM	6713	O	SER	E	171	2.269	89.978	−7.692	1.00	35.85	B000	O
ATOM	6714	CB	SER	E	171	−0.030	87.625	−6.873	1.00	33.20	B000	C
ATOM	6715	OG	SER	E	171	−0.796	88.688	−7.418	1.00	38.78	B000	O
ATOM	6716	N	GLY	E	172	2.519	87.895	−8.521	1.00	30.60	B000	N
ATOM	6717	CA	GLY	E	172	3.411	88.281	−9.590	1.00	32.88	B000	C
ATOM	6718	C	GLY	E	172	2.710	88.558	−10.905	1.00	33.42	B000	C
ATOM	6719	O	GLY	E	172	1.628	88.050	−11.168	1.00	38.97	B000	O
ATOM	6720	N	LYS	E	173	3.360	89.389	−11.723	1.00	34.61	B000	N
ATOM	6721	CA	LYS	E	173	2.968	89.700	−13.090	1.00	31.95	B000	C
ATOM	6722	C	LYS	E	173	4.217	90.055	−13.875	1.00	32.50	B000	C
ATOM	6723	O	LYS	E	173	5.168	90.618	−13.327	1.00	29.30	B000	O
ATOM	6724	CB	LYS	E	173	1.999	90.887	−13.185	1.00	35.19	B000	C
ATOM	6725	CG	LYS	E	173	0.540	90.586	−12.876	1.00	36.71	B000	C
ATOM	6726	CD	LYS	E	173	−0.272	91.847	−13.150	1.00	36.28	B000	C
ATOM	6727	CE	LYS	E	173	−1.752	91.726	−12.775	1.00	37.38	B000	C
ATOM	6728	NZ	LYS	E	173	−2.515	90.874	−13.720	1.00	40.13	B000	N1+
ATOM	6729	N	ALA	E	174	4.199	89.739	−15.165	1.00	34.25	B000	N
ATOM	6730	CA	ALA	E	174	5.174	90.319	−16.074	1.00	31.99	B000	C
ATOM	6731	C	ALA	E	174	5.058	91.834	−16.026	1.00	33.17	B000	C
ATOM	6732	O	ALA	E	174	3.962	92.387	−15.834	1.00	28.18	B000	O
ATOM	6733	CB	ALA	E	174	4.938	89.837	−17.503	1.00	26.95	B000	C
ATOM	6734	N	TRP	E	175	6.199	92.506	−16.231	1.00	27.62	B000	N
ATOM	6735	CA	TRP	E	175	6.257	93.962	−16.080	1.00	28.95	B000	C
ATOM	6736	C	TRP	E	175	5.178	94.667	−16.903	1.00	31.61	B000	C
ATOM	6737	O	TRP	E	175	4.487	95.560	−16.403	1.00	35.29	B000	O
ATOM	6738	CB	TRP	E	175	7.641	94.464	−16.472	1.00	34.77	B000	C
ATOM	6739	CG	TRP	E	175	7.893	95.874	−16.085	1.00	35.77	B000	C
ATOM	6740	CD1	TRP	E	175	8.505	96.308	−14.950	1.00	35.08	B000	C
ATOM	6741	CD2	TRP	E	175	7.574	97.046	−16.846	1.00	33.62	B000	C
ATOM	6742	NE1	TRP	E	175	8.582	97.688	−14.946	1.00	39.22	B000	N
ATOM	6743	CE2	TRP	E	175	8.021	98.164	−16.099	1.00	37.24	B000	C
ATOM	6744	CE3	TRP	E	175	6.965	97.259	−18.086	1.00	30.92	B000	C
ATOM	6745	CZ2	TRP	E	175	7.878	99.471	−16.550	1.00	34.67	B000	C
ATOM	6746	CZ3	TRP	E	175	6.812	98.559	−18.531	1.00	41.35	B000	C
ATOM	6747	CH2	TRP	E	175	7.273	99.651	−17.769	1.00	41.09	B000	C
ATOM	6748	N	ALA	E	176	5.003	94.268	−18.164	1.00	31.68	B000	N
ATOM	6749	CA	ALA	E	176	4.017	94.938	−19.011	1.00	34.92	B000	C
ATOM	6750	C	ALA	E	176	2.598	94.731	−18.504	1.00	42.84	B000	C
ATOM	6751	O	ALA	E	176	1.760	95.625	−18.637	1.00	44.50	B000	O
ATOM	6752	CB	ALA	E	176	4.121	94.464	−20.459	1.00	27.15	B000	C
ATOM	6753	N	ASP	E	177	2.296	93.569	−17.928	1.00	38.72	B000	N
ATOM	6754	CA	ASP	E	177	0.959	93.397	−17.376	1.00	38.20	B000	C
ATOM	6755	C	ASP	E	177	0.800	94.189	−16.085	1.00	37.56	B000	C
ATOM	6756	O	ASP	E	177	−0.277	94.742	−15.824	1.00	35.06	B000	O
ATOM	6757	CB	ASP	E	177	0.658	91.915	−17.144	1.00	38.76	B000	C
ATOM	6758	CG	ASP	E	177	0.524	91.144	−18.441	1.00	44.40	B000	C
ATOM	6759	OD1	ASP	E	177	−0.060	91.696	−19.397	1.00	46.46	B000	O
ATOM	6760	OD2	ASP	E	177	1.027	90.000	−18.513	1.00	46.19	B000	O1−
ATOM	6761	N	ALA	E	178	1.851	94.231	−15.255	1.00	34.06	B000	N
ATOM	6762	CA	ALA	E	178	1.810	95.046	−14.045	1.00	37.97	B000	C
ATOM	6763	C	ALA	E	178	1.710	96.521	−14.403	1.00	38.84	B000	C
ATOM	6764	O	ALA	E	178	1.028	97.294	−13.722	1.00	36.52	B000	O
ATOM	6765	CB	ALA	E	178	3.040	94.776	−13.174	1.00	36.54	B000	C
ATOM	6766	N	ASP	E	179	2.391	96.921	−15.471	1.00	38.85	B000	N
ATOM	6767	CA	ASP	E	179	2.284	98.283	−15.969	1.00	39.27	B000	C
ATOM	6768	C	ASP	E	179	0.840	98.610	−16.344	1.00	44.49	B000	C
ATOM	6769	O	ASP	E	179	0.287	99.630	−15.911	1.00	43.34	B000	O
ATOM	6770	CB	ASP	E	179	3.233	98.437	−17.155	1.00	41.76	B000	C
ATOM	6771	CG	ASP	E	179	3.180	99.817	−17.795	1.00	53.27	B000	C
ATOM	6772	OD1	ASP	E	179	3.353	100.836	−17.081	1.00	46.80	B000	O
ATOM	6773	OD2	ASP	E	179	2.980	99.863	−19.031	1.00	46.92	B000	O1−
ATOM	6774	N	ASN	E	180	0.193	97.723	−17.106	1.00	42.03	B000	N
ATOM	6775	CA	ASN	E	180	−1.199	97.957	−17.482	1.00	44.06	B000	C
ATOM	6776	C	ASN	E	180	−2.105	97.976	−16.261	1.00	47.76	B000	C
ATOM	6777	O	ASN	E	180	−3.071	98.746	−16.212	1.00	47.34	B000	O
ATOM	6778	CB	ASN	E	180	−1.687	96.905	−18.488	1.00	43.06	B000	C
ATOM	6779	CG	ASN	E	180	−1.015	97.046	−19.870	1.00	67.38	B000	C
ATOM	6780	OD1	ASN	E	180	−0.489	98.113	−20.216	1.00	70.80	B000	O
ATOM	6781	ND2	ASN	E	180	−1.053	95.971	−20.670	1.00	65.59	B000	N
ATOM	6782	N	TYR	E	181	−1.826	97.126	−15.271	1.00	39.12	B000	N
ATOM	6783	CA	TYR	E	181	−2.653	97.125	−14.068	1.00	43.01	B000	C
ATOM	6784	C	TYR	E	181	−2.651	98.498	−13.388	1.00	42.74	B000	C
ATOM	6785	O	TYR	E	181	−3.710	99.015	−13.016	1.00	42.29	B000	O
ATOM	6786	CB	TYR	E	181	−2.191	96.021	−13.109	1.00	37.06	B000	C
ATOM	6787	CG	TYR	E	181	−2.917	96.012	−11.794	1.00	38.21	B000	C
ATOM	6788	CD1	TYR	E	181	−2.558	96.897	−10.772	1.00	34.22	B000	C
ATOM	6789	CD2	TYR	E	181	−3.956	95.118	−11.558	1.00	37.19	B000	C
ATOM	6790	CE1	TYR	E	181	−3.234	96.912	−9.562	1.00	38.89	B000	C
ATOM	6791	CE2	TYR	E	181	−4.640	95.112	−10.337	1.00	36.01	B000	C
ATOM	6792	CZ	TYR	E	181	−4.276	96.010	−9.345	1.00	44.74	B000	C
ATOM	6793	OH	TYR	E	181	−4.927	95.998	−8.128	1.00	40.18	B000	O
ATOM	6794	N	CYS	E	182	−1.472	99.100	−13.203	1.00	38.84	B000	N
ATOM	6795	CA	CYS	E	182	−1.422	100.388	−12.511	1.00	45.63	B000	C
ATOM	6796	C	CYS	E	182	−2.149	101.467	−13.312	1.00	47.11	B000	C
ATOM	6797	O	CYS	E	182	−2.911	102.262	−12.747	1.00	44.58	B000	O
ATOM	6798	CB	CYS	E	182	0.031	100.804	−12.239	1.00	42.50	B000	C
ATOM	6799	SG	CYS	E	182	0.953	99.774	−11.010	1.00	49.37	B000	S
ATOM	6800	N	ARG	E	183	−1.957	101.483	−14.636	1.00	46.95	B000	N
ATOM	6801	CA	ARG	E	183	−2.612	102.478	−15.481	1.00	44.11	B000	C
ATOM	6802	C	ARG	E	183	−4.130	102.366	−15.394	1.00	50.00	B000	C
ATOM	6803	O	ARG	E	183	−4.833	103.386	−15.359	1.00	44.76	B000	O
ATOM	6804	CB	ARG	E	183	−2.113	102.348	−16.926	1.00	40.71	B000	C
ATOM	6805	CG	ARG	E	183	−0.821	103.153	−17.173	1.00	63.11	B000	C
ATOM	6806	CD	ARG	E	183	0.070	102.668	−18.340	1.00	66.43	B000	C
ATOM	6807	NE	ARG	E	183	1.428	103.228	−18.202	1.00	85.06	B000	N
ATOM	6808	CZ	ARG	E	183	2.473	102.943	−18.989	1.00	82.14	B000	C
ATOM	6809	NH1	ARG	E	183	2.333	102.088	−19.998	1.00	86.34	B000	N1+
ATOM	6810	NH2	ARG	E	183	3.667	103.501	−18.759	1.00	56.98	B000	N
ATOM	6811	N	LEU	E	184	−4.656	101.136	−15.327	1.00	45.91	B000	N
ATOM	6812	CA	LEU	E	184	−6.094	100.958	−15.156	1.00	43.34	B000	C
ATOM	6813	C	LEU	E	184	−6.575	101.442	−13.804	1.00	44.25	B000	C
ATOM	6814	O	LEU	E	184	−7.769	101.694	−13.646	1.00	51.06	B000	O
ATOM	6815	CB	LEU	E	184	−6.497	99.490	−15.302	1.00	47.73	B000	C
ATOM	6816	CG	LEU	E	184	−6.471	98.840	−16.680	1.00	54.62	B000	C
ATOM	6817	CD1	LEU	E	184	−6.890	97.380	−16.546	1.00	41.74	B000	C
ATOM	6818	CD2	LEU	E	184	−7.353	99.606	−17.678	1.00	43.16	B000	C
ATOM	6819	N	GLU	E	185	−5.685	101.579	−12.827	1.00	49.85	B000	N
ATOM	6820	CA	GLU	E	185	−6.032	102.169	−11.541	1.00	49.61	B000	C
ATOM	6821	C	GLU	E	185	−5.766	103.658	−11.502	1.00	48.64	B000	C
ATOM	6822	O	GLU	E	185	−5.704	104.233	−10.412	1.00	53.97	B000	O
ATOM	6823	CB	GLU	E	185	−5.258	101.484	−10.416	1.00	52.10	B000	C
ATOM	6824	CG	GLU	E	185	−5.516	100.002	−10.355	1.00	58.31	B000	C
ATOM	6825	CD	GLU	E	185	−6.899	99.698	−9.827	1.00	64.50	B000	C
ATOM	6826	OE1	GLU	E	185	−7.284	100.277	−8.780	1.00	62.30	B000	O
ATOM	6827	OE2	GLU	E	185	−7.614	98.911	−10.485	1.00	74.36	B000	O1−
ATOM	6828	N	ASP	E	186	−5.571	104.286	−12.662	1.00	44.48	B000	N
ATOM	6829	CA	ASP	E	186	−5.173	105.692	−12.731	1.00	54.36	B000	C
ATOM	6830	C	ASP	E	186	−3.929	105.951	−11.874	1.00	51.31	B000	C
ATOM	6831	O	ASP	E	186	−3.859	106.883	−11.069	1.00	57.99	B000	O
ATOM	6832	CB	ASP	E	186	−6.337	106.604	−12.332	1.00	56.91	B000	C
ATOM	6833	CG	ASP	E	186	−6.105	108.048	−12.733	1.00	74.54	B000	C
ATOM	6834	OD1	ASP	E	186	−5.482	108.279	−13.798	1.00	78.01	B000	O
ATOM	6835	OD2	ASP	E	186	−6.541	108.948	−11.982	1.00	75.17	B000	O1−
ATOM	6836	N	ALA	E	187	−2.940	105.083	−12.033	1.00	50.91	B000	N
ATOM	6837	CA	ALA	E	187	−1.713	105.165	−11.265	1.00	42.37	B000	C
ATOM	6838	C	ALA	E	187	−0.593	104.718	−12.183	1.00	37.72	B000	C
ATOM	6839	O	ALA	E	187	−0.810	104.469	−13.372	1.00	44.89	B000	O
ATOM	6840	CB	ALA	E	187	−1.820	104.332	−9.980	1.00	41.53	B000	C
ATOM	6841	N	HIS	E	188	0.612	104.603	−11.641	1.00	40.45	B000	N
ATOM	6842	CA	HIS	E	188	1.724	104.095	−12.422	1.00	40.26	B000	C
ATOM	6843	C	HIS	E	188	2.622	103.249	−11.526	1.00	42.46	B000	C
ATOM	6844	O	HIS	E	188	2.526	103.288	−10.296	1.00	40.81	B000	O
ATOM	6845	CB	HIS	E	188	2.499	105.237	−13.079	1.00	40.08	B000	C
ATOM	6846	CG	HIS	E	188	2.996	106.266	−12.107	1.00	47.93	B000	C
ATOM	6847	ND1	HIS	E	188	4.133	106.085	−11.346	1.00	46.18	B000	N
ATOM	6848	CD2	HIS	E	188	2.508	107.486	−11.772	1.00	40.80	B000	C
ATOM	6849	CE1	HIS	E	188	4.327	107.151	−10.587	1.00	51.18	B000	C
ATOM	6850	NE2	HIS	E	188	3.358	108.017	−10.829	1.00	50.42	B000	N
ATOM	6851	N	LEU	E	189	3.518	102.490	−12.157	1.00	37.36	B000	N
ATOM	6852	CA	LEU	E	189	4.459	101.686	−11.393	1.00	38.98	B000	C
ATOM	6853	C	LEU	E	189	5.384	102.583	−10.588	1.00	38.79	B000	C
ATOM	6854	O	LEU	E	189	5.766	103.663	−11.040	1.00	44.62	B000	O
ATOM	6855	CB	LEU	E	189	5.264	100.782	−12.324	1.00	42.15	B000	C
ATOM	6856	CG	LEU	E	189	4.561	99.535	−12.851	1.00	38.45	B000	C
ATOM	6857	CD1	LEU	E	189	5.376	98.948	−13.979	1.00	31.59	B000	C
ATOM	6858	CD2	LEU	E	189	4.384	98.533	−11.707	1.00	36.53	B000	C
ATOM	6859	N	VAL	E	190	5.742	102.130	−9.386	1.00	33.02	B000	N
ATOM	6860	CA	VAL	E	190	6.360	103.022	−8.410	1.00	37.67	B000	C
ATOM	6861	C	VAL	E	190	7.627	103.653	−8.977	1.00	41.59	B000	C
ATOM	6862	O	VAL	E	190	8.477	102.978	−9.571	1.00	39.37	B000	O
ATOM	6863	CB	VAL	E	190	6.626	102.274	−7.093	1.00	40.50	B000	C
ATOM	6864	CG1	VAL	E	190	7.570	101.068	−7.292	1.00	36.01	B000	C
ATOM	6865	CG2	VAL	E	190	7.216	103.229	−6.056	1.00	39.66	B000	C
ATOM	6866	N	VAL	E	191	7.751	104.967	−8.792	1.00	42.38	B000	N
ATOM	6867	CA	VAL	E	191	8.934	105.734	−9.169	1.00	38.93	B000	C
ATOM	6868	C	VAL	E	191	9.618	106.183	−7.886	1.00	41.89	B000	C
ATOM	6869	O	VAL	E	191	8.994	106.850	−7.054	1.00	49.00	B000	O
ATOM	6870	CB	VAL	E	191	8.569	106.923	−10.062	1.00	39.27	B000	C
ATOM	6871	CG1	VAL	E	191	9.802	107.734	−10.381	1.00	41.98	B000	C
ATOM	6872	CG2	VAL	E	191	7.920	106.410	−11.351	1.00	37.38	B000	C
ATOM	6873	N	VAL	E	192	10.885	105.796	−7.712	1.00	36.78	B000	N
ATOM	6874	CA	VAL	E	192	11.606	106.006	−6.456	1.00	43.13	B000	C
ATOM	6875	C	VAL	E	192	12.466	107.255	−6.601	1.00	46.90	B000	C
ATOM	6876	O	VAL	E	192	13.429	107.274	−7.375	1.00	45.02	B000	O
ATOM	6877	CB	VAL	E	192	12.459	104.793	−6.065	1.00	41.45	B000	C
ATOM	6878	CG1	VAL	E	192	13.073	105.013	−4.679	1.00	35.87	B000	C
ATOM	6879	CG2	VAL	E	192	11.618	103.512	−6.094	1.00	37.77	B000	C
ATOM	6880	N	THR	E	193	12.117	108.311	−5.870	1.00	47.21	B000	N
ATOM	6881	CA	THR	E	193	12.800	109.589	−6.012	1.00	54.54	B000	C
ATOM	6882	C	THR	E	193	13.689	109.963	−4.828	1.00	53.96	B000	C
ATOM	6883	O	THR	E	193	14.342	111.005	−4.886	1.00	57.35	B000	O
ATOM	6884	CB	THR	E	193	11.775	110.701	−6.279	1.00	47.81	B000	C
ATOM	6885	OG1	THR	E	193	10.889	110.829	−5.158	1.00	54.26	B000	O
ATOM	6886	CG2	THR	E	193	10.954	110.359	−7.522	1.00	49.33	B000	C
ATOM	6887	N	SER	E	194	13.765	109.142	−3.779	1.00	50.25	B000	N
ATOM	6888	CA	SER	E	194	14.493	109.535	−2.577	1.00	47.10	B000	C
ATOM	6889	C	SER	E	194	14.737	108.321	−1.701	1.00	54.45	B000	C
ATOM	6890	O	SER	E	194	14.097	107.277	−1.857	1.00	55.35	B000	O
ATOM	6891	CB	SER	E	194	13.727	110.596	−1.779	1.00	50.58	B000	C
ATOM	6892	OG	SER	E	194	12.588	110.027	−1.152	1.00	52.89	B000	O
ATOM	6893	N	TRP	E	195	15.656	108.488	−0.749	1.00	54.05	B000	N
ATOM	6894	CA	TRP	E	195	15.954	107.418	0.196	1.00	53.90	B000	C
ATOM	6895	C	TRP	E	195	14.742	107.048	1.047	1.00	56.80	B000	C
ATOM	6896	O	TRP	E	195	14.512	105.862	1.323	1.00	53.39	B000	O
ATOM	6897	CB	TRP	E	195	17.124	107.822	1.086	1.00	52.43	B000	C
ATOM	6898	CG	TRP	E	195	18.407	107.331	0.552	1.00	62.39	B000	C
ATOM	6899	CD1	TRP	E	195	19.444	108.092	0.068	1.00	63.42	B000	C
ATOM	6900	CD2	TRP	E	195	18.804	105.965	0.402	1.00	65.61	B000	C
ATOM	6901	NE1	TRP	E	195	20.464	107.278	−0.362	1.00	65.18	B000	N
ATOM	6902	CE2	TRP	E	195	20.100	105.969	−0.170	1.00	69.72	B000	C
ATOM	6903	CE3	TRP	E	195	18.199	104.739	0.703	1.00	59.71	B000	C
ATOM	6904	CZ2	TRP	E	195	20.797	104.792	−0.447	1.00	59.79	B000	C
ATOM	6905	CZ3	TRP	E	195	18.890	103.571	0.425	1.00	54.31	B000	C
ATOM	6906	CH2	TRP	E	195	20.174	103.605	−0.142	1.00	59.74	B000	C
ATOM	6907	N	GLU	E	196	13.961	108.038	1.487	1.00	55.10	B000	N
ATOM	6908	CA	GLU	E	196	12.781	107.723	2.292	1.00	58.29	B000	C
ATOM	6909	C	GLU	E	196	11.786	106.895	1.505	1.00	53.21	B000	C
ATOM	6910	O	GLU	E	196	11.299	105.874	1.999	1.00	56.81	B000	O
ATOM	6911	CB	GLU	E	196	12.127	108.987	2.849	1.00	67.43	B000	C
ATOM	6912	CG	GLU	E	196	12.825	109.494	4.092	1.00	75.36	B000	C
ATOM	6913	CD	GLU	E	196	14.139	110.132	3.758	1.00	90.49	B000	C
ATOM	6914	OE1	GLU	E	196	14.259	110.606	2.610	1.00	89.70	B000	O
ATOM	6915	OE2	GLU	E	196	15.055	110.128	4.613	1.00	94.74	B000	O1−
ATOM	6916	N	GLU	E	197	11.460	107.326	0.281	1.00	51.77	B000	N
ATOM	6917	CA	GLU	E	197	10.589	106.525	−0.570	1.00	52.50	B000	C
ATOM	6918	C	GLU	E	197	11.155	105.116	−0.740	1.00	51.92	B000	C
ATOM	6919	O	GLU	E	197	10.436	104.125	−0.567	1.00	48.95	B000	O
ATOM	6920	CB	GLU	E	197	10.376	107.217	−1.920	1.00	44.93	B000	C
ATOM	6921	CG	GLU	E	197	9.163	106.692	−2.685	1.00	46.53	B000	C
ATOM	6922	CD	GLU	E	197	8.827	107.482	−3.949	1.00	48.66	B000	C
ATOM	6923	OE1	GLU	E	197	9.651	108.313	−4.402	1.00	48.86	B000	O
ATOM	6924	OE2	GLU	E	197	7.727	107.257	−4.507	1.00	50.40	B000	O1−
ATOM	6925	N	GLN	E	198	12.462	105.006	−1.006	1.00	45.93	B000	N
ATOM	6926	CA	GLN	E	198	13.088	103.692	−1.102	1.00	44.41	B000	C
ATOM	6927	C	GLN	E	198	12.894	102.888	0.183	1.00	52.88	B000	C
ATOM	6928	O	GLN	E	198	12.542	101.701	0.145	1.00	50.74	B000	O
ATOM	6929	CB	GLN	E	198	14.572	103.831	−1.416	1.00	39.60	B000	C
ATOM	6930	CG	GLN	E	198	15.367	102.576	−1.148	1.00	36.79	B000	C
ATOM	6931	CD	GLN	E	198	15.210	101.541	−2.254	1.00	42.68	B000	C
ATOM	6932	OE1	GLN	E	198	14.942	101.881	−3.399	1.00	38.01	B000	O
ATOM	6933	NE2	GLN	E	198	15.359	100.273	−1.906	1.00	40.53	B000	N
ATOM	6934	N	LYS	E	199	13.135	103.512	1.337	1.00	51.74	B000	N
ATOM	6935	CA	LYS	E	199	13.004	102.770	2.587	1.00	50.49	B000	C
ATOM	6936	C	LYS	E	199	11.544	102.452	2.890	1.00	51.58	B000	C
ATOM	6937	O	LYS	E	199	11.242	101.379	3.427	1.00	48.97	B000	O
ATOM	6938	CB	LYS	E	199	13.670	103.539	3.731	1.00	53.77	B000	C
ATOM	6939	CG	LYS	E	199	15.157	103.755	3.500	1.00	55.44	B000	C
ATOM	6940	CD	LYS	E	199	15.992	103.547	4.755	1.00	75.31	B000	C
ATOM	6941	CE	LYS	E	199	17.390	104.165	4.583	1.00	85.03	B000	C
ATOM	6942	NZ	LYS	E	199	18.151	104.301	5.862	1.00	83.45	B000	N1+
ATOM	6943	N	PHE	E	200	10.631	103.358	2.531	1.00	48.81	B000	N
ATOM	6944	CA	PHE	E	200	9.204	103.098	2.691	1.00	48.98	B000	C
ATOM	6945	C	PHE	E	200	8.773	101.845	1.931	1.00	55.28	B000	C
ATOM	6946	O	PHE	E	200	8.032	101.010	2.465	1.00	54.84	B000	O
ATOM	6947	CB	PHE	E	200	8.406	104.312	2.224	1.00	46.91	B000	C
ATOM	6948	CG	PHE	E	200	6.965	104.034	2.006	1.00	50.71	B000	C
ATOM	6949	CD1	PHE	E	200	6.112	103.847	3.085	1.00	53.71	B000	C
ATOM	6950	CD2	PHE	E	200	6.449	103.965	0.722	1.00	51.62	B000	C
ATOM	6951	CE1	PHE	E	200	4.756	103.588	2.891	1.00	52.00	B000	C
ATOM	6952	CE2	PHE	E	200	5.097	103.710	0.512	1.00	50.54	B000	C
ATOM	6953	CZ	PHE	E	200	4.248	103.518	1.605	1.00	54.40	B000	C
ATOM	6954	N	VAL	E	201	9.229	101.697	0.680	1.00	51.49	B000	N
ATOM	6955	CA	VAL	E	201	8.826	100.553	−0.137	1.00	48.07	B000	C
ATOM	6956	C	VAL	E	201	9.420	99.254	0.413	1.00	49.06	B000	C
ATOM	6957	O	VAL	E	201	8.706	98.253	0.569	1.00	46.98	B000	O
ATOM	6958	CB	VAL	E	201	9.208	100.788	−1.611	1.00	46.66	B000	C
ATOM	6959	CG1	VAL	E	201	9.067	99.495	−2.434	1.00	41.41	B000	C
ATOM	6960	CG2	VAL	E	201	8.349	101.902	−2.212	1.00	37.70	B000	C
ATOM	6961	N	GLN	E	202	10.728	99.252	0.723	1.00	49.32	B000	N
ATOM	6962	CA	GLN	E	202	11.380	98.063	1.284	1.00	50.74	B000	C
ATOM	6963	C	GLN	E	202	10.622	97.528	2.481	1.00	51.55	B000	C
ATOM	6964	O	GLN	E	202	10.464	96.310	2.640	1.00	56.45	B000	O
ATOM	6965	CB	GLN	E	202	12.803	98.371	1.749	1.00	47.47	B000	C
ATOM	6966	CG	GLN	E	202	13.739	98.831	0.710	1.00	55.69	B000	C
ATOM	6967	CD	GLN	E	202	15.139	98.987	1.254	1.00	56.47	B000	C
ATOM	6968	OE1	GLN	E	202	15.907	99.831	0.790	1.00	57.62	B000	O
ATOM	6969	NE2	GLN	E	202	15.490	98.154	2.219	1.00	53.11	B000	N
ATOM	6970	N	HIS	E	203	10.189	98.433	3.360	1.00	51.67	B000	N
ATOM	6971	CA	HIS	E	203	9.452	98.030	4.546	1.00	53.23	B000	C
ATOM	6972	C	HIS	E	203	8.230	97.215	4.173	1.00	58.75	B000	C
ATOM	6973	O	HIS	E	203	7.901	96.227	4.840	1.00	59.40	B000	O
ATOM	6974	CB	HIS	E	203	9.043	99.256	5.346	1.00	52.17	B000	C
ATOM	6975	CG	HIS	E	203	8.280	98.924	6.587	1.00	63.88	B000	C
ATOM	6976	ND1	HIS	E	203	6.924	99.142	6.710	1.00	66.92	B000	N
ATOM	6977	CD2	HIS	E	203	8.681	98.359	7.750	1.00	59.72	B000	C
ATOM	6978	CE1	HIS	E	203	6.525	98.741	7.904	1.00	64.58	B000	C
ATOM	6979	NE2	HIS	E	203	7.572	98.265	8.555	1.00	67.38	B000	N
ATOM	6980	N	HIS	E	204	7.548	97.609	3.105	1.00	51.87	B000	N
ATOM	6981	CA	HIS	E	204	6.320	96.930	2.742	1.00	47.42	B000	C
ATOM	6982	C	HIS	E	204	6.528	95.712	1.851	1.00	45.87	B000	C
ATOM	6983	O	HIS	E	204	5.734	94.781	1.934	1.00	46.13	B000	O
ATOM	6984	CB	HIS	E	204	5.375	97.925	2.086	1.00	43.64	B000	C
ATOM	6985	CG	HIS	E	204	4.761	98.864	3.071	1.00	55.52	B000	C
ATOM	6986	ND1	HIS	E	204	5.277	100.116	3.331	1.00	62.43	B000	N
ATOM	6987	CD2	HIS	E	204	3.719	98.703	3.917	1.00	51.63	B000	C
ATOM	6988	CE1	HIS	E	204	4.551	100.702	4.265	1.00	56.76	B000	C
ATOM	6989	NE2	HIS	E	204	3.598	99.867	4.634	1.00	58.19	B000	N
ATOM	6990	N	ILE	E	205	7.554	95.673	0.998	1.00	45.67	B000	N
ATOM	6991	CA	ILE	E	205	7.676	94.532	0.097	1.00	43.17	B000	C
ATOM	6992	C	ILE	E	205	8.408	93.363	0.749	1.00	43.69	B000	C
ATOM	6993	O	ILE	E	205	8.193	92.215	0.356	1.00	42.25	B000	O
ATOM	6994	CB	ILE	E	205	8.346	94.913	−1.235	1.00	39.71	B000	C
ATOM	6995	CG1	ILE	E	205	9.791	95.341	−1.023	1.00	34.62	B000	C
ATOM	6996	CG2	ILE	E	205	7.572	96.011	−1.954	1.00	32.37	B000	C
ATOM	6997	CD1	ILE	E	205	10.470	95.665	−2.317	1.00	33.57	B000	C
ATOM	6998	N	GLY	E	206	9.273	93.616	1.728	1.00	45.56	B000	N
ATOM	6999	CA	GLY	E	206	10.038	92.555	2.352	1.00	38.77	B000	C
ATOM	7000	C	GLY	E	206	11.058	91.943	1.409	1.00	45.53	B000	C
ATOM	7001	O	GLY	E	206	11.640	92.616	0.551	1.00	53.68	B000	O
ATOM	7002	N	PRO	E	207	11.268	90.646	1.525	1.00	41.49	B000	N
ATOM	7003	CA	PRO	E	207	12.312	89.995	0.720	1.00	48.79	B000	C
ATOM	7004	C	PRO	E	207	11.816	89.452	−0.616	1.00	39.32	B000	C
ATOM	7005	O	PRO	E	207	12.233	88.359	−0.999	1.00	49.37	B000	O
ATOM	7006	CB	PRO	E	207	12.736	88.837	1.624	1.00	42.37	B000	C
ATOM	7007	CG	PRO	E	207	11.386	88.411	2.205	1.00	39.72	B000	C
ATOM	7008	CD	PRO	E	207	10.597	89.687	2.422	1.00	38.72	B000	C
ATOM	7009	N	VAL	E	208	10.949	90.169	−1.333	1.00	40.46	B000	N
ATOM	7010	CA	VAL	E	208	10.315	89.659	−2.546	1.00	37.68	B000	C
ATOM	7011	C	VAL	E	208	10.706	90.542	−3.729	1.00	38.16	B000	C
ATOM	7012	O	VAL	E	208	10.561	91.767	−3.665	1.00	39.77	B000	O
ATOM	7013	CB	VAL	E	208	8.785	89.601	−2.383	1.00	40.03	B000	C
ATOM	7014	CG1	VAL	E	208	8.133	88.976	−3.608	1.00	32.03	B000	C
ATOM	7015	CG2	VAL	E	208	8.427	88.819	−1.106	1.00	41.62	B000	C
ATOM	7016	N	ASN	E	209	11.186	89.917	−4.812	1.00	35.17	B000	N
ATOM	7017	CA	ASN	E	209	11.506	90.657	−6.028	1.00	30.25	B000	C
ATOM	7018	C	ASN	E	209	10.268	91.389	−6.522	1.00	39.60	B000	C
ATOM	7019	O	ASN	E	209	9.189	90.792	−6.646	1.00	35.43	B000	O
ATOM	7020	CB	ASN	E	209	12.020	89.710	−7.105	1.00	33.04	B000	C
ATOM	7021	CG	ASN	E	209	13.430	89.196	−6.817	1.00	37.45	B000	C
ATOM	7022	OD1	ASN	E	209	14.282	89.914	−6.286	1.00	39.88	B000	O
ATOM	7023	ND2	ASN	E	209	13.676	87.948	−7.166	1.00	34.14	B000	N
ATOM	7024	N	THR	E	210	10.417	92.686	−6.801	1.00	32.18	B000	N
ATOM	7025	CA	THR	E	210	9.258	93.553	−6.998	1.00	34.27	B000	C
ATOM	7026	C	THR	E	210	9.571	94.589	−8.068	1.00	34.48	B000	C
ATOM	7027	O	THR	E	210	10.533	95.349	−7.932	1.00	31.68	B000	O
ATOM	7028	CB	THR	E	210	8.864	94.225	−5.667	1.00	33.37	B000	C
ATOM	7029	OG1	THR	E	210	8.661	93.210	−4.675	1.00	35.38	B000	O
ATOM	7030	CG2	THR	E	210	7.604	95.081	−5.789	1.00	26.61	B000	C
ATOM	7031	N	TRP	E	211	8.743	94.626	−9.112	1.00	29.97	B000	N
ATOM	7032	CA	TRP	E	211	8.933	95.562	−10.208	1.00	27.14	B000	C
ATOM	7033	C	TRP	E	211	8.801	97.006	−9.731	1.00	35.31	B000	C
ATOM	7034	O	TRP	E	211	7.981	97.316	−8.863	1.00	35.67	B000	O
ATOM	7035	CB	TRP	E	211	7.887	95.312	−11.297	1.00	30.90	B000	C
ATOM	7036	CG	TRP	E	211	8.066	94.071	−12.124	1.00	34.50	B000	C
ATOM	7037	CD1	TRP	E	211	7.104	93.138	−12.433	1.00	29.56	B000	C
ATOM	7038	CD2	TRP	E	211	9.267	93.640	−12.788	1.00	34.63	B000	C
ATOM	7039	NE1	TRP	E	211	7.630	92.160	−13.254	1.00	28.60	B000	N
ATOM	7040	CE2	TRP	E	211	8.955	92.439	−13.482	1.00	35.28	B000	C
ATOM	7041	CE3	TRP	E	211	10.575	94.146	−12.860	1.00	35.02	B000	C
ATOM	7042	CZ2	TRP	E	211	9.904	91.741	−14.231	1.00	29.26	B000	C
ATOM	7043	CZ3	TRP	E	211	11.518	93.452	−13.602	1.00	36.35	B000	C
ATOM	7044	CH2	TRP	E	211	11.177	92.251	−14.275	1.00	30.95	B000	C
ATOM	7045	N	MET	E	212	9.605	97.895	−10.316	1.00	32.55	B000	N
ATOM	7046	CA	MET	E	212	9.380	99.331	−10.239	1.00	29.40	B000	C
ATOM	7047	C	MET	E	212	9.191	99.869	−11.652	1.00	37.49	B000	C
ATOM	7048	O	MET	E	212	9.421	99.163	−12.641	1.00	33.69	B000	O
ATOM	7049	CB	MET	E	212	10.532	100.045	−9.538	1.00	32.77	B000	C
ATOM	7050	CG	MET	E	212	11.802	100.197	−10.374	1.00	37.02	B000	C
ATOM	7051	SD	MET	E	212	13.201	100.683	−9.319	1.00	36.83	B000	S
ATOM	7052	CE	MET	E	212	13.620	99.156	−8.467	1.00	32.94	B000	C
ATOM	7053	N	GLY	E	213	8.730	101.124	−11.741	1.00	37.19	B000	N
ATOM	7054	CA	GLY	E	213	8.440	101.761	−13.019	1.00	32.81	B000	C
ATOM	7055	C	GLY	E	213	9.662	102.269	−13.761	1.00	40.32	B000	C
ATOM	7056	O	GLY	E	213	9.719	103.432	−14.187	1.00	38.40	B000	O
ATOM	7057	N	LEU	E	214	10.634	101.380	−13.941	1.00	34.17	B000	N
ATOM	7058	CA	LEU	E	214	11.934	101.714	−14.503	1.00	39.27	B000	C
ATOM	7059	C	LEU	E	214	12.321	100.610	−15.473	1.00	39.76	B000	C
ATOM	7060	O	LEU	E	214	12.335	99.431	−15.100	1.00	41.29	B000	O
ATOM	7061	CB	LEU	E	214	12.988	101.877	−13.395	1.00	36.55	B000	C
ATOM	7062	CG	LEU	E	214	14.450	102.064	−13.797	1.00	42.98	B000	C
ATOM	7063	CD1	LEU	E	214	14.624	103.269	−14.744	1.00	38.04	B000	C
ATOM	7064	CD2	LEU	E	214	15.305	102.224	−12.529	1.00	37.75	B000	C
ATOM	7065	N	HIS	E	215	12.601	100.987	−16.718	1.00	36.19	B000	N
ATOM	7066	CA	HIS	E	215	12.875	100.024	−17.774	1.00	39.33	B000	C
ATOM	7067	C	HIS	E	215	13.746	100.691	−18.829	1.00	41.39	B000	C
ATOM	7068	O	HIS	E	215	13.843	101.921	−18.899	1.00	36.50	B000	O
ATOM	7069	CB	HIS	E	215	11.588	99.528	−18.420	1.00	37.31	B000	C
ATOM	7070	CG	HIS	E	215	10.877	100.605	−19.156	1.00	43.54	B000	C
ATOM	7071	ND1	HIS	E	215	10.975	100.759	−20.521	1.00	59.96	B000	N
ATOM	7072	CD2	HIS	E	215	10.149	101.654	−18.708	1.00	43.07	B000	C
ATOM	7073	CE1	HIS	E	215	10.292	101.830	−20.888	1.00	55.73	B000	C
ATOM	7074	NE2	HIS	E	215	9.780	102.387	−19.807	1.00	46.66	B000	N
ATOM	7075	N	ASP	E	216	14.341	99.858	−19.680	1.00	35.15	B000	N
ATOM	7076	CA	ASP	E	216	15.301	100.290	−20.686	1.00	39.15	B000	C
ATOM	7077	C	ASP	E	216	14.788	99.998	−22.085	1.00	42.63	B000	C
ATOM	7078	O	ASP	E	216	15.571	99.773	−23.004	1.00	42.03	B000	O
ATOM	7079	CB	ASP	E	216	16.648	99.600	−20.467	1.00	41.75	B000	C
ATOM	7080	CG	ASP	E	216	16.632	98.097	−20.849	1.00	44.42	B000	C
ATOM	7081	OD1	ASP	E	216	15.551	97.505	−21.130	1.00	37.16	B000	O
ATOM	7082	OD2	ASP	E	216	17.732	97.502	−20.848	1.00	43.61	B000	O1−
ATOM	7083	N	GLN	E	217	13.476	99.947	−22.253	1.00	46.29	B000	N
ATOM	7084	CA	GLN	E	217	12.991	99.214	−23.411	1.00	59.57	B000	C
ATOM	7085	C	GLN	E	217	13.208	99.957	−24.721	1.00	65.22	B000	C
ATOM	7086	O	GLN	E	217	13.083	99.331	−25.778	1.00	73.01	B000	O
ATOM	7087	CB	GLN	E	217	11.516	98.820	−23.200	1.00	62.75	B000	C
ATOM	7088	CG	GLN	E	217	11.375	97.683	−22.125	1.00	61.06	B000	C
ATOM	7089	CD	GLN	E	217	9.984	97.034	−22.070	1.00	67.45	B000	C
ATOM	7090	OE1	GLN	E	217	9.134	97.409	−21.253	1.00	58.29	B000	O
ATOM	7091	NE2	GLN	E	217	9.759	96.044	−22.936	1.00	73.72	B000	N
ATOM	7092	N	ASN	E	218	13.622	101.226	−24.688	1.00	54.85	B000	N
ATOM	7093	CA	ASN	E	218	14.065	101.896	−25.900	1.00	56.88	B000	C
ATOM	7094	C	ASN	E	218	15.579	101.999	−25.997	1.00	63.85	B000	C
ATOM	7095	O	ASN	E	218	16.099	102.476	−27.010	1.00	65.96	B000	O
ATOM	7096	CB	ASN	E	218	13.440	103.283	−25.982	1.00	68.65	B000	C
ATOM	7097	CG	ASN	E	218	11.988	103.230	−26.379	1.00	76.18	B000	C
ATOM	7098	OD1	ASN	E	218	11.117	103.732	−25.663	1.00	80.28	B000	O
ATOM	7099	ND2	ASN	E	218	11.710	102.603	−27.524	1.00	70.77	B000	N
ATOM	7100	N	GLY	E	219	16.294	101.546	−24.980	1.00	55.99	B000	N
ATOM	7101	CA	GLY	E	219	17.721	101.702	−24.908	1.00	47.24	B000	C
ATOM	7102	C	GLY	E	219	18.086	102.395	−23.615	1.00	46.37	B000	C
ATOM	7103	O	GLY	E	219	18.657	101.797	−22.697	1.00	45.37	B000	O
ATOM	7104	N	PRO	E	220	17.760	103.679	−23.515	1.00	47.23	B000	N
ATOM	7105	CA	PRO	E	220	18.027	104.396	−22.266	1.00	48.53	B000	C
ATOM	7106	C	PRO	E	220	17.055	103.993	−21.169	1.00	44.15	B000	C
ATOM	7107	O	PRO	E	220	15.875	103.736	−21.413	1.00	47.26	B000	O
ATOM	7108	CB	PRO	E	220	17.875	105.872	−22.658	1.00	43.34	B000	C
ATOM	7109	CG	PRO	E	220	17.055	105.868	−23.864	1.00	50.66	B000	C
ATOM	7110	CD	PRO	E	220	17.359	104.593	−24.598	1.00	46.49	B000	C
ATOM	7111	N	TRP	E	221	17.592	103.878	−19.961	1.00	41.42	B000	N
ATOM	7112	CA	TRP	E	221	16.767	103.695	−18.783	1.00	38.08	B000	C
ATOM	7113	C	TRP	E	221	15.871	104.916	−18.561	1.00	43.21	B000	C
ATOM	7114	O	TRP	E	221	16.325	106.062	−18.630	1.00	45.08	B000	O
ATOM	7115	CB	TRP	E	221	17.672	103.446	−17.577	1.00	37.90	B000	C
ATOM	7116	CG	TRP	E	221	18.256	102.057	−17.559	1.00	35.77	B000	C
ATOM	7117	CD1	TRP	E	221	19.520	101.683	−17.939	1.00	39.29	B000	C
ATOM	7118	CD2	TRP	E	221	17.586	100.853	−17.157	1.00	36.68	B000	C
ATOM	7119	NE1	TRP	E	221	19.676	100.323	−17.789	1.00	39.97	B000	N
ATOM	7120	CE2	TRP	E	221	18.501	99.790	−17.318	1.00	39.47	B000	C
ATOM	7121	CE3	TRP	E	221	16.296	100.571	−16.676	1.00	37.85	B000	C
ATOM	7122	CZ2	TRP	E	221	18.176	98.469	−16.997	1.00	34.61	B000	C
ATOM	7123	CZ3	TRP	E	221	15.970	99.246	−16.364	1.00	38.91	B000	C
ATOM	7124	CH2	TRP	E	221	16.909	98.220	−16.523	1.00	36.77	B000	C
ATOM	7125	N	LYS	E	222	14.591	104.666	−18.298	1.00	42.42	B000	N
ATOM	7126	CA	LYS	E	222	13.600	105.715	−18.110	1.00	45.91	B000	C
ATOM	7127	C	LYS	E	222	12.648	105.317	−16.994	1.00	49.90	B000	C
ATOM	7128	O	LYS	E	222	12.383	104.131	−16.772	1.00	45.80	B000	O
ATOM	7129	CB	LYS	E	222	12.766	105.968	−19.368	1.00	48.31	B000	C
ATOM	7130	CG	LYS	E	222	13.519	106.492	−20.561	1.00	57.72	B000	C
ATOM	7131	CD	LYS	E	222	12.640	106.357	−21.800	1.00	65.32	B000	C
ATOM	7132	CE	LYS	E	222	12.661	104.903	−22.305	1.00	75.88	B000	C
ATOM	7133	NZ	LYS	E	222	12.007	104.696	−23.635	1.00	76.97	B000	N1+
ATOM	7134	N	TRP	E	223	12.133	106.321	−16.298	1.00	47.14	B000	N
ATOM	7135	CA	TRP	E	223	11.031	106.134	−15.372	1.00	41.03	B000	C
ATOM	7136	C	TRP	E	223	9.714	106.314	−16.124	1.00	47.51	B000	C
ATOM	7137	O	TRP	E	223	9.617	107.117	−17.056	1.00	50.81	B000	O
ATOM	7138	CB	TRP	E	223	11.115	107.123	−14.218	1.00	39.77	B000	C
ATOM	7139	CG	TRP	E	223	12.293	106.912	−13.328	1.00	40.93	B000	C
ATOM	7140	CD1	TRP	E	223	13.467	107.621	−13.338	1.00	41.70	B000	C
ATOM	7141	CD2	TRP	E	223	12.410	105.957	−12.270	1.00	41.60	B000	C
ATOM	7142	NE1	TRP	E	223	14.311	107.148	−12.366	1.00	40.09	B000	N
ATOM	7143	CE2	TRP	E	223	13.688	106.129	−11.692	1.00	39.35	B000	C
ATOM	7144	CE3	TRP	E	223	11.561	104.962	−11.758	1.00	42.49	B000	C
ATOM	7145	CZ2	TRP	E	223	14.141	105.342	−10.627	1.00	38.41	B000	C
ATOM	7146	CZ3	TRP	E	223	12.010	104.183	−10.698	1.00	39.66	B000	C
ATOM	7147	CH2	TRP	E	223	13.291	104.374	−10.147	1.00	37.68	B000	C
ATOM	7148	N	VAL	E	224	8.693	105.555	−15.715	1.00	38.47	B000	N
ATOM	7149	CA	VAL	E	224	7.441	105.568	−16.467	1.00	44.59	B000	C
ATOM	7150	C	VAL	E	224	6.732	106.924	−16.423	1.00	46.85	B000	C
ATOM	7151	O	VAL	E	224	5.908	107.197	−17.298	1.00	50.06	B000	O
ATOM	7152	CB	VAL	E	224	6.487	104.458	−15.967	1.00	42.40	B000	C
ATOM	7153	CG1	VAL	E	224	7.059	103.070	−16.288	1.00	42.00	B000	C
ATOM	7154	CG2	VAL	E	224	6.227	104.600	−14.475	1.00	34.29	B000	C
ATOM	7155	N	ASP	E	225	7.017	107.790	−15.444	1.00	48.54	B000	N
ATOM	7156	CA	ASP	E	225	6.329	109.079	−15.338	1.00	53.13	B000	C
ATOM	7157	C	ASP	E	225	7.149	110.250	−15.865	1.00	51.10	B000	C
ATOM	7158	O	ASP	E	225	6.709	111.394	−15.749	1.00	47.62	B000	O
ATOM	7159	CB	ASP	E	225	5.898	109.358	−13.886	1.00	39.25	B000	C
ATOM	7160	CG	ASP	E	225	7.078	109.617	−12.948	1.00	49.56	B000	C
ATOM	7161	OD1	ASP	E	225	8.244	109.417	−13.352	1.00	47.55	B000	O
ATOM	7162	OD2	ASP	E	225	6.834	109.961	−11.767	1.00	55.28	B000	O1−
ATOM	7163	N	GLY	E	226	8.319	110.001	−16.449	1.00	50.70	B000	N
ATOM	7164	CA	GLY	E	226	9.118	111.058	−17.029	1.00	50.75	B000	C
ATOM	7165	C	GLY	E	226	10.206	111.608	−16.128	1.00	49.85	B000	C
ATOM	7166	O	GLY	E	226	11.083	112.321	−16.614	1.00	55.13	B000	O
ATOM	7167	N	THR	E	227	10.149	111.328	−14.832	1.00	46.51	B000	N
ATOM	7168	CA	THR	E	227	11.258	111.622	−13.942	1.00	42.53	B000	C
ATOM	7169	C	THR	E	227	12.579	111.301	−14.624	1.00	50.97	B000	C
ATOM	7170	O	THR	E	227	12.760	110.213	−15.178	1.00	57.64	B000	O
ATOM	7171	CB	THR	E	227	11.117	110.795	−12.667	1.00	48.55	B000	C
ATOM	7172	OG1	THR	E	227	9.834	111.037	−12.070	1.00	46.24	B000	O
ATOM	7173	CG2	THR	E	227	12.226	111.120	−11.690	1.00	41.66	B000	C
ATOM	7174	N	ASP	E	228	13.490	112.268	−14.601	1.00	59.03	B000	N
ATOM	7175	CA	ASP	E	228	14.770	112.131	−15.280	1.00	45.94	B000	C
ATOM	7176	C	ASP	E	228	15.624	111.088	−14.580	1.00	51.75	B000	C
ATOM	7177	O	ASP	E	228	15.872	111.182	−13.374	1.00	56.28	B000	O
ATOM	7178	CB	ASP	E	228	15.501	113.474	−15.311	1.00	47.30	B000	C
ATOM	7179	CG	ASP	E	228	16.845	113.379	−15.998	1.00	56.00	B000	C
ATOM	7180	OD1	ASP	E	228	16.859	113.296	−17.250	1.00	54.17	B000	O
ATOM	7181	OD2	ASP	E	228	17.881	113.348	−15.290	1.00	56.42	B000	O1−
ATOM	7182	N	TYR	E	229	16.112	110.114	−15.350	1.00	52.14	B000	N
ATOM	7183	CA	TYR	E	229	16.829	109.000	−14.743	1.00	46.06	B000	C
ATOM	7184	C	TYR	E	229	18.227	109.400	−14.287	1.00	47.79	B000	C
ATOM	7185	O	TYR	E	229	18.667	108.998	−13.201	1.00	47.55	B000	O
ATOM	7186	CB	TYR	E	229	16.901	107.830	−15.729	1.00	43.66	B000	C
ATOM	7187	CG	TYR	E	229	17.852	106.745	−15.304	1.00	42.09	B000	C
ATOM	7188	CD1	TYR	E	229	17.523	105.882	−14.269	1.00	38.14	B000	C
ATOM	7189	CD2	TYR	E	229	19.090	106.594	−15.917	1.00	42.41	B000	C
ATOM	7190	CE1	TYR	E	229	18.387	104.882	−13.864	1.00	40.35	B000	C
ATOM	7191	CE2	TYR	E	229	19.968	105.589	−15.517	1.00	46.35	B000	C
ATOM	7192	CZ	TYR	E	229	19.599	104.734	−14.486	1.00	46.45	B000	C
ATOM	7193	OH	TYR	E	229	20.450	103.738	−14.064	1.00	40.57	B000	O
ATOM	7194	N	GLU	E	230	18.954	110.170	−15.103	1.00	49.15	B000	N
ATOM	7195	CA	GLU	E	230	20.375	110.365	−14.821	1.00	46.97	B000	C
ATOM	7196	C	GLU	E	230	20.591	111.198	−13.556	1.00	51.12	B000	C
ATOM	7197	O	GLU	E	230	21.457	110.879	−12.738	1.00	53.36	B000	O
ATOM	7198	CB	GLU	E	230	21.082	110.992	−16.017	1.00	50.20	B000	C
ATOM	7199	CG	GLU	E	230	22.607	110.803	−15.963	1.00	63.82	B000	C
ATOM	7200	CD	GLU	E	230	23.021	109.363	−15.585	1.00	76.02	B000	C
ATOM	7201	OE1	GLU	E	230	22.553	108.396	−16.253	1.00	66.88	B000	O
ATOM	7202	OE2	GLU	E	230	23.821	109.201	−14.625	1.00	79.76	B000	O1−
ATOM	7203	N	THR	E	231	19.809	112.248	−13.359	1.00	48.10	B000	N
ATOM	7204	CA	THR	E	231	19.981	113.081	−12.176	1.00	56.05	B000	C
ATOM	7205	C	THR	E	231	19.161	112.602	−10.988	1.00	60.28	B000	C
ATOM	7206	O	THR	E	231	19.280	113.183	−9.900	1.00	51.86	B000	O
ATOM	7207	CB	THR	E	231	19.606	114.531	−12.495	1.00	52.22	B000	C
ATOM	7208	OG1	THR	E	231	18.217	114.591	−12.844	1.00	53.83	B000	O
ATOM	7209	CG2	THR	E	231	20.445	115.043	−13.668	1.00	46.56	B000	C
ATOM	7210	N	GLY	E	232	18.363	111.540	−11.160	1.00	55.84	B000	N
ATOM	7211	CA	GLY	E	232	17.470	111.077	−10.123	1.00	48.35	B000	C
ATOM	7212	C	GLY	E	232	18.105	110.067	−9.184	1.00	48.84	B000	C
ATOM	7213	O	GLY	E	232	19.249	109.642	−9.345	1.00	44.82	B000	O
ATOM	7214	N	PHE	E	233	17.313	109.679	−8.185	1.00	47.45	B000	N
ATOM	7215	CA	PHE	E	233	17.724	108.672	−7.218	1.00	45.48	B000	C
ATOM	7216	C	PHE	E	233	17.998	107.339	−7.920	1.00	45.39	B000	C
ATOM	7217	O	PHE	E	233	17.309	106.963	−8.870	1.00	43.33	B000	O
ATOM	7218	CB	PHE	E	233	16.627	108.531	−6.141	1.00	43.07	B000	C
ATOM	7219	CG	PHE	E	233	16.952	107.537	−5.062	1.00	49.50	B000	C
ATOM	7220	CD1	PHE	E	233	17.819	107.865	−4.031	1.00	49.13	B000	C
ATOM	7221	CD2	PHE	E	233	16.393	106.267	−5.077	1.00	46.36	B000	C
ATOM	7222	CE1	PHE	E	233	18.130	106.941	−3.043	1.00	56.48	B000	C
ATOM	7223	CE2	PHE	E	233	16.703	105.332	−4.089	1.00	43.16	B000	C
ATOM	7224	CZ	PHE	E	233	17.570	105.668	−3.073	1.00	50.08	B000	C
ATOM	7225	N	LYS	E	234	19.027	106.631	−7.461	1.00	43.29	B000	N
ATOM	7226	CA	LYS	E	234	19.350	105.304	−7.964	1.00	42.55	B000	C
ATOM	7227	C	LYS	E	234	19.835	104.464	−6.800	1.00	48.47	B000	C
ATOM	7228	O	LYS	E	234	20.501	104.989	−5.904	1.00	44.87	B000	O
ATOM	7229	CB	LYS	E	234	20.433	105.329	−9.047	1.00	43.84	B000	C
ATOM	7230	CG	LYS	E	234	20.093	106.096	−10.319	1.00	43.53	B000	C
ATOM	7231	CD	LYS	E	234	21.305	106.028	−11.250	1.00	42.53	B000	C
ATOM	7232	CE	LYS	E	234	21.235	107.016	−12.398	1.00	46.96	B000	C
ATOM	7233	NZ	LYS	E	234	21.273	108.424	−11.907	1.00	55.21	B000	N1+
ATOM	7234	N	ASN	E	235	19.486	103.171	−6.793	1.00	46.39	B000	N
ATOM	7235	CA	ASN	E	235	19.925	102.276	−5.717	1.00	42.44	B000	C
ATOM	7236	C	ASN	E	235	20.263	100.885	−6.277	1.00	41.99	B000	C
ATOM	7237	O	ASN	E	235	19.881	99.849	−5.728	1.00	41.55	B000	O
ATOM	7238	CB	ASN	E	235	18.867	102.211	−4.605	1.00	37.90	B000	C
ATOM	7239	CG	ASN	E	235	19.353	101.448	−3.380	1.00	40.64	B000	C
ATOM	7240	OD1	ASN	E	235	20.538	101.458	−3.079	1.00	45.11	B000	O
ATOM	7241	ND2	ASN	E	235	18.449	100.769	−2.685	1.00	41.74	B000	N
ATOM	7242	N	TRP	E	236	21.051	100.853	−7.346	1.00	39.52	B000	N
ATOM	7243	CA	TRP	E	236	21.407	99.599	−7.994	1.00	37.91	B000	C
ATOM	7244	C	TRP	E	236	22.266	98.720	−7.099	1.00	42.70	B000	C
ATOM	7245	O	TRP	E	236	23.054	99.199	−6.281	1.00	46.72	B000	O
ATOM	7246	CB	TRP	E	236	22.178	99.848	−9.299	1.00	34.60	B000	C
ATOM	7247	CG	TRP	E	236	21.377	100.494	−10.396	1.00	43.16	B000	C
ATOM	7248	CD1	TRP	E	236	21.452	101.794	−10.810	1.00	36.82	B000	C
ATOM	7249	CD2	TRP	E	236	20.363	99.873	−11.207	1.00	38.15	B000	C
ATOM	7250	NE1	TRP	E	236	20.565	102.017	−11.839	1.00	41.26	B000	N
ATOM	7251	CE2	TRP	E	236	19.884	100.857	−12.103	1.00	39.75	B000	C
ATOM	7252	CE3	TRP	E	236	19.831	98.581	−11.273	1.00	36.10	B000	C
ATOM	7253	CZ2	TRP	E	236	18.894	100.591	−13.054	1.00	35.54	B000	C
ATOM	7254	CZ3	TRP	E	236	18.850	98.311	−12.219	1.00	35.95	B000	C
ATOM	7255	CH2	TRP	E	236	18.389	99.317	−13.096	1.00	41.76	B000	C
ATOM	7256	N	ARG	E	237	22.102	97.410	−7.274	1.00	45.40	B000	N
ATOM	7257	CA	ARG	E	237	23.050	96.440	−6.763	1.00	47.18	B000	C
ATOM	7258	C	ARG	E	237	24.449	96.720	−7.314	1.00	51.81	B000	C
ATOM	7259	O	ARG	E	237	24.595	97.350	−8.368	1.00	43.69	B000	O
ATOM	7260	CB	ARG	E	237	22.634	95.041	−7.185	1.00	46.24	B000	C
ATOM	7261	CG	ARG	E	237	21.530	94.422	−6.393	1.00	51.40	B000	C
ATOM	7262	CD	ARG	E	237	22.096	93.585	−5.285	1.00	58.45	B000	C
ATOM	7263	NE	ARG	E	237	21.038	92.772	−4.710	1.00	70.66	B000	N
ATOM	7264	CZ	ARG	E	237	21.262	91.703	−3.961	1.00	72.34	B000	C
ATOM	7265	NH1	ARG	E	237	20.232	90.990	−3.494	1.00	63.81	B000	N1+
ATOM	7266	NH2	ARG	E	237	22.525	91.368	−3.681	1.00	60.30	B000	N
ATOM	7267	N	PRO	E	238	25.489	96.240	−6.628	1.00	52.18	B000	N
ATOM	7268	CA	PRO	E	238	26.853	96.359	−7.163	1.00	56.03	B000	C
ATOM	7269	C	PRO	E	238	26.950	95.788	−8.569	1.00	52.87	B000	C
ATOM	7270	O	PRO	E	238	26.528	94.660	−8.830	1.00	56.32	B000	O
ATOM	7271	CB	PRO	E	238	27.694	95.545	−6.171	1.00	52.68	B000	C
ATOM	7272	CG	PRO	E	238	26.934	95.614	−4.891	1.00	56.74	B000	C
ATOM	7273	CD	PRO	E	238	25.473	95.617	−5.291	1.00	58.40	B000	C
ATOM	7274	N	GLU	E	239	27.508	96.588	−9.477	1.00	54.34	B000	N
ATOM	7275	CA	GLU	E	239	27.753	96.254	−10.877	1.00	53.49	B000	C
ATOM	7276	C	GLU	E	239	26.481	96.144	−11.711	1.00	55.15	B000	C
ATOM	7277	O	GLU	E	239	26.545	95.684	−12.862	1.00	57.25	B000	O
ATOM	7278	CB	GLU	E	239	28.578	94.974	−11.029	1.00	50.60	B000	C
ATOM	7279	CG	GLU	E	239	30.001	95.104	−10.514	1.00	66.65	B000	C
ATOM	7280	CD	GLU	E	239	30.663	93.760	−10.297	1.00	83.88	B000	C
ATOM	7281	OE1	GLU	E	239	30.038	92.728	−10.639	1.00	75.71	B000	O
ATOM	7282	OE2	GLU	E	239	31.816	93.739	−9.808	1.00	96.45	B000	O1−
ATOM	7283	N	GLN	E	240	25.336	96.571	−11.187	1.00	42.77	B000	N
ATOM	7284	CA	GLN	E	240	24.126	96.666	−11.990	1.00	44.13	B000	C
ATOM	7285	C	GLN	E	240	23.886	98.142	−12.320	1.00	39.19	B000	C
ATOM	7286	O	GLN	E	240	24.353	99.013	−11.600	1.00	37.74	B000	O
ATOM	7287	CB	GLN	E	240	22.931	96.054	−11.253	1.00	41.92	B000	C
ATOM	7288	CG	GLN	E	240	23.174	94.638	−10.737	1.00	41.56	B000	C
ATOM	7289	CD	GLN	E	240	23.857	93.758	−11.761	1.00	47.34	B000	C
ATOM	7290	OE1	GLN	E	240	23.461	93.713	−12.927	1.00	45.90	B000	O
ATOM	7291	NE2	GLN	E	240	24.908	93.071	−11.336	1.00	53.15	B000	N
ATOM	7292	N	PRO	E	241	23.176	98.433	−13.423	1.00	39.17	B000	N
ATOM	7293	CA	PRO	E	241	22.582	97.492	−14.382	1.00	41.50	B000	C
ATOM	7294	C	PRO	E	241	23.654	96.945	−15.327	1.00	39.88	B000	C
ATOM	7295	O	PRO	E	241	24.800	97.332	−15.130	1.00	47.11	B000	O
ATOM	7296	CB	PRO	E	241	21.539	98.350	−15.114	1.00	41.31	B000	C
ATOM	7297	CG	PRO	E	241	22.116	99.770	−15.042	1.00	40.16	B000	C
ATOM	7298	CD	PRO	E	241	22.851	99.844	−13.732	1.00	35.10	B000	C
ATOM	7299	N	ASP	E	242	23.325	96.074	−16.287	1.00	39.07	B000	N
ATOM	7300	CA	ASP	E	242	24.337	95.571	−17.221	1.00	42.10	B000	C
ATOM	7301	C	ASP	E	242	25.112	96.732	−17.827	1.00	45.64	B000	C
ATOM	7302	O	ASP	E	242	24.512	97.697	−18.317	1.00	42.87	B000	O
ATOM	7303	CB	ASP	E	242	23.691	94.761	−18.348	1.00	42.84	B000	C
ATOM	7304	CG	ASP	E	242	22.886	93.568	−17.852	1.00	43.37	B000	C
ATOM	7305	OD1	ASP	E	242	23.330	92.905	−16.895	1.00	46.50	B000	O
ATOM	7306	OD2	ASP	E	242	21.800	93.308	−18.430	1.00	43.11	B000	O1−
ATOM	7307	N	ASP	E	243	26.448	96.634	−17.808	1.00	39.31	B000	N
ATOM	7308	CA	ASP	E	243	27.300	97.761	−18.190	1.00	47.79	B000	C
ATOM	7309	C	ASP	E	243	27.812	97.693	−19.621	1.00	43.78	B000	C
ATOM	7310	O	ASP	E	243	28.698	98.475	−19.976	1.00	46.39	B000	O
ATOM	7311	CB	ASP	E	243	28.506	97.880	−17.250	1.00	43.08	B000	C
ATOM	7312	CG	ASP	E	243	29.395	96.633	−17.252	1.00	54.01	B000	C
ATOM	7313	OD1	ASP	E	243	29.151	95.676	−18.025	1.00	56.31	B000	O
ATOM	7314	OD2	ASP	E	243	30.350	96.604	−16.453	1.00	60.30	B000	O1−
ATOM	7315	N	TRP	E	244	27.332	96.754	−20.435	1.00	42.79	B000	N
ATOM	7316	CA	TRP	E	244	27.941	96.563	−21.742	1.00	44.21	B000	C
ATOM	7317	C	TRP	E	244	27.283	97.361	−22.860	1.00	43.63	B000	C
ATOM	7318	O	TRP	E	244	27.674	97.194	−24.018	1.00	43.92	B000	O
ATOM	7319	CB	TRP	E	244	28.043	95.072	−22.108	1.00	43.09	B000	C
ATOM	7320	CG	TRP	E	244	26.891	94.182	−21.886	1.00	44.80	B000	C
ATOM	7321	CD1	TRP	E	244	25.879	93.900	−22.770	1.00	47.43	B000	C
ATOM	7322	CD2	TRP	E	244	26.668	93.355	−20.746	1.00	43.82	B000	C
ATOM	7323	NE1	TRP	E	244	25.016	92.980	−22.226	1.00	44.04	B000	N
ATOM	7324	CE2	TRP	E	244	25.482	92.621	−20.987	1.00	46.21	B000	C
ATOM	7325	CE3	TRP	E	244	27.346	93.171	−19.540	1.00	42.76	B000	C
ATOM	7326	CZ2	TRP	E	244	24.957	91.729	−20.060	1.00	44.01	B000	C
ATOM	7327	CZ3	TRP	E	244	26.827	92.292	−18.622	1.00	42.24	B000	C
ATOM	7328	CH2	TRP	E	244	25.641	91.579	−18.883	1.00	49.08	B000	C
ATOM	7329	N	TYR	E	245	26.330	98.242	−22.550	1.00	43.45	B000	N
ATOM	7330	CA	TYR	E	245	25.626	99.013	−23.574	1.00	45.01	B000	C
ATOM	7331	C	TYR	E	245	26.012	100.481	−23.628	1.00	42.12	B000	C
ATOM	7332	O	TYR	E	245	25.598	101.169	−24.560	1.00	45.10	B000	O
ATOM	7333	CB	TYR	E	245	24.099	98.947	−23.366	1.00	42.26	B000	C
ATOM	7334	CG	TYR	E	245	23.544	97.553	−23.256	1.00	43.72	B000	C
ATOM	7335	CD1	TYR	E	245	23.355	96.770	−24.391	1.00	40.29	B000	C
ATOM	7336	CD2	TYR	E	245	23.224	97.006	−22.016	1.00	39.35	B000	C
ATOM	7337	CE1	TYR	E	245	22.841	95.500	−24.301	1.00	39.08	B000	C
ATOM	7338	CE2	TYR	E	245	22.717	95.722	−21.918	1.00	43.84	B000	C
ATOM	7339	CZ	TYR	E	245	22.533	94.976	−23.064	1.00	41.96	B000	C
ATOM	7340	OH	TYR	E	245	22.036	93.706	−22.975	1.00	45.97	B000	O
ATOM	7341	N	GLY	E	246	26.710	101.001	−22.638	1.00	41.64	B000	N
ATOM	7342	CA	GLY	E	246	26.989	102.420	−22.592	1.00	43.53	B000	C
ATOM	7343	C	GLY	E	246	26.255	103.119	−21.455	1.00	47.49	B000	C
ATOM	7344	O	GLY	E	246	25.273	102.626	−20.898	1.00	44.82	B000	O
ATOM	7345	N	HIS	E	247	26.714	104.343	−21.189	1.00	50.58	B000	N
ATOM	7346	CA	HIS	E	247	26.284	105.118	−20.030	1.00	42.87	B000	C
ATOM	7347	C	HIS	E	247	24.783	105.367	−20.033	1.00	44.35	B000	C
ATOM	7348	O	HIS	E	247	24.236	105.933	−20.985	1.00	45.35	B000	O
ATOM	7349	CB	HIS	E	247	27.044	106.440	−20.003	1.00	53.73	B000	C
ATOM	7350	CG	HIS	E	247	26.584	107.373	−18.933	1.00	56.75	B000	C
ATOM	7351	ND1	HIS	E	247	26.920	107.206	−17.607	1.00	59.80	B000	N
ATOM	7352	CD2	HIS	E	247	25.799	108.476	−18.991	1.00	55.82	B000	C
ATOM	7353	CE1	HIS	E	247	26.367	108.172	−16.894	1.00	66.18	B000	C
ATOM	7354	NE2	HIS	E	247	25.682	108.956	−17.710	1.00	63.47	B000	N
ATOM	7355	N	GLY	E	248	24.117	104.949	−18.954	1.00	45.02	B000	N
ATOM	7356	CA	GLY	E	248	22.680	105.131	−18.847	1.00	45.46	B000	C
ATOM	7357	C	GLY	E	248	21.849	104.287	−19.791	1.00	46.59	B000	C
ATOM	7358	O	GLY	E	248	20.659	104.568	−19.979	1.00	40.42	B000	O
ATOM	7359	N	LEU	E	249	22.431	103.242	−20.380	1.00	42.75	B000	N
ATOM	7360	CA	LEU	E	249	21.760	102.493	−21.430	1.00	42.93	B000	C
ATOM	7361	C	LEU	E	249	21.579	101.026	−21.050	1.00	42.71	B000	C
ATOM	7362	O	LEU	E	249	22.327	100.466	−20.239	1.00	35.38	B000	O
ATOM	7363	CB	LEU	E	249	22.536	102.595	−22.750	1.00	39.36	B000	C
ATOM	7364	CG	LEU	E	249	22.689	104.006	−23.343	1.00	42.86	B000	C
ATOM	7365	CD1	LEU	E	249	23.340	103.916	−24.714	1.00	39.37	B000	C
ATOM	7366	CD2	LEU	E	249	21.350	104.700	−23.442	1.00	40.64	B000	C
ATOM	7367	N	GLY	E	250	20.569	100.410	−21.653	1.00	40.13	B000	N
ATOM	7368	CA	GLY	E	250	20.394	98.976	−21.584	1.00	34.39	B000	C
ATOM	7369	C	GLY	E	250	20.162	98.460	−22.986	1.00	42.96	B000	C
ATOM	7370	O	GLY	E	250	20.251	99.242	−23.936	1.00	39.19	B000	O
ATOM	7371	N	GLY	E	251	19.857	97.167	−23.135	1.00	42.21	B000	N
ATOM	7372	CA	GLY	E	251	19.622	96.533	−24.418	1.00	38.08	B000	C
ATOM	7373	C	GLY	E	251	18.179	96.437	−24.892	1.00	41.51	B000	C
ATOM	7374	O	GLY	E	251	17.932	95.813	−25.932	1.00	47.66	B000	O
ATOM	7375	N	GLY	E	252	17.209	97.010	−24.169	1.00	45.08	B000	N
ATOM	7376	CA	GLY	E	252	15.832	97.049	−24.628	1.00	44.10	B000	C
ATOM	7377	C	GLY	E	252	14.893	95.971	−24.115	1.00	40.91	B000	C
ATOM	7378	O	GLY	E	252	13.707	96.009	−24.452	1.00	51.51	B000	O
ATOM	7379	N	GLU	E	253	15.380	94.997	−23.351	1.00	49.13	B000	N
ATOM	7380	CA	GLU	E	253	14.569	93.886	−22.849	1.00	44.54	B000	C
ATOM	7381	C	GLU	E	253	14.410	93.867	−21.335	1.00	40.80	B000	C
ATOM	7382	O	GLU	E	253	13.844	92.902	−20.810	1.00	43.41	B000	O
ATOM	7383	CB	GLU	E	253	15.180	92.537	−23.273	1.00	49.30	B000	C
ATOM	7384	CG	GLU	E	253	15.553	92.443	−24.748	1.00	58.40	B000	C
ATOM	7385	CD	GLU	E	253	14.373	92.111	−25.651	1.00	68.11	B000	C
ATOM	7386	OE1	GLU	E	253	13.919	90.934	−25.628	1.00	71.69	B000	O
ATOM	7387	OE2	GLU	E	253	13.900	93.027	−26.378	1.00	62.49	B000	O1−
ATOM	7388	N	ASP	E	254	14.951	94.848	−20.611	1.00	41.14	B000	N
ATOM	7389	CA	ASP	E	254	15.056	94.754	−19.159	1.00	36.67	B000	C
ATOM	7390	C	ASP	E	254	14.148	95.742	−18.448	1.00	37.02	B000	C
ATOM	7391	O	ASP	E	254	13.733	96.776	−18.990	1.00	37.00	B000	O
ATOM	7392	CB	ASP	E	254	16.497	94.967	−18.685	1.00	34.36	B000	C
ATOM	7393	CG	ASP	E	254	17.333	93.693	−18.779	1.00	37.96	B000	C
ATOM	7394	OD1	ASP	E	254	16.776	92.662	−19.226	1.00	36.64	B000	O
ATOM	7395	OD2	ASP	E	254	18.547	93.740	−18.453	1.00	41.46	B000	O1−
ATOM	7396	N	CYS	E	255	13.822	95.368	−17.219	1.00	35.51	B000	N
ATOM	7397	CA	CYS	E	255	13.086	96.210	−16.300	1.00	32.38	B000	C
ATOM	7398	C	CYS	E	255	13.781	96.107	−14.955	1.00	37.45	B000	C
ATOM	7399	O	CYS	E	255	14.493	95.137	−14.689	1.00	34.78	B000	O
ATOM	7400	CB	CYS	E	255	11.612	95.789	−16.219	1.00	34.76	B000	C
ATOM	7401	SG	CYS	E	255	10.671	96.035	−17.761	1.00	37.35	B000	S
ATOM	7402	N	ALA	E	256	13.609	97.138	−14.123	1.00	31.93	B000	N
ATOM	7403	CA	ALA	E	256	14.263	97.192	−12.823	1.00	34.86	B000	C
ATOM	7404	C	ALA	E	256	13.329	96.663	−11.744	1.00	35.59	B000	C
ATOM	7405	O	ALA	E	256	12.138	96.994	−11.720	1.00	30.92	B000	O
ATOM	7406	CB	ALA	E	256	14.688	98.621	−12.480	1.00	33.92	B000	C
ATOM	7407	N	HIS	E	257	13.870	95.833	−10.854	1.00	28.95	B000	N
ATOM	7408	CA	HIS	E	257	13.097	95.348	−9.721	1.00	35.16	B000	C
ATOM	7409	C	HIS	E	257	13.897	95.485	−8.434	1.00	35.13	B000	C
ATOM	7410	O	HIS	E	257	15.130	95.402	−8.425	1.00	34.18	B000	O
ATOM	7411	CB	HIS	E	257	12.655	93.884	−9.909	1.00	30.40	B000	C
ATOM	7412	CG	HIS	E	257	13.789	92.909	−10.005	1.00	36.00	B000	C
ATOM	7413	ND1	HIS	E	257	14.213	92.160	−8.930	1.00	36.61	B000	N
ATOM	7414	CD2	HIS	E	257	14.576	92.547	−11.050	1.00	29.26	B000	C
ATOM	7415	CE1	HIS	E	257	15.205	91.373	−9.306	1.00	36.08	B000	C
ATOM	7416	NE2	HIS	E	257	15.444	91.589	−10.588	1.00	41.23	B000	N
ATOM	7417	N	PHE	E	258	13.178	95.722	−7.344	1.00	32.98	B000	N
ATOM	7418	CA	PHE	E	258	13.783	95.567	−6.036	1.00	35.47	B000	C
ATOM	7419	C	PHE	E	258	14.126	94.102	−5.825	1.00	36.56	B000	C
ATOM	7420	O	PHE	E	258	13.342	93.217	−6.182	1.00	37.64	B000	O
ATOM	7421	CB	PHE	E	258	12.828	96.024	−4.943	1.00	34.07	B000	C
ATOM	7422	CG	PHE	E	258	12.279	97.408	−5.140	1.00	36.26	B000	C
ATOM	7423	CD1	PHE	E	258	12.991	98.528	−4.707	1.00	31.80	B000	C
ATOM	7424	CD2	PHE	E	258	11.025	97.588	−5.714	1.00	31.31	B000	C
ATOM	7425	CE1	PHE	E	258	12.469	99.798	−4.865	1.00	33.16	B000	C
ATOM	7426	CE2	PHE	E	258	10.492	98.861	−5.882	1.00	39.41	B000	C
ATOM	7427	CZ	PHE	E	258	11.208	99.972	−5.462	1.00	34.38	B000	C
ATOM	7428	N	THR	E	259	15.302	93.853	−5.249	1.00	37.86	B000	N
ATOM	7429	CA	THR	E	259	15.716	92.540	−4.772	1.00	42.13	B000	C
ATOM	7430	C	THR	E	259	15.405	92.419	−3.289	1.00	44.25	B000	C
ATOM	7431	O	THR	E	259	14.879	93.339	−2.660	1.00	47.92	B000	O
ATOM	7432	CB	THR	E	259	17.209	92.303	−4.996	1.00	42.54	B000	C
ATOM	7433	OG1	THR	E	259	17.953	93.161	−4.117	1.00	44.35	B000	O
ATOM	7434	CG2	THR	E	259	17.579	92.593	−6.433	1.00	39.50	B000	C
ATOM	7435	N	ASP	E	260	15.785	91.280	−2.712	1.00	46.15	B000	N
ATOM	7436	CA	ASP	E	260	15.408	91.003	−1.334	1.00	48.77	B000	C
ATOM	7437	C	ASP	E	260	16.141	91.866	−0.318	1.00	51.79	B000	C
ATOM	7438	O	ASP	E	260	15.772	91.841	0.862	1.00	57.39	B000	O
ATOM	7439	CB	ASP	E	260	15.627	89.530	−1.002	1.00	48.59	B000	C
ATOM	7440	CG	ASP	E	260	17.039	89.064	−1.282	1.00	52.19	B000	C
ATOM	7441	OD1	ASP	E	260	17.934	89.890	−1.563	1.00	54.71	B000	O
ATOM	7442	OD2	ASP	E	260	17.255	87.847	−1.199	1.00	57.65	B000	O1−
ATOM	7443	N	ASP	E	261	17.175	92.602	−0.719	1.00	46.10	B000	N
ATOM	7444	CA	ASP	E	261	17.795	93.567	0.177	1.00	47.68	B000	C
ATOM	7445	C	ASP	E	261	17.411	95.007	−0.158	1.00	43.64	B000	C
ATOM	7446	O	ASP	E	261	17.959	95.938	0.434	1.00	50.15	B000	O
ATOM	7447	CB	ASP	E	261	19.322	93.386	0.195	1.00	43.46	B000	C
ATOM	7448	CG	ASP	E	261	20.013	93.851	−1.092	1.00	51.38	B000	C
ATOM	7449	OD1	ASP	E	261	19.414	94.549	−1.938	1.00	53.10	B000	O
ATOM	7450	OD2	ASP	E	261	21.201	93.523	−1.249	1.00	61.28	B000	O1−
ATOM	7451	N	GLY	E	262	16.490	95.208	−1.098	1.00	41.82	B000	N
ATOM	7452	CA	GLY	E	262	16.009	96.524	−1.460	1.00	37.30	B000	C
ATOM	7453	C	GLY	E	262	16.761	97.180	−2.597	1.00	36.57	B000	C
ATOM	7454	O	GLY	E	262	16.212	98.052	−3.272	1.00	41.75	B000	O
ATOM	7455	N	ARG	E	263	18.012	96.804	−2.802	1.00	38.36	B000	N
ATOM	7456	CA	ARG	E	263	18.764	97.311	−3.928	1.00	41.20	B000	C
ATOM	7457	C	ARG	E	263	18.224	96.727	−5.227	1.00	45.69	B000	C
ATOM	7458	O	ARG	E	263	17.553	95.687	−5.250	1.00	42.28	B000	O
ATOM	7459	CB	ARG	E	263	20.242	96.991	−3.749	1.00	41.55	B000	C
ATOM	7460	CG	ARG	E	263	20.841	97.820	−2.615	1.00	42.80	B000	C
ATOM	7461	CD	ARG	E	263	22.274	97.464	−2.375	1.00	42.94	B000	C
ATOM	7462	NE	ARG	E	263	22.431	96.060	−2.029	1.00	50.20	B000	N
ATOM	7463	CZ	ARG	E	263	23.609	95.464	−1.881	1.00	58.64	B000	C
ATOM	7464	NH1	ARG	E	263	24.728	96.164	−2.057	1.00	53.73	B000	N1+
ATOM	7465	NH2	ARG	E	263	23.670	94.172	−1.573	1.00	56.41	B000	N
ATOM	7466	N	TRP	E	264	18.506	97.428	−6.314	1.00	43.23	B000	N
ATOM	7467	CA	TRP	E	264	17.854	97.186	−7.588	1.00	42.16	B000	C
ATOM	7468	C	TRP	E	264	18.687	96.288	−8.491	1.00	43.43	B000	C
ATOM	7469	O	TRP	E	264	19.921	96.322	−8.465	1.00	41.15	B000	O
ATOM	7470	CB	TRP	E	264	17.595	98.493	−8.322	1.00	37.69	B000	C
ATOM	7471	CG	TRP	E	264	16.910	99.526	−7.547	1.00	42.39	B000	C
ATOM	7472	CD1	TRP	E	264	16.342	99.410	−6.306	1.00	42.33	B000	C
ATOM	7473	CD2	TRP	E	264	16.714	100.874	−7.958	1.00	41.30	B000	C
ATOM	7474	NE1	TRP	E	264	15.797	100.613	−5.924	1.00	37.50	B000	N
ATOM	7475	CE2	TRP	E	264	16.011	101.530	−6.921	1.00	43.31	B000	C
ATOM	7476	CE3	TRP	E	264	17.068	101.595	−9.104	1.00	38.49	B000	C
ATOM	7477	CZ2	TRP	E	264	15.649	102.882	−6.999	1.00	46.31	B000	C
ATOM	7478	CZ3	TRP	E	264	16.716	102.938	−9.179	1.00	44.68	B000	C
ATOM	7479	CH2	TRP	E	264	16.005	103.564	−8.135	1.00	47.08	B000	C
ATOM	7480	N	ASN	E	265	17.986	95.533	−9.339	1.00	40.37	B000	N
ATOM	7481	CA	ASN	E	265	18.601	94.718	−10.374	1.00	38.67	B000	C
ATOM	7482	C	ASN	E	265	17.770	94.816	−11.652	1.00	35.88	B000	C
ATOM	7483	O	ASN	E	265	16.561	95.055	−11.608	1.00	33.72	B000	O
ATOM	7484	CB	ASN	E	265	18.731	93.267	−9.899	1.00	40.88	B000	C
ATOM	7485	CG	ASN	E	265	19.363	92.369	−10.940	1.00	49.30	B000	C
ATOM	7486	OD1	ASN	E	265	20.484	92.622	−11.373	1.00	46.08	B000	O
ATOM	7487	ND2	ASN	E	265	18.667	91.288	−11.315	1.00	49.35	B000	N
ATOM	7488	N	ASP	E	266	18.431	94.646	−12.795	1.00	37.44	B000	N
ATOM	7489	CA	ASP	E	266	17.769	94.648	−14.092	1.00	34.38	B000	C
ATOM	7490	C	ASP	E	266	17.585	93.211	−14.559	1.00	35.40	B000	C
ATOM	7491	O	ASP	E	266	18.516	92.408	−14.481	1.00	38.07	B000	O
ATOM	7492	CB	ASP	E	266	18.549	95.463	−15.137	1.00	34.61	B000	C
ATOM	7493	CG	ASP	E	266	20.046	95.092	−15.230	1.00	42.09	B000	C
ATOM	7494	OD1	ASP	E	266	20.690	94.762	−14.202	1.00	40.07	B000	O
ATOM	7495	OD2	ASP	E	266	20.593	95.167	−16.358	1.00	40.68	B000	O1−
ATOM	7496	N	ASP	E	267	16.372	92.880	−15.001	1.00	37.34	B000	N
ATOM	7497	CA	ASP	E	267	16.034	91.524	−15.412	1.00	36.69	B000	C
ATOM	7498	C	ASP	E	267	15.052	91.576	−16.581	1.00	35.84	B000	C
ATOM	7499	O	ASP	E	267	14.431	92.609	−16.843	1.00	37.16	B000	O
ATOM	7500	CB	ASP	E	267	15.448	90.748	−14.230	1.00	33.55	B000	C
ATOM	7501	CG	ASP	E	267	15.724	89.244	−14.319	1.00	44.66	B000	C
ATOM	7502	OD1	ASP	E	267	16.128	88.792	−15.410	1.00	43.90	B000	O
ATOM	7503	OD2	ASP	E	267	15.535	88.518	−13.301	1.00	45.36	B000	O1−
ATOM	7504	N	VAL	E	268	14.901	90.455	−17.294	1.00	32.21	B000	N
ATOM	7505	CA	VAL	E	268	13.973	90.457	−18.423	1.00	34.18	B000	C
ATOM	7506	C	VAL	E	268	12.553	90.719	−17.928	1.00	37.30	B000	C
ATOM	7507	O	VAL	E	268	12.123	90.211	−16.883	1.00	38.04	B000	O
ATOM	7508	CB	VAL	E	268	14.050	89.154	−19.239	1.00	37.36	B000	C
ATOM	7509	CG1	VAL	E	268	15.409	89.057	−19.938	1.00	36.15	B000	C
ATOM	7510	CG2	VAL	E	268	13.806	87.936	−18.370	1.00	35.18	B000	C
ATOM	7511	N	CYS	E	269	11.809	91.513	−18.697	1.00	36.57	B000	N
ATOM	7512	CA	CYS	E	269	10.538	92.045	−18.240	1.00	36.70	B000	C
ATOM	7513	C	CYS	E	269	9.449	90.995	−18.103	1.00	34.59	B000	C
ATOM	7514	O	CYS	E	269	8.418	91.294	−17.500	1.00	35.91	B000	O
ATOM	7515	CB	CYS	E	269	10.088	93.163	−19.185	1.00	42.38	B000	C
ATOM	7516	SG	CYS	E	269	11.267	94.591	−19.164	1.00	53.92	B000	S
ATOM	7517	N	GLN	E	270	9.643	89.777	−18.595	1.00	33.91	B000	N
ATOM	7518	CA	GLN	E	270	8.591	88.778	−18.422	1.00	38.11	B000	C
ATOM	7519	C	GLN	E	270	8.652	88.057	−17.086	1.00	33.78	B000	C
ATOM	7520	O	GLN	E	270	7.760	87.247	−16.828	1.00	33.42	B000	O
ATOM	7521	CB	GLN	E	270	8.578	87.723	−19.549	1.00	38.43	B000	C
ATOM	7522	CG	GLN	E	270	9.815	87.602	−20.390	1.00	44.86	B000	C
ATOM	7523	CD	GLN	E	270	10.038	88.821	−21.260	1.00	52.91	B000	C
ATOM	7524	OE1	GLN	E	270	11.140	89.358	−21.293	1.00	55.48	B000	O
ATOM	7525	NE2	GLN	E	270	8.986	89.280	−21.949	1.00	51.33	B000	N
ATOM	7526	N	ARG	E	271	9.649	88.338	−16.229	1.00	31.87	B000	N
ATOM	7527	CA	ARG	E	271	9.677	87.758	−14.889	1.00	29.54	B000	C
ATOM	7528	C	ARG	E	271	8.356	88.049	−14.171	1.00	36.60	B000	C
ATOM	7529	O	ARG	E	271	7.873	89.192	−14.210	1.00	35.38	B000	O
ATOM	7530	CB	ARG	E	271	10.829	88.325	−14.050	1.00	28.67	B000	C
ATOM	7531	CG	ARG	E	271	12.220	87.973	−14.479	1.00	27.89	B000	C
ATOM	7532	CD	ARG	E	271	12.418	86.476	−14.518	1.00	31.48	B000	C
ATOM	7533	NE	ARG	E	271	13.822	86.098	−14.676	1.00	33.37	B000	N
ATOM	7534	CZ	ARG	E	271	14.203	84.864	−14.987	1.00	37.02	B000	C
ATOM	7535	NH1	ARG	E	271	13.268	83.937	−15.180	1.00	30.74	B000	N1+
ATOM	7536	NH2	ARG	E	271	15.492	84.540	−15.076	1.00	29.23	B000	N
ATOM	7537	N	PRO	E	272	7.778	87.122	−13.565	1.00	34.45	B000	N
ATOM	7538	CA	PRO	E	272	6.493	87.373	−12.870	1.00	35.22	B000	C
ATOM	7539	C	PRO	E	272	6.670	87.925	−11.455	1.00	35.16	B000	C
ATOM	7540	O	PRO	E	272	6.234	87.321	−10.470	1.00	31.89	B000	O
ATOM	7541	CB	PRO	E	272	5.847	85.979	−12.867	1.00	31.77	B000	C
ATOM	7542	CG	PRO	E	272	7.003	85.036	−12.787	1.00	32.91	B000	C
ATOM	7543	CD	PRO	E	272	8.114	85.689	−13.621	1.00	30.82	B000	C
ATOM	7544	N	TYR	E	273	7.295	89.101	−11.344	1.00	31.62	B000	N
ATOM	7545	CA	TYR	E	273	7.555	89.672	−10.028	1.00	32.44	B000	C
ATOM	7546	C	TYR	E	273	6.327	90.398	−9.474	1.00	33.52	B000	C
ATOM	7547	O	TYR	E	273	5.355	90.667	−10.183	1.00	33.94	B000	O
ATOM	7548	CB	TYR	E	273	8.752	90.615	−10.089	1.00	32.72	B000	C
ATOM	7549	CG	TYR	E	273	10.050	89.893	−10.371	1.00	34.81	B000	C
ATOM	7550	CD1	TYR	E	273	10.215	88.558	−10.004	1.00	30.34	B000	C
ATOM	7551	CD2	TYR	E	273	11.125	90.546	−10.996	1.00	34.47	B000	C
ATOM	7552	CE1	TYR	E	273	11.428	87.883	−10.249	1.00	31.47	B000	C
ATOM	7553	CE2	TYR	E	273	12.329	89.879	−11.245	1.00	31.66	B000	C
ATOM	7554	CZ	TYR	E	273	12.468	88.549	−10.867	1.00	32.58	B000	C
ATOM	7555	OH	TYR	E	273	13.639	87.883	−11.117	1.00	37.35	B000	O
ATOM	7556	N	ARG	E	274	6.356	90.671	−8.170	1.00	34.37	B000	N
ATOM	7557	CA	ARG	E	274	5.350	91.549	−7.579	1.00	32.60	B000	C
ATOM	7558	C	ARG	E	274	5.542	92.978	−8.089	1.00	35.51	B000	C
ATOM	7559	O	ARG	E	274	6.533	93.300	−8.757	1.00	31.65	B000	O
ATOM	7560	CB	ARG	E	274	5.426	91.519	−6.048	1.00	31.74	B000	C
ATOM	7561	CG	ARG	E	274	5.044	90.177	−5.455	1.00	35.22	B000	C
ATOM	7562	CD	ARG	E	274	4.922	90.200	−3.952	1.00	36.81	B000	C
ATOM	7563	NE	ARG	E	274	4.320	88.966	−3.474	1.00	36.66	B000	N
ATOM	7564	CZ	ARG	E	274	4.010	88.714	−2.206	1.00	38.82	B000	C
ATOM	7565	NH1	ARG	E	274	4.266	89.605	−1.260	1.00	40.20	B000	N1+
ATOM	7566	NH2	ARG	E	274	3.432	87.563	−1.886	1.00	37.93	B000	N
ATOM	7567	N	TRP	E	275	4.591	93.857	−7.757	1.00	34.71	B000	N
ATOM	7568	CA	TRP	E	275	4.709	95.242	−8.207	1.00	35.25	B000	C
ATOM	7569	C	TRP	E	275	4.038	96.177	−7.209	1.00	33.77	B000	C
ATOM	7570	O	TRP	E	275	3.288	95.762	−6.316	1.00	34.64	B000	O
ATOM	7571	CB	TRP	E	275	4.133	95.429	−9.622	1.00	29.33	B000	C
ATOM	7572	CG	TRP	E	275	2.633	95.433	−9.666	1.00	41.26	B000	C
ATOM	7573	CD1	TRP	E	275	1.824	96.531	−9.687	1.00	32.79	B000	C
ATOM	7574	CD2	TRP	E	275	1.762	94.290	−9.659	1.00	35.30	B000	C
ATOM	7575	NE1	TRP	E	275	0.516	96.147	−9.707	1.00	34.43	B000	N
ATOM	7576	CE2	TRP	E	275	0.441	94.779	−9.687	1.00	41.97	B000	C
ATOM	7577	CE3	TRP	E	275	1.971	92.908	−9.650	1.00	34.18	B000	C
ATOM	7578	CZ2	TRP	E	275	−0.681	93.928	−9.698	1.00	39.53	B000	C
ATOM	7579	CZ3	TRP	E	275	0.861	92.059	−9.654	1.00	40.96	B000	C
ATOM	7580	CH2	TRP	E	275	−0.445	92.574	−9.680	1.00	40.67	B000	C
ATOM	7581	N	VAL	E	276	4.345	97.453	−7.367	1.00	32.75	B000	N
ATOM	7582	CA	VAL	E	276	3.827	98.520	−6.528	1.00	36.54	B000	C
ATOM	7583	C	VAL	E	276	3.248	99.578	−7.451	1.00	43.35	B000	C
ATOM	7584	O	VAL	E	276	3.916	99.998	−8.404	1.00	39.24	B000	O
ATOM	7585	CB	VAL	E	276	4.932	99.125	−5.636	1.00	39.71	B000	C
ATOM	7586	CG1	VAL	E	276	4.364	100.226	−4.708	1.00	36.15	B000	C
ATOM	7587	CG2	VAL	E	276	5.626	98.033	−4.830	1.00	33.07	B000	C
ATOM	7588	N	CYS	E	277	2.015	100.004	−7.176	1.00	41.27	B000	N
ATOM	7589	CA	CYS	E	277	1.403	101.127	−7.878	1.00	39.77	B000	C
ATOM	7590	C	CYS	E	277	1.513	102.387	−7.022	1.00	46.66	B000	C
ATOM	7591	O	CYS	E	277	1.519	102.321	−5.786	1.00	41.72	B000	O
ATOM	7592	CB	CYS	E	277	−0.063	100.847	−8.209	1.00	41.42	B000	C
ATOM	7593	SG	CYS	E	277	−0.364	99.509	−9.393	1.00	51.15	B000	S
ATOM	7594	N	GLU	E	278	1.622	103.536	−7.698	1.00	43.54	B000	N
ATOM	7595	CA	GLU	E	278	1.776	104.841	−7.069	1.00	38.79	B000	C
ATOM	7596	C	GLU	E	278	0.862	105.858	−7.751	1.00	45.95	B000	C
ATOM	7597	O	GLU	E	278	0.782	105.914	−8.988	1.00	39.44	B000	O
ATOM	7598	CB	GLU	E	278	3.243	105.302	−7.137	1.00	47.37	B000	C
ATOM	7599	CG	GLU	E	278	3.523	106.665	−6.506	1.00	54.07	B000	C
ATOM	7600	CD	GLU	E	278	4.983	107.122	−6.640	1.00	55.74	B000	C
ATOM	7601	OE1	GLU	E	278	5.813	106.384	−7.214	1.00	49.09	B000	O
ATOM	7602	OE2	GLU	E	278	5.299	108.234	−6.158	1.00	63.05	B000	O1−
ATOM	7603	N	THR	E	279	0.194	106.677	−6.933	1.00	44.07	B000	N
ATOM	7604	CA	THR	E	279	−0.653	107.764	−7.416	1.00	49.75	B000	C
ATOM	7605	C	THR	E	279	−0.567	108.944	−6.440	1.00	52.93	B000	C
ATOM	7606	O	THR	E	279	0.043	108.854	−5.367	1.00	51.44	B000	O
ATOM	7607	CB	THR	E	279	−2.103	107.288	−7.604	1.00	51.62	B000	C
ATOM	7608	OG1	THR	E	279	−2.814	108.206	−8.438	1.00	58.36	B000	O
ATOM	7609	CG2	THR	E	279	−2.815	107.204	−6.271	1.00	48.77	B000	C
ATOM	7610	N	GLU	E	280	−1.195	110.058	−6.818	1.00	57.24	B000	N
ATOM	7611	CA	GLU	E	280	−1.083	111.317	−6.090	1.00	59.43	B000	C
ATOM	7612	C	GLU	E	280	−2.071	111.410	−4.922	1.00	60.25	B000	C
ATOM	7613	O	GLU	E	280	−2.950	110.567	−4.738	1.00	57.16	B000	O
ATOM	7614	CB	GLU	E	280	−1.329	112.479	−7.040	1.00	72.93	B000	C
ATOM	7615	CG	GLU	E	280	−1.062	112.139	−8.487	1.00	81.08	B000	C
ATOM	7616	CD	GLU	E	280	−0.073	113.097	−9.119	1.00	105.55	B000	C
ATOM	7617	OE1	GLU	E	280	−0.010	114.263	−8.665	1.00	104.59	B000	O
ATOM	7618	OE2	GLU	E	280	0.648	112.680	−10.055	1.00	113.25	B000	O1−
ATOM	7619	N	LEU	E	281	−1.917	112.479	−4.135	1.00	77.88	B000	N
ATOM	7620	CA	LEU	E	281	−2.807	112.826	−3.011	1.00	70.25	B000	C
ATOM	7621	C	LEU	E	281	−2.681	111.825	−1.876	1.00	67.47	B000	C
ATOM	7622	O	LEU	E	281	−2.139	112.153	−0.819	1.00	68.88	B000	O
ATOM	7623	CB	LEU	E	281	−4.279	112.937	−3.459	1.00	61.71	B000	C
ATOM	7624	CG	LEU	E	281	−4.707	114.296	−4.035	1.00	80.45	B000	C
ATOM	7625	CD1	LEU	E	281	−5.181	114.179	−5.490	1.00	71.81	B000	C
ATOM	7626	CD2	LEU	E	281	−5.774	114.969	−3.143	1.00	70.21	B000	C
TER
ATOM	7627	O	THR	F	152	−18.909	43.540	−2.518	1.00	85.67	B000	O
ATOM	7628	N	THR	F	152	−17.763	41.399	−0.880	1.00	85.67	B000	N
ATOM	7629	CA	THR	F	152	−16.968	42.333	−1.678	1.00	88.53	B000	C
ATOM	7630	C	THR	F	152	−17.777	43.608	−2.017	1.00	91.37	B000	C
ATOM	7631	CB	THR	F	152	−16.431	41.637	−2.979	1.00	92.20	B000	C
ATOM	7632	OG1	THR	F	152	−15.806	42.597	−3.844	1.00	90.90	B000	O
ATOM	7633	CG2	THR	F	152	−17.541	40.894	−3.731	1.00	84.33	B000	C
ATOM	7634	N	CYS	F	153	−17.202	44.774	−1.715	1.00	87.63	B000	N
ATOM	7635	CA	CYS	F	153	−17.870	46.050	−1.926	1.00	82.80	B000	C
ATOM	7636	C	CYS	F	153	−17.103	46.899	−2.940	1.00	77.69	B000	C
ATOM	7637	O	CYS	F	153	−15.918	46.673	−3.212	1.00	67.09	B000	O
ATOM	7638	CB	CYS	F	153	−18.029	46.817	−0.596	1.00	79.27	B000	C
ATOM	7639	SG	CYS	F	153	−19.643	46.575	0.239	1.00	104.11	B000	S
ATOM	7640	N	CYS	F	154	−17.803	47.886	−3.508	1.00	76.91	B000	N
ATOM	7641	CA	CYS	F	154	−17.185	48.793	−4.462	1.00	59.34	B000	C
ATOM	7642	C	CYS	F	154	−16.202	49.711	−3.745	1.00	54.16	B000	C
ATOM	7643	O	CYS	F	154	−16.398	50.041	−2.575	1.00	63.36	B000	O
ATOM	7644	CB	CYS	F	154	−18.244	49.634	−5.172	1.00	55.19	B000	C
ATOM	7645	SG	CYS	F	154	−19.186	48.756	−6.443	1.00	69.85	B000	S
ATOM	7646	N	PRO	F	155	−15.156	50.163	−4.429	1.00	53.28	B000	N
ATOM	7647	CA	PRO	F	155	−14.236	51.130	−3.812	1.00	56.60	B000	C
ATOM	7648	C	PRO	F	155	−14.973	52.379	−3.346	1.00	57.95	B000	C
ATOM	7649	O	PRO	F	155	−16.130	52.640	−3.696	1.00	55.60	B000	O
ATOM	7650	CB	PRO	F	155	−13.243	51.459	−4.932	1.00	48.00	B000	C
ATOM	7651	CG	PRO	F	155	−13.374	50.336	−5.913	1.00	55.49	B000	C
ATOM	7652	CD	PRO	F	155	−14.777	49.826	−5.811	1.00	51.46	B000	C
ATOM	7653	N	VAL	F	156	−14.268	53.174	−2.539	1.00	56.46	B000	N
ATOM	7654	CA	VAL	F	156	−14.855	54.394	−1.991	1.00	63.80	B000	C
ATOM	7655	C	VAL	F	156	−15.250	55.333	−3.126	1.00	59.48	B000	C
ATOM	7656	O	VAL	F	156	−14.488	55.538	−4.081	1.00	58.09	B000	O
ATOM	7657	CB	VAL	F	156	−13.873	55.058	−1.014	1.00	62.21	B000	C
ATOM	7658	CG1	VAL	F	156	−14.577	56.145	−0.211	1.00	55.24	B000	C
ATOM	7659	CG2	VAL	F	156	−13.256	54.002	−0.096	1.00	73.19	B000	C
ATOM	7660	N	ASN	F	157	−16.460	55.891	−3.031	1.00	53.19	B000	N
ATOM	7661	CA	ASN	F	157	−17.093	56.831	−3.964	1.00	54.02	B000	C
ATOM	7662	C	ASN	F	157	−17.605	56.142	−5.227	1.00	54.32	B000	C
ATOM	7663	O	ASN	F	157	−18.209	56.814	−6.072	1.00	53.93	B000	O
ATOM	7664	CB	ASN	F	157	−16.170	57.985	−4.387	1.00	49.92	B000	C
ATOM	7665	CG	ASN	F	157	−15.632	58.759	−3.202	1.00	59.88	B000	C
ATOM	7666	OD1	ASN	F	157	−16.357	59.008	−2.236	1.00	56.12	B000	O
ATOM	7667	ND2	ASN	F	157	−14.346	59.136	−3.262	1.00	53.76	B000	N
ATOM	7668	N	TRP	F	158	−17.394	54.844	−5.396	1.00	49.14	B000	N
ATOM	7669	CA	TRP	F	158	−18.015	54.160	−6.516	1.00	47.06	B000	C
ATOM	7670	C	TRP	F	158	−19.353	53.577	−6.080	1.00	46.07	B000	C
ATOM	7671	O	TRP	F	158	−19.629	53.429	−4.891	1.00	48.01	B000	O
ATOM	7672	CB	TRP	F	158	−17.109	53.069	−7.059	1.00	48.92	B000	C
ATOM	7673	CG	TRP	F	158	−15.830	53.586	−7.632	1.00	42.48	B000	C
ATOM	7674	CD1	TRP	F	158	−14.854	54.269	−6.967	1.00	46.04	B000	C
ATOM	7675	CD2	TRP	F	158	−15.364	53.425	−8.975	1.00	40.30	B000	C
ATOM	7676	NE1	TRP	F	158	−13.811	54.549	−7.812	1.00	40.04	B000	N
ATOM	7677	CE2	TRP	F	158	−14.098	54.047	−9.053	1.00	40.63	B000	C
ATOM	7678	CE3	TRP	F	158	−15.900	52.830	−10.124	1.00	38.93	B000	C
ATOM	7679	CZ2	TRP	F	158	−13.358	54.092	−10.234	1.00	36.03	B000	C
ATOM	7680	CZ3	TRP	F	158	−15.164	52.864	−11.283	1.00	40.94	B000	C
ATOM	7681	CH2	TRP	F	158	−13.908	53.499	−11.336	1.00	38.94	B000	C
ATOM	7682	N	VAL	F	159	−20.207	53.303	−7.065	1.00	48.15	B000	N
ATOM	7683	CA	VAL	F	159	−21.584	52.872	−6.854	1.00	43.77	B000	C
ATOM	7684	C	VAL	F	159	−21.777	51.526	−7.536	1.00	53.64	B000	C
ATOM	7685	O	VAL	F	159	−21.317	51.328	−8.666	1.00	50.16	B000	O
ATOM	7686	CB	VAL	F	159	−22.571	53.918	−7.409	1.00	47.04	B000	C
ATOM	7687	CG1	VAL	F	159	−24.008	53.459	−7.275	1.00	49.61	B000	C
ATOM	7688	CG2	VAL	F	159	−22.361	55.239	−6.711	1.00	48.78	B000	C
ATOM	7689	N	GLU	F	160	−22.478	50.611	−6.864	1.00	57.06	B000	N
ATOM	7690	CA	GLU	F	160	−22.632	49.242	−7.343	1.00	56.04	B000	C
ATOM	7691	C	GLU	F	160	−23.958	49.061	−8.070	1.00	50.46	B000	C
ATOM	7692	O	GLU	F	160	−25.000	49.538	−7.619	1.00	54.39	B000	O
ATOM	7693	CB	GLU	F	160	−22.568	48.223	−6.201	1.00	59.56	B000	C
ATOM	7694	CG	GLU	F	160	−22.813	46.795	−6.710	1.00	68.99	B000	C
ATOM	7695	CD	GLU	F	160	−23.041	45.748	−5.621	1.00	80.25	B000	C
ATOM	7696	OE1	GLU	F	160	−22.777	46.016	−4.427	1.00	79.75	B000	O
ATOM	7697	OE2	GLU	F	160	−23.491	44.637	−5.985	1.00	78.26	B000	O1−
ATOM	7698	N	HIS	F	161	−23.912	48.328	−9.175	1.00	51.49	B000	N
ATOM	7699	CA	HIS	F	161	−25.104	47.913	−9.892	1.00	49.49	B000	C
ATOM	7700	C	HIS	F	161	−24.786	46.601	−10.587	1.00	53.28	B000	C
ATOM	7701	O	HIS	F	161	−23.801	46.508	−11.332	1.00	47.92	B000	O
ATOM	7702	CB	HIS	F	161	−25.561	48.959	−10.901	1.00	47.30	B000	C
ATOM	7703	CG	HIS	F	161	−26.699	48.503	−11.759	1.00	52.32	B000	C
ATOM	7704	ND1	HIS	F	161	−26.511	47.794	−12.930	1.00	49.15	B000	N
ATOM	7705	CD2	HIS	F	161	−28.039	48.641	−11.611	1.00	49.74	B000	C
ATOM	7706	CE1	HIS	F	161	−27.687	47.540	−13.478	1.00	52.61	B000	C
ATOM	7707	NE2	HIS	F	161	−28.630	48.037	−12.696	1.00	54.26	B000	N
ATOM	7708	N	GLU	F	162	−25.666	45.618	−10.386	1.00	61.24	B000	N
ATOM	7709	CA	GLU	F	162	−25.426	44.226	−10.751	1.00	57.31	B000	C
ATOM	7710	C	GLU	F	162	−24.028	43.809	−10.315	1.00	59.22	B000	C
ATOM	7711	O	GLU	F	162	−23.715	43.833	−9.118	1.00	59.32	B000	O
ATOM	7712	CB	GLU	F	162	−25.596	44.005	−12.253	1.00	54.87	B000	C
ATOM	7713	CG	GLU	F	162	−26.901	44.546	−12.835	1.00	59.80	B000	C
ATOM	7714	CD	GLU	F	162	−28.197	43.921	−12.303	1.00	84.54	B000	C
ATOM	7715	OE1	GLU	F	162	−28.210	43.290	−11.211	1.00	82.94	B000	O
ATOM	7716	OE2	GLU	F	162	−29.231	44.078	−13.007	1.00	83.83	B000	O1−
ATOM	7717	N	ARG	F	163	−23.163	43.459	−11.263	1.00	55.56	B000	N
ATOM	7718	CA	ARG	F	163	−21.811	43.028	−10.919	1.00	70.50	B000	C
ATOM	7719	C	ARG	F	163	−20.730	44.041	−11.292	1.00	65.87	B000	C
ATOM	7720	O	ARG	F	163	−19.541	43.699	−11.301	1.00	61.99	B000	O
ATOM	7721	CB	ARG	F	163	−21.533	41.645	−11.517	1.00	71.43	B000	C
ATOM	7722	CG	ARG	F	163	−22.636	40.621	−11.170	1.00	84.91	B000	C
ATOM	7723	CD	ARG	F	163	−23.371	40.027	−12.366	1.00	94.82	B000	C
ATOM	7724	NE	ARG	F	163	−23.213	38.571	−12.447	1.00	110.28	B000	N
ATOM	7725	CZ	ARG	F	163	−22.337	37.951	−13.238	1.00	109.36	B000	C
ATOM	7726	NH1	ARG	F	163	−21.538	38.656	−14.031	1.00	107.55	B000	N1+
ATOM	7727	NH2	ARG	F	163	−22.266	36.625	−13.245	1.00	108.51	B000	N
ATOM	7728	N	SER	F	164	−21.104	45.289	−11.551	1.00	62.99	B000	N
ATOM	7729	CA	SER	F	164	−20.137	46.326	−11.872	1.00	54.70	B000	C
ATOM	7730	C	SER	F	164	−20.163	47.454	−10.845	1.00	52.59	B000	C
ATOM	7731	O	SER	F	164	−21.153	47.666	−10.136	1.00	53.73	B000	O
ATOM	7732	CB	SER	F	164	−20.405	46.896	−13.272	1.00	56.24	B000	C
ATOM	7733	OG	SER	F	164	−19.909	46.041	−14.287	1.00	65.36	B000	O
ATOM	7734	N	CYS	F	165	−19.036	48.161	−10.771	1.00	51.69	B000	N
ATOM	7735	CA	CYS	F	165	−18.866	49.373	−9.981	1.00	51.61	B000	C
ATOM	7736	C	CYS	F	165	−18.723	50.574	−10.909	1.00	50.55	B000	C
ATOM	7737	O	CYS	F	165	−18.004	50.511	−11.912	1.00	48.71	B000	O
ATOM	7738	CB	CYS	F	165	−17.633	49.280	−9.076	1.00	55.01	B000	C
ATOM	7739	SG	CYS	F	165	−17.771	48.053	−7.751	1.00	71.45	B000	S
ATOM	7740	N	TYR	F	166	−19.410	51.670	−10.577	1.00	48.64	B000	N
ATOM	7741	CA	TYR	F	166	−19.481	52.838	−11.449	1.00	45.58	B000	C
ATOM	7742	C	TYR	F	166	−19.040	54.104	−10.722	1.00	51.09	B000	C
ATOM	7743	O	TYR	F	166	−19.325	54.283	−9.533	1.00	49.78	B000	O
ATOM	7744	CB	TYR	F	166	−20.886	53.045	−11.982	1.00	39.51	B000	C
ATOM	7745	CG	TYR	F	166	−21.427	51.889	−12.777	1.00	45.13	B000	C
ATOM	7746	CD1	TYR	F	166	−21.884	50.732	−12.151	1.00	50.08	B000	C
ATOM	7747	CD2	TYR	F	166	−21.471	51.945	−14.159	1.00	46.42	B000	C
ATOM	7748	CE1	TYR	F	166	−22.393	49.667	−12.887	1.00	48.67	B000	C
ATOM	7749	CE2	TYR	F	166	−21.968	50.892	−14.902	1.00	52.75	B000	C
ATOM	7750	CZ	TYR	F	166	−22.429	49.752	−14.264	1.00	51.87	B000	C
ATOM	7751	OH	TYR	F	166	−22.922	48.712	−15.024	1.00	47.43	B000	O
ATOM	7752	N	TRP	F	167	−18.358	54.989	−11.446	1.00	41.54	B000	N
ATOM	7753	CA	TRP	F	167	−17.941	56.279	−10.914	1.00	39.17	B000	C
ATOM	7754	C	TRP	F	167	−18.472	57.396	−11.821	1.00	40.61	B000	C
ATOM	7755	O	TRP	F	167	−18.300	57.352	−13.048	1.00	39.85	B000	O
ATOM	7756	CB	TRP	F	167	−16.408	56.328	−10.776	1.00	39.26	B000	C
ATOM	7757	CG	TRP	F	167	−15.921	57.583	−10.131	1.00	47.81	B000	C
ATOM	7758	CD1	TRP	F	167	−15.728	57.812	−8.787	1.00	43.33	B000	C
ATOM	7759	CD2	TRP	F	167	−15.599	58.806	−10.799	1.00	36.88	B000	C
ATOM	7760	NE1	TRP	F	167	−15.292	59.110	−8.588	1.00	37.39	B000	N
ATOM	7761	CE2	TRP	F	167	−15.191	59.735	−9.807	1.00	42.60	B000	C
ATOM	7762	CE3	TRP	F	167	−15.593	59.202	−12.140	1.00	35.30	B000	C
ATOM	7763	CZ2	TRP	F	167	−14.796	61.049	−10.122	1.00	32.52	B000	C
ATOM	7764	CZ3	TRP	F	167	−15.177	60.506	−12.455	1.00	41.65	B000	C
ATOM	7765	CH2	TRP	F	167	−14.805	61.415	−11.442	1.00	34.25	B000	C
ATOM	7766	N	PHE	F	168	−19.128	58.386	−11.215	1.00	32.85	B000	N
ATOM	7767	CA	PHE	F	168	−19.816	59.459	−11.933	1.00	36.14	B000	C
ATOM	7768	C	PHE	F	168	−19.062	60.768	−11.757	1.00	33.17	B000	C
ATOM	7769	O	PHE	F	168	−18.933	61.266	−10.640	1.00	32.62	B000	O
ATOM	7770	CB	PHE	F	168	−21.257	59.611	−11.439	1.00	31.85	B000	C
ATOM	7771	CG	PHE	F	168	−22.092	58.410	−11.718	1.00	43.90	B000	C
ATOM	7772	CD1	PHE	F	168	−22.788	58.303	−12.918	1.00	37.94	B000	C
ATOM	7773	CD2	PHE	F	168	−22.121	57.349	−10.824	1.00	37.92	B000	C
ATOM	7774	CE1	PHE	F	168	−23.534	57.188	−13.204	1.00	33.97	B000	C
ATOM	7775	CE2	PHE	F	168	−22.863	56.231	−11.102	1.00	43.27	B000	C
ATOM	7776	CZ	PHE	F	168	−23.576	56.147	−12.299	1.00	39.89	B000	C
ATOM	7777	N	SER	F	169	−18.544	61.311	−12.851	1.00	34.64	B000	N
ATOM	7778	CA	SER	F	169	−17.896	62.613	−12.753	1.00	37.47	B000	C
ATOM	7779	C	SER	F	169	−18.933	63.691	−12.453	1.00	35.48	B000	C
ATOM	7780	O	SER	F	169	−20.132	63.531	−12.708	1.00	35.12	B000	O
ATOM	7781	CB	SER	F	169	−17.154	62.974	−14.046	1.00	31.74	B000	C
ATOM	7782	OG	SER	F	169	−18.061	63.533	−14.999	1.00	33.74	B000	O
ATOM	7783	N	ARG	F	170	−18.454	64.810	−11.921	1.00	32.66	B000	N
ATOM	7784	CA	ARG	F	170	−19.292	65.983	−11.718	1.00	35.64	B000	C
ATOM	7785	C	ARG	F	170	−18.692	67.198	−12.423	1.00	37.46	B000	C
ATOM	7786	O	ARG	F	170	−18.918	68.347	−12.037	1.00	32.51	B000	O
ATOM	7787	CB	ARG	F	170	−19.527	66.211	−10.228	1.00	30.96	B000	C
ATOM	7788	CG	ARG	F	170	−20.457	65.128	−9.645	1.00	33.93	B000	C
ATOM	7789	CD	ARG	F	170	−20.628	65.237	−8.142	1.00	36.53	B000	C
ATOM	7790	NE	ARG	F	170	−19.466	64.712	−7.440	1.00	46.87	B000	N
ATOM	7791	CZ	ARG	F	170	−19.272	64.766	−6.121	1.00	50.98	B000	C
ATOM	7792	NH1	ARG	F	170	−18.153	64.253	−5.600	1.00	44.20	B000	N1+
ATOM	7793	NH2	ARG	F	170	−20.184	65.325	−5.321	1.00	43.86	B000	N
ATOM	7794	N	SER	F	171	−17.935	66.933	−13.484	1.00	32.24	B000	N
ATOM	7795	CA	SER	F	171	−17.355	67.964	−14.328	1.00	32.82	B000	C
ATOM	7796	C	SER	F	171	−17.068	67.317	−15.673	1.00	33.70	B000	C
ATOM	7797	O	SER	F	171	−17.093	66.090	−15.807	1.00	32.42	B000	O
ATOM	7798	CB	SER	F	171	−16.078	68.565	−13.724	1.00	32.95	B000	C
ATOM	7799	OG	SER	F	171	−15.041	67.584	−13.595	1.00	37.93	B000	O
ATOM	7800	N	GLY	F	172	−16.766	68.160	−16.662	1.00	27.87	B000	N
ATOM	7801	CA	GLY	F	172	−16.607	67.725	−18.032	1.00	30.72	B000	C
ATOM	7802	C	GLY	F	172	−15.165	67.477	−18.471	1.00	37.04	B000	C
ATOM	7803	O	GLY	F	172	−14.203	68.006	−17.891	1.00	31.19	B000	O
ATOM	7804	N	LYS	F	173	−15.039	66.642	−19.510	1.00	31.65	B000	N
ATOM	7805	CA	LYS	F	173	−13.782	66.382	−20.205	1.00	34.23	B000	C
ATOM	7806	C	LYS	F	173	−14.091	66.048	−21.659	1.00	34.10	B000	C
ATOM	7807	O	LYS	F	173	−15.137	65.468	−21.967	1.00	27.67	B000	O
ATOM	7808	CB	LYS	F	173	−12.986	65.212	−19.599	1.00	36.67	B000	C
ATOM	7809	CG	LYS	F	173	−12.212	65.491	−18.319	1.00	36.30	B000	C
ATOM	7810	CD	LYS	F	173	−11.406	64.251	−17.943	1.00	31.78	B000	C
ATOM	7811	CE	LYS	F	173	−10.707	64.369	−16.569	1.00	33.56	B000	C
ATOM	7812	NZ	LYS	F	173	−9.556	65.313	−16.523	1.00	45.73	B000	N1+
ATOM	7813	N	ALA	F	174	−13.167	66.400	−22.557	1.00	31.22	B000	N
ATOM	7814	CA	ALA	F	174	−13.226	65.821	−23.890	1.00	31.29	B000	C
ATOM	7815	C	ALA	F	174	−13.149	64.297	−23.774	1.00	30.96	B000	C
ATOM	7816	O	ALA	F	174	−12.525	63.758	−22.851	1.00	33.23	B000	O
ATOM	7817	CB	ALA	F	174	−12.099	66.364	−24.763	1.00	29.41	B000	C
ATOM	7818	N	TRP	F	175	−13.823	63.602	−24.698	1.00	28.04	B000	N
ATOM	7819	CA	TRP	F	175	−13.972	62.145	−24.586	1.00	34.38	B000	C
ATOM	7820	C	TRP	F	175	−12.623	61.449	−24.421	1.00	37.26	B000	C
ATOM	7821	O	TRP	F	175	−12.450	60.587	−23.549	1.00	35.08	B000	O
ATOM	7822	CB	TRP	F	175	−14.700	61.599	−25.815	1.00	28.70	B000	C
ATOM	7823	CG	TRP	F	175	−15.152	60.160	−25.730	1.00	37.75	B000	C
ATOM	7824	CD1	TRP	F	175	−16.401	59.702	−25.374	1.00	32.61	B000	C
ATOM	7825	CD2	TRP	F	175	−14.381	58.992	−26.056	1.00	35.80	B000	C
ATOM	7826	NE1	TRP	F	175	−16.440	58.337	−25.446	1.00	36.32	B000	N
ATOM	7827	CE2	TRP	F	175	−15.219	57.874	−25.866	1.00	39.10	B000	C
ATOM	7828	CE3	TRP	F	175	−13.067	58.786	−26.488	1.00	34.63	B000	C
ATOM	7829	CZ2	TRP	F	175	−14.788	56.573	−26.097	1.00	34.59	B000	C
ATOM	7830	CZ3	TRP	F	175	−12.637	57.494	−26.720	1.00	37.06	B000	C
ATOM	7831	CH2	TRP	F	175	−13.493	56.402	−26.517	1.00	41.92	B000	C
ATOM	7832	N	ALA	F	176	−11.637	61.842	−25.230	1.00	31.21	B000	N
ATOM	7833	CA	ALA	F	176	−10.356	61.158	−25.149	1.00	35.56	B000	C
ATOM	7834	C	ALA	F	176	−9.749	61.306	−23.765	1.00	38.45	B000	C
ATOM	7835	O	ALA	F	176	−9.108	60.373	−23.270	1.00	39.51	B000	O
ATOM	7836	CB	ALA	F	176	−9.403	61.684	−26.229	1.00	24.62	B000	C
ATOM	7837	N	ASP	F	177	−9.964	62.449	−23.107	1.00	34.61	B000	N
ATOM	7838	CA	ASP	F	177	−9.426	62.601	−21.759	1.00	35.23	B000	C
ATOM	7839	C	ASP	F	177	−10.233	61.808	−20.751	1.00	37.46	B000	C
ATOM	7840	O	ASP	F	177	−9.663	61.241	−19.812	1.00	34.54	B000	O
ATOM	7841	CB	ASP	F	177	−9.379	64.072	−21.351	1.00	34.09	B000	C
ATOM	7842	CG	ASP	F	177	−8.386	64.859	−22.167	1.00	41.05	B000	C
ATOM	7843	OD1	ASP	F	177	−7.313	64.292	−22.458	1.00	42.78	B000	O
ATOM	7844	OD2	ASP	F	177	−8.681	66.028	−22.531	1.00	43.34	B000	O1−
ATOM	7845	N	ALA	F	178	−11.561	61.775	−20.907	1.00	34.72	B000	N
ATOM	7846	CA	ALA	F	178	−12.357	60.941	−20.010	1.00	40.52	B000	C
ATOM	7847	C	ALA	F	178	−11.978	59.471	−20.186	1.00	36.67	B000	C
ATOM	7848	O	ALA	F	178	−11.853	58.724	−19.208	1.00	36.37	B000	O
ATOM	7849	CB	ALA	F	178	−13.850	61.165	−20.268	1.00	32.74	B000	C
ATOM	7850	N	ASP	F	179	−11.714	59.070	−21.424	1.00	34.82	B000	N
ATOM	7851	CA	ASP	F	179	−11.257	57.715	−21.706	1.00	36.26	B000	C
ATOM	7852	C	ASP	F	179	−9.957	57.397	−20.955	1.00	42.39	B000	C
ATOM	7853	O	ASP	F	179	−9.861	56.368	−20.275	1.00	44.65	B000	O
ATOM	7854	CB	ASP	F	179	−11.107	57.584	−23.221	1.00	41.84	B000	C
ATOM	7855	CG	ASP	F	179	−10.618	56.220	−23.670	1.00	52.24	B000	C
ATOM	7856	OD1	ASP	F	179	−11.237	55.192	−23.304	1.00	48.91	B000	O
ATOM	7857	OD2	ASP	F	179	−9.620	56.195	−24.430	1.00	51.25	B000	O1−
ATOM	7858	N	ASN	F	180	−8.959	58.292	−21.019	1.00	36.75	B000	N
ATOM	7859	CA	ASN	F	180	−7.704	58.044	−20.302	1.00	37.14	B000	C
ATOM	7860	C	ASN	F	180	−7.923	58.008	−18.796	1.00	39.01	B000	C
ATOM	7861	O	ASN	F	180	−7.306	57.205	−18.089	1.00	45.89	B000	O
ATOM	7862	CB	ASN	F	180	−6.654	59.118	−20.615	1.00	46.92	B000	C
ATOM	7863	CG	ASN	F	180	−6.153	59.087	−22.053	1.00	58.49	B000	C
ATOM	7864	OD1	ASN	F	180	−6.232	58.070	−22.751	1.00	61.49	B000	O
ATOM	7865	ND2	ASN	F	180	−5.630	60.232	−22.507	1.00	67.59	B000	N
ATOM	7866	N	TYR	F	181	−8.782	58.887	−18.283	1.00	43.70	B000	N
ATOM	7867	CA	TYR	F	181	−9.073	58.899	−16.852	1.00	39.91	B000	C
ATOM	7868	C	TYR	F	181	−9.597	57.540	−16.394	1.00	37.95	B000	C
ATOM	7869	O	TYR	F	181	−9.186	57.026	−15.351	1.00	39.77	B000	O
ATOM	7870	CB	TYR	F	181	−10.089	60.009	−16.524	1.00	38.63	B000	C
ATOM	7871	CG	TYR	F	181	−10.493	60.066	−15.056	1.00	41.58	B000	C
ATOM	7872	CD1	TYR	F	181	−11.438	59.167	−14.527	1.00	31.11	B000	C
ATOM	7873	CD2	TYR	F	181	−9.928	61.018	−14.193	1.00	31.82	B000	C
ATOM	7874	CE1	TYR	F	181	−11.782	59.205	−13.193	1.00	31.20	B000	C
ATOM	7875	CE2	TYR	F	181	−10.285	61.067	−12.856	1.00	32.07	B000	C
ATOM	7876	CZ	TYR	F	181	−11.206	60.153	−12.364	1.00	37.73	B000	C
ATOM	7877	OH	TYR	F	181	−11.565	60.192	−11.049	1.00	44.00	B000	O
ATOM	7878	N	CYS	F	182	−10.545	56.962	−17.133	1.00	38.33	B000	N
ATOM	7879	CA	CYS	F	182	−11.080	55.671	−16.702	1.00	46.48	B000	C
ATOM	7880	C	CYS	F	182	−10.008	54.591	−16.772	1.00	43.13	B000	C
ATOM	7881	O	CYS	F	182	−9.877	53.782	−15.848	1.00	43.36	B000	O
ATOM	7882	CB	CYS	F	182	−12.309	55.282	−17.529	1.00	39.09	B000	C
ATOM	7883	SG	CYS	F	182	−13.808	56.319	−17.269	1.00	47.89	B000	S
ATOM	7884	N	ARG	F	183	−9.196	54.599	−17.834	1.00	45.20	B000	N
ATOM	7885	CA	ARG	F	183	−8.147	53.596	−17.968	1.00	43.53	B000	C
ATOM	7886	C	ARG	F	183	−7.166	53.667	−16.806	1.00	46.41	B000	C
ATOM	7887	O	ARG	F	183	−6.782	52.629	−16.254	1.00	47.85	B000	O
ATOM	7888	CB	ARG	F	183	−7.439	53.764	−19.316	1.00	41.85	B000	C
ATOM	7889	CG	ARG	F	183	−8.193	53.051	−20.444	1.00	61.73	B000	C
ATOM	7890	CD	ARG	F	183	−7.918	53.573	−21.866	1.00	68.72	B000	C
ATOM	7891	NE	ARG	F	183	−8.968	53.099	−22.784	1.00	81.47	B000	N
ATOM	7892	CZ	ARG	F	183	−9.062	53.405	−24.082	1.00	84.12	B000	C
ATOM	7893	NH1	ARG	F	183	−8.149	54.199	−24.652	1.00	78.81	B000	N1+
ATOM	7894	NH2	ARG	F	183	−10.082	52.925	−24.811	1.00	60.08	B000	N
ATOM	7895	N	LEU	F	184	−6.805	54.884	−16.367	1.00	42.66	B000	N
ATOM	7896	CA	LEU	F	184	−5.910	55.030	−15.220	1.00	41.52	B000	C
ATOM	7897	C	LEU	F	184	−6.542	54.558	−13.921	1.00	45.58	B000	C
ATOM	7898	O	LEU	F	184	−5.822	54.349	−12.944	1.00	51.35	B000	O
ATOM	7899	CB	LEU	F	184	−5.441	56.481	−15.057	1.00	36.16	B000	C
ATOM	7900	CG	LEU	F	184	−4.410	57.032	−16.056	1.00	52.39	B000	C
ATOM	7901	CD1	LEU	F	184	−4.128	58.507	−15.803	1.00	41.04	B000	C
ATOM	7902	CD2	LEU	F	184	−3.105	56.258	−15.999	1.00	43.74	B000	C
ATOM	7903	N	GLU	F	185	−7.862	54.403	−13.875	1.00	49.78	B000	N
ATOM	7904	CA	GLU	F	185	−8.548	53.829	−12.724	1.00	54.22	B000	C
ATOM	7905	C	GLU	F	185	−8.765	52.324	−12.849	1.00	48.30	B000	C
ATOM	7906	O	GLU	F	185	−9.579	51.769	−12.104	1.00	50.24	B000	O
ATOM	7907	CB	GLU	F	185	−9.905	54.506	−12.523	1.00	53.96	B000	C
ATOM	7908	CG	GLU	F	185	−9.835	55.994	−12.368	1.00	48.05	B000	C
ATOM	7909	CD	GLU	F	185	−9.246	56.395	−11.042	1.00	60.24	B000	C
ATOM	7910	OE1	GLU	F	185	−9.666	55.804	−10.016	1.00	64.06	B000	O
ATOM	7911	OE2	GLU	F	185	−8.376	57.300	−11.033	1.00	63.60	B000	O1−
ATOM	7912	N	ASP	F	186	−8.062	51.659	−13.765	1.00	48.69	B000	N
ATOM	7913	CA	ASP	F	186	−8.311	50.254	−14.090	1.00	49.60	B000	C
ATOM	7914	C	ASP	F	186	−9.782	50.054	−14.431	1.00	52.34	B000	C
ATOM	7915	O	ASP	F	186	−10.445	49.131	−13.950	1.00	49.55	B000	O
ATOM	7916	CB	ASP	F	186	−7.889	49.319	−12.951	1.00	53.42	B000	C
ATOM	7917	CG	ASP	F	186	−6.443	49.508	−12.545	1.00	79.16	B000	C
ATOM	7918	OD1	ASP	F	186	−5.652	50.034	−13.366	1.00	85.17	B000	O
ATOM	7919	OD2	ASP	F	186	−6.093	49.125	−11.403	1.00	86.75	B000	O1−
ATOM	7920	N	ALA	F	187	−10.303	50.958	−15.252	1.00	50.66	B000	N
ATOM	7921	CA	ALA	F	187	−11.705	50.915	−15.627	1.00	43.40	B000	C
ATOM	7922	C	ALA	F	187	−11.822	51.404	−17.061	1.00	39.32	B000	C
ATOM	7923	O	ALA	F	187	−10.822	51.623	−17.752	1.00	42.43	B000	O
ATOM	7924	CB	ALA	F	187	−12.559	51.716	−14.636	1.00	37.47	B000	C
ATOM	7925	N	HIS	F	188	−13.048	51.547	−17.523	1.00	38.43	B000	N
ATOM	7926	CA	HIS	F	188	−13.273	52.036	−18.864	1.00	42.96	B000	C
ATOM	7927	C	HIS	F	188	−14.539	52.878	−18.839	1.00	39.88	B000	C
ATOM	7928	O	HIS	F	188	−15.291	52.871	−17.865	1.00	47.38	B000	O
ATOM	7929	CB	HIS	F	188	−13.377	50.872	−19.852	1.00	40.78	B000	C
ATOM	7930	CG	HIS	F	188	−14.461	49.901	−19.512	1.00	40.48	B000	C
ATOM	7931	ND1	HIS	F	188	−15.783	50.124	−19.830	1.00	46.61	B000	N
ATOM	7932	CD2	HIS	F	188	−14.427	48.716	−18.858	1.00	45.33	B000	C
ATOM	7933	CE1	HIS	F	188	−16.515	49.109	−19.403	1.00	45.57	B000	C
ATOM	7934	NE2	HIS	F	188	−15.716	48.241	−18.811	1.00	46.51	B000	N
ATOM	7935	N	LEU	F	189	−14.764	53.613	−19.918	1.00	37.01	B000	N
ATOM	7936	CA	LEU	F	189	−15.978	54.400	−20.036	1.00	37.46	B000	C
ATOM	7937	C	LEU	F	189	−17.191	53.475	−20.121	1.00	43.07	B000	C
ATOM	7938	O	LEU	F	189	−17.135	52.415	−20.754	1.00	37.38	B000	O
ATOM	7939	CB	LEU	F	189	−15.891	55.299	−21.263	1.00	31.01	B000	C
ATOM	7940	CG	LEU	F	189	−14.995	56.532	−21.160	1.00	35.76	B000	C
ATOM	7941	CD1	LEU	F	189	−14.766	57.097	−22.537	1.00	33.40	B000	C
ATOM	7942	CD2	LEU	F	189	−15.624	57.607	−20.257	1.00	34.63	B000	C
ATOM	7943	N	VAL	F	190	−18.301	53.904	−19.502	1.00	37.96	B000	N
ATOM	7944	CA	VAL	F	190	−19.417	53.006	−19.237	1.00	34.67	B000	C
ATOM	7945	C	VAL	F	190	−19.928	52.393	−20.536	1.00	42.14	B000	C
ATOM	7946	O	VAL	F	190	−20.044	53.064	−21.573	1.00	40.38	B000	O
ATOM	7947	CB	VAL	F	190	−20.551	53.722	−18.477	1.00	36.38	B000	C
ATOM	7948	CG1	VAL	F	190	−21.205	54.857	−19.319	1.00	31.50	B000	C
ATOM	7949	CG2	VAL	F	190	−21.573	52.718	−18.006	1.00	38.12	B000	C
ATOM	7950	N	VAL	F	191	−20.178	51.085	−20.485	1.00	40.92	B000	N
ATOM	7951	CA	VAL	F	191	−20.787	50.325	−21.567	1.00	40.00	B000	C
ATOM	7952	C	VAL	F	191	−22.162	49.884	−21.082	1.00	41.46	B000	C
ATOM	7953	O	VAL	F	191	−22.265	49.187	−20.063	1.00	51.69	B000	O
ATOM	7954	CB	VAL	F	191	−19.928	49.113	−21.966	1.00	43.90	B000	C
ATOM	7955	CG1	VAL	F	191	−20.596	48.350	−23.106	1.00	38.60	B000	C
ATOM	7956	CG2	VAL	F	191	−18.503	49.546	−22.338	1.00	38.08	B000	C
ATOM	7957	N	VAL	F	192	−23.209	50.284	−21.805	1.00	39.60	B000	N
ATOM	7958	CA	VAL	F	192	−24.603	50.091	−21.402	1.00	40.55	B000	C
ATOM	7959	C	VAL	F	192	−25.139	48.872	−22.134	1.00	42.33	B000	C
ATOM	7960	O	VAL	F	192	−25.454	48.955	−23.326	1.00	43.63	B000	O
ATOM	7961	CB	VAL	F	192	−25.464	51.319	−21.747	1.00	43.28	B000	C
ATOM	7962	CG1	VAL	F	192	−26.869	51.182	−21.155	1.00	32.94	B000	C
ATOM	7963	CG2	VAL	F	192	−24.772	52.629	−21.333	1.00	35.84	B000	C
ATOM	7964	N	THR	F	193	−25.341	47.762	−21.429	1.00	48.94	B000	N
ATOM	7965	CA	THR	F	193	−25.745	46.531	−22.105	1.00	47.71	B000	C
ATOM	7966	C	THR	F	193	−27.211	46.169	−21.896	1.00	49.57	B000	C
ATOM	7967	O	THR	F	193	−27.654	45.172	−22.465	1.00	51.89	B000	O
ATOM	7968	CB	THR	F	193	−24.866	45.344	−21.673	1.00	37.74	B000	C
ATOM	7969	OG1	THR	F	193	−25.053	45.097	−20.280	1.00	43.14	B000	O
ATOM	7970	CG2	THR	F	193	−23.361	45.624	−21.935	1.00	34.77	B000	C
ATOM	7971	N	SER	F	194	−27.986	46.957	−21.143	1.00	45.16	B000	N
ATOM	7972	CA	SER	F	194	−29.364	46.570	−20.845	1.00	43.88	B000	C
ATOM	7973	C	SER	F	194	−30.163	47.775	−20.395	1.00	47.69	B000	C
ATOM	7974	O	SER	F	194	−29.609	48.782	−19.938	1.00	48.48	B000	O
ATOM	7975	CB	SER	F	194	−29.443	45.506	−19.738	1.00	52.95	B000	C
ATOM	7976	OG	SER	F	194	−29.162	46.065	−18.455	1.00	47.85	B000	O
ATOM	7977	N	TRP	F	195	−31.488	47.622	−20.464	1.00	48.46	B000	N
ATOM	7978	CA	TRP	F	195	−32.386	48.680	−20.012	1.00	44.88	B000	C
ATOM	7979	C	TRP	F	195	−32.160	49.001	−18.546	1.00	47.13	B000	C
ATOM	7980	O	TRP	F	195	−32.238	50.165	−18.133	1.00	45.99	B000	O
ATOM	7981	CB	TRP	F	195	−33.843	48.288	−20.250	1.00	41.25	B000	C
ATOM	7982	CG	TRP	F	195	−34.410	48.910	−21.469	1.00	54.27	B000	C
ATOM	7983	CD1	TRP	F	195	−34.863	48.275	−22.601	1.00	50.60	B000	C
ATOM	7984	CD2	TRP	F	195	−34.541	50.319	−21.716	1.00	55.13	B000	C
ATOM	7985	NE1	TRP	F	195	−35.307	49.212	−23.521	1.00	52.12	B000	N
ATOM	7986	CE2	TRP	F	195	−35.114	50.470	−23.005	1.00	54.46	B000	C
ATOM	7987	CE3	TRP	F	195	−34.246	51.467	−20.964	1.00	50.27	B000	C
ATOM	7988	CZ2	TRP	F	195	−35.391	51.727	−23.561	1.00	62.09	B000	C
ATOM	7989	CZ3	TRP	F	195	−34.530	52.721	−21.513	1.00	54.11	B000	C
ATOM	7990	CH2	TRP	F	195	−35.091	52.837	−22.804	1.00	59.63	B000	C
ATOM	7991	N	GLU	F	196	−31.875	47.980	−17.747	1.00	43.73	B000	N
ATOM	7992	CA	GLU	F	196	−31.638	48.202	−16.330	1.00	46.25	B000	C
ATOM	7993	C	GLU	F	196	−30.421	49.094	−16.133	1.00	48.83	B000	C
ATOM	7994	O	GLU	F	196	−30.505	50.141	−15.480	1.00	50.61	B000	O
ATOM	7995	CB	GLU	F	196	−31.445	46.853	−15.623	1.00	52.52	B000	C
ATOM	7996	CG	GLU	F	196	−32.744	46.023	−15.500	1.00	56.68	B000	C
ATOM	7997	CD	GLU	F	196	−33.141	45.323	−16.823	1.00	67.73	B000	C
ATOM	7998	OE1	GLU	F	196	−32.250	45.039	−17.660	1.00	66.56	B000	O
ATOM	7999	OE2	GLU	F	196	−34.348	45.063	−17.030	1.00	76.24	B000	O1−
ATOM	8000	N	GLU	F	197	−29.293	48.717	−16.744	1.00	40.21	B000	N
ATOM	8001	CA	GLU	F	197	−28.089	49.533	−16.666	1.00	46.56	B000	C
ATOM	8002	C	GLU	F	197	−28.364	50.956	−17.149	1.00	46.02	B000	C
ATOM	8003	O	GLU	F	197	−27.964	51.927	−16.494	1.00	39.09	B000	O
ATOM	8004	CB	GLU	F	197	−26.965	48.881	−17.475	1.00	41.68	B000	C
ATOM	8005	CG	GLU	F	197	−25.566	49.351	−17.097	1.00	46.61	B000	C
ATOM	8006	CD	GLU	F	197	−24.465	48.581	−17.830	1.00	49.56	B000	C
ATOM	8007	OE1	GLU	F	197	−24.781	47.861	−18.816	1.00	45.94	B000	O
ATOM	8008	OE2	GLU	F	197	−23.283	48.692	−17.413	1.00	45.17	B000	O1−
ATOM	8009	N	GLN	F	198	−29.087	51.091	−18.271	1.00	37.03	B000	N
ATOM	8010	CA	GLN	F	198	−29.451	52.403	−18.794	1.00	36.33	B000	C
ATOM	8011	C	GLN	F	198	−30.217	53.231	−17.769	1.00	44.55	B000	C
ATOM	8012	O	GLN	F	198	−29.896	54.400	−17.546	1.00	40.80	B000	O
ATOM	8013	CB	GLN	F	198	−30.275	52.248	−20.065	1.00	35.40	B000	C
ATOM	8014	CG	GLN	F	198	−31.035	53.513	−20.445	1.00	35.73	B000	C
ATOM	8015	CD	GLN	F	198	−30.137	54.563	−21.106	1.00	43.38	B000	C
ATOM	8016	OE1	GLN	F	198	−29.107	54.240	−21.704	1.00	38.10	B000	O
ATOM	8017	NE2	GLN	F	198	−30.535	55.821	−21.007	1.00	38.22	B000	N
ATOM	8018	N	LYS	F	199	−31.229	52.641	−17.123	1.00	47.51	B000	N
ATOM	8019	CA	LYS	F	199	−32.018	53.399	−16.154	1.00	44.51	B000	C
ATOM	8020	C	LYS	F	199	−31.196	53.714	−14.918	1.00	39.60	B000	C
ATOM	8021	O	LYS	F	199	−31.308	54.805	−14.351	1.00	43.02	B000	O
ATOM	8022	CB	LYS	F	199	−33.276	52.619	−15.760	1.00	48.82	B000	C
ATOM	8023	CG	LYS	F	199	−34.257	52.311	−16.891	1.00	50.78	B000	C
ATOM	8024	CD	LYS	F	199	−35.683	52.463	−16.392	1.00	65.99	B000	C
ATOM	8025	CE	LYS	F	199	−36.698	51.763	−17.281	1.00	72.04	B000	C
ATOM	8026	NZ	LYS	F	199	−38.023	51.636	−16.575	1.00	76.98	B000	N1+
ATOM	8027	N	PHE	F	200	−30.351	52.773	−14.502	1.00	38.71	B000	N
ATOM	8028	CA	PHE	F	200	−29.447	53.007	−13.388	1.00	38.04	B000	C
ATOM	8029	C	PHE	F	200	−28.557	54.224	−13.641	1.00	47.55	B000	C
ATOM	8030	O	PHE	F	200	−28.381	55.073	−12.761	1.00	42.70	B000	O
ATOM	8031	CB	PHE	F	200	−28.604	51.759	−13.163	1.00	40.51	B000	C
ATOM	8032	CG	PHE	F	200	−27.381	51.999	−12.347	1.00	41.69	B000	C
ATOM	8033	CD1	PHE	F	200	−27.473	52.215	−10.980	1.00	38.29	B000	C
ATOM	8034	CD2	PHE	F	200	−26.130	52.027	−12.953	1.00	37.96	B000	C
ATOM	8035	CE1	PHE	F	200	−26.330	52.448	−10.216	1.00	42.63	B000	C
ATOM	8036	CE2	PHE	F	200	−24.978	52.252	−12.205	1.00	39.67	B000	C
ATOM	8037	CZ	PHE	F	200	−25.076	52.466	−10.830	1.00	44.08	B000	C
ATOM	8038	N	VAL	F	201	−27.984	54.328	−14.842	1.00	43.83	B000	N
ATOM	8039	CA	VAL	F	201	−27.087	55.445	−15.131	1.00	40.81	B000	C
ATOM	8040	C	VAL	F	201	−27.865	56.756	−15.182	1.00	44.68	B000	C
ATOM	8041	O	VAL	F	201	−27.442	57.758	−14.596	1.00	42.14	B000	O
ATOM	8042	CB	VAL	F	201	−26.313	55.196	−16.438	1.00	40.73	B000	C
ATOM	8043	CG1	VAL	F	201	−25.631	56.475	−16.900	1.00	38.56	B000	C
ATOM	8044	CG2	VAL	F	201	−25.297	54.053	−16.260	1.00	34.68	B000	C
ATOM	8045	N	GLN	F	202	−29.005	56.768	−15.894	1.00	37.85	B000	N
ATOM	8046	CA	GLN	F	202	−29.859	57.956	−15.959	1.00	43.72	B000	C
ATOM	8047	C	GLN	F	202	−30.185	58.499	−14.582	1.00	46.87	B000	C
ATOM	8048	O	GLN	F	202	−30.211	59.720	−14.367	1.00	46.96	B000	O
ATOM	8049	CB	GLN	F	202	−31.184	57.645	−16.634	1.00	43.62	B000	C
ATOM	8050	CG	GLN	F	202	−31.156	57.250	−18.044	1.00	46.33	B000	C
ATOM	8051	CD	GLN	F	202	−32.572	57.120	−18.537	1.00	50.37	B000	C
ATOM	8052	OE1	GLN	F	202	−32.871	56.353	−19.451	1.00	47.40	B000	O
ATOM	8053	NE2	GLN	F	202	−33.469	57.864	−17.901	1.00	48.25	B000	N
ATOM	8054	N	HIS	F	203	−30.503	57.603	−13.654	1.00	41.20	B000	N
ATOM	8055	CA	HIS	F	203	−30.825	58.034	−12.307	1.00	44.02	B000	C
ATOM	8056	C	HIS	F	203	−29.701	58.866	−11.707	1.00	47.89	B000	C
ATOM	8057	O	HIS	F	203	−29.958	59.896	−11.078	1.00	47.99	B000	O
ATOM	8058	CB	HIS	F	203	−31.106	56.827	−11.421	1.00	40.71	B000	C
ATOM	8059	CG	HIS	F	203	−31.413	57.206	−10.013	1.00	53.47	B000	C
ATOM	8060	ND1	HIS	F	203	−30.514	57.028	−8.982	1.00	56.30	B000	N
ATOM	8061	CD2	HIS	F	203	−32.499	57.805	−9.470	1.00	46.30	B000	C
ATOM	8062	CE1	HIS	F	203	−31.044	57.478	−7.858	1.00	55.89	B000	C
ATOM	8063	NE2	HIS	F	203	−32.248	57.953	−8.127	1.00	56.08	B000	N
ATOM	8064	N	HIS	F	204	−28.444	58.458	−11.918	1.00	41.43	B000	N
ATOM	8065	CA	HIS	F	204	−27.328	59.148	−11.283	1.00	39.37	B000	C
ATOM	8066	C	HIS	F	204	−26.814	60.355	−12.055	1.00	40.69	B000	C
ATOM	8067	O	HIS	F	204	−26.317	61.291	−11.426	1.00	42.64	B000	O
ATOM	8068	CB	HIS	F	204	−26.174	58.188	−11.035	1.00	43.78	B000	C
ATOM	8069	CG	HIS	F	204	−26.401	57.295	−9.864	1.00	48.22	B000	C
ATOM	8070	ND1	HIS	F	204	−26.903	56.017	−9.983	1.00	46.54	B000	N
ATOM	8071	CD2	HIS	F	204	−26.255	57.524	−8.538	1.00	40.29	B000	C
ATOM	8072	CE1	HIS	F	204	−27.021	55.484	−8.781	1.00	48.73	B000	C
ATOM	8073	NE2	HIS	F	204	−26.638	56.378	−7.887	1.00	42.03	B000	N
ATOM	8074	N	ILE	F	205	−26.916	60.374	−13.387	1.00	37.14	B000	N
ATOM	8075	CA	ILE	F	205	−26.350	61.499	−14.131	1.00	36.61	B000	C
ATOM	8076	C	ILE	F	205	−27.319	62.674	−14.148	1.00	42.45	B000	C
ATOM	8077	O	ILE	F	205	−26.895	63.820	−14.292	1.00	40.59	B000	O
ATOM	8078	CB	ILE	F	205	−25.950	61.116	−15.576	1.00	34.16	B000	C
ATOM	8079	CG1	ILE	F	205	−27.167	60.709	−16.402	1.00	34.84	B000	C
ATOM	8080	CG2	ILE	F	205	−24.871	60.040	−15.609	1.00	29.47	B000	C
ATOM	8081	CD1	ILE	F	205	−26.829	60.403	−17.814	1.00	37.88	B000	C
ATOM	8082	N	GLY	F	206	−28.620	62.416	−14.017	1.00	43.01	B000	N
ATOM	8083	CA	GLY	F	206	−29.611	63.456	−14.094	1.00	36.11	B000	C
ATOM	8084	C	GLY	F	206	−29.691	64.031	−15.491	1.00	41.59	B000	C
ATOM	8085	O	GLY	F	206	−29.511	63.335	−16.493	1.00	41.37	B000	O
ATOM	8086	N	PRO	F	207	−29.950	65.320	−15.574	1.00	36.32	B000	N
ATOM	8087	CA	PRO	F	207	−30.143	65.969	−16.875	1.00	39.41	B000	C
ATOM	8088	C	PRO	F	207	−28.881	66.583	−17.484	1.00	35.53	B000	C
ATOM	8089	O	PRO	F	207	−28.943	67.699	−18.000	1.00	50.85	B000	O
ATOM	8090	CB	PRO	F	207	−31.148	67.068	−16.531	1.00	38.74	B000	C
ATOM	8091	CG	PRO	F	207	−30.663	67.508	−15.160	1.00	35.34	B000	C
ATOM	8092	CD	PRO	F	207	−30.199	66.246	−14.457	1.00	39.53	B000	C
ATOM	8093	N	VAL	F	208	−27.741	65.910	−17.422	1.00	33.23	B000	N
ATOM	8094	CA	VAL	F	208	−26.468	66.469	−17.858	1.00	39.13	B000	C
ATOM	8095	C	VAL	F	208	−25.919	65.604	−18.985	1.00	35.96	B000	C
ATOM	8096	O	VAL	F	208	−25.881	64.378	−18.856	1.00	36.23	B000	O
ATOM	8097	CB	VAL	F	208	−25.470	66.542	−16.690	1.00	35.73	B000	C
ATOM	8098	CG1	VAL	F	208	−24.205	67.239	−17.130	1.00	31.91	B000	C
ATOM	8099	CG2	VAL	F	208	−26.108	67.258	−15.495	1.00	37.34	B000	C
ATOM	8100	N	ASN	F	209	−25.509	66.232	−20.088	1.00	32.26	B000	N
ATOM	8101	CA	ASN	F	209	−24.855	65.476	−21.157	1.00	32.97	B000	C
ATOM	8102	C	ASN	F	209	−23.617	64.755	−20.626	1.00	34.25	B000	C
ATOM	8103	O	ASN	F	209	−22.796	65.346	−19.917	1.00	33.13	B000	O
ATOM	8104	CB	ASN	F	209	−24.481	66.389	−22.315	1.00	30.89	B000	C
ATOM	8105	CG	ASN	F	209	−25.679	66.764	−23.167	1.00	37.35	B000	C
ATOM	8106	OD1	ASN	F	209	−26.585	65.948	−23.377	1.00	36.11	B000	O
ATOM	8107	ND2	ASN	F	209	−25.682	67.989	−23.685	1.00	31.49	B000	N
ATOM	8108	N	THR	F	210	−23.508	63.458	−20.934	1.00	30.22	B000	N
ATOM	8109	CA	THR	F	210	−22.544	62.592	−20.266	1.00	31.09	B000	C
ATOM	8110	C	THR	F	210	−21.985	61.559	−21.244	1.00	34.46	B000	C
ATOM	8111	O	THR	F	210	−22.756	60.821	−21.873	1.00	32.16	B000	O
ATOM	8112	CB	THR	F	210	−23.210	61.900	−19.071	1.00	32.23	B000	C
ATOM	8113	OG1	THR	F	210	−23.838	62.882	−18.229	1.00	31.01	B000	O
ATOM	8114	CG2	THR	F	210	−22.187	61.116	−18.256	1.00	27.20	B000	C
ATOM	8115	N	TRP	F	211	−20.650	61.510	−21.371	1.00	29.01	B000	N
ATOM	8116	CA	TRP	F	211	−19.987	60.567	−22.278	1.00	30.78	B000	C
ATOM	8117	C	TRP	F	211	−20.208	59.116	−21.857	1.00	33.57	B000	C
ATOM	8118	O	TRP	F	211	−20.215	58.792	−20.667	1.00	33.68	B000	O
ATOM	8119	CB	TRP	F	211	−18.473	60.834	−22.329	1.00	28.32	B000	C
ATOM	8120	CG	TRP	F	211	−18.041	62.091	−23.074	1.00	29.99	B000	C
ATOM	8121	CD1	TRP	F	211	−17.177	63.044	−22.623	1.00	28.61	B000	C
ATOM	8122	CD2	TRP	F	211	−18.423	62.498	−24.404	1.00	30.26	B000	C
ATOM	8123	NE1	TRP	F	211	−16.989	64.012	−23.580	1.00	32.26	B000	N
ATOM	8124	CE2	TRP	F	211	−17.742	63.709	−24.681	1.00	29.27	B000	C
ATOM	8125	CE3	TRP	F	211	−19.273	61.958	−25.381	1.00	26.34	B000	C
ATOM	8126	CZ2	TRP	F	211	−17.891	64.402	−25.888	1.00	28.81	B000	C
ATOM	8127	CZ3	TRP	F	211	−19.431	62.640	−26.575	1.00	28.36	B000	C
ATOM	8128	CH2	TRP	F	211	−18.739	63.866	−26.818	1.00	34.89	B000	C
ATOM	8129	N	MET	F	212	−20.359	58.232	−22.845	1.00	36.13	B000	N
ATOM	8130	CA	MET	F	212	−20.261	56.789	−22.634	1.00	36.28	B000	C
ATOM	8131	C	MET	F	212	−19.149	56.198	−23.506	1.00	41.20	B000	C
ATOM	8132	O	MET	F	212	−18.610	56.848	−24.412	1.00	38.23	B000	O
ATOM	8133	CB	MET	F	212	−21.598	56.096	−22.919	1.00	36.01	B000	C
ATOM	8134	CG	MET	F	212	−21.950	55.930	−24.386	1.00	32.65	B000	C
ATOM	8135	SD	MET	F	212	−23.698	55.486	−24.615	1.00	40.40	B000	S
ATOM	8136	CE	MET	F	212	−24.541	57.090	−24.376	1.00	32.88	B000	C
ATOM	8137	N	GLY	F	213	−18.810	54.942	−23.233	1.00	41.45	B000	N
ATOM	8138	CA	GLY	F	213	−17.729	54.287	−23.952	1.00	36.96	B000	C
ATOM	8139	C	GLY	F	213	−18.090	53.824	−25.345	1.00	39.99	B000	C
ATOM	8140	O	GLY	F	213	−17.905	52.645	−25.677	1.00	38.24	B000	O
ATOM	8141	N	LEU	F	214	−18.614	54.732	−26.173	1.00	34.09	B000	N
ATOM	8142	CA	LEU	F	214	−19.135	54.371	−27.489	1.00	37.28	B000	C
ATOM	8143	C	LEU	F	214	−18.700	55.449	−28.470	1.00	36.04	B000	C
ATOM	8144	O	LEU	F	214	−18.965	56.632	−28.244	1.00	38.95	B000	O
ATOM	8145	CB	LEU	F	214	−20.673	54.216	−27.453	1.00	36.90	B000	C
ATOM	8146	CG	LEU	F	214	−21.474	53.990	−28.753	1.00	39.75	B000	C
ATOM	8147	CD1	LEU	F	214	−20.997	52.758	−29.501	1.00	40.07	B000	C
ATOM	8148	CD2	LEU	F	214	−22.967	53.871	−28.493	1.00	34.46	B000	C
ATOM	8149	N	HIS	F	215	−18.023	55.054	−29.545	1.00	41.21	B000	N
ATOM	8150	CA	HIS	F	215	−17.454	56.028	−30.471	1.00	43.32	B000	C
ATOM	8151	C	HIS	F	215	−17.360	55.421	−31.860	1.00	44.63	B000	C
ATOM	8152	O	HIS	F	215	−17.496	54.209	−32.041	1.00	41.89	B000	O
ATOM	8153	CB	HIS	F	215	−16.081	56.493	−30.014	1.00	37.84	B000	C
ATOM	8154	CG	HIS	F	215	−15.059	55.406	−30.023	1.00	48.13	B000	C
ATOM	8155	ND1	HIS	F	215	−14.161	55.238	−31.054	1.00	51.31	B000	N
ATOM	8156	CD2	HIS	F	215	−14.806	54.416	−29.137	1.00	50.71	B000	C
ATOM	8157	CE1	HIS	F	215	−13.391	54.198	−30.797	1.00	52.71	B000	C
ATOM	8158	NE2	HIS	F	215	−13.760	53.683	−29.639	1.00	46.57	B000	N
ATOM	8159	N	ASP	F	216	−17.144	56.288	−32.853	1.00	40.97	B000	N
ATOM	8160	CA	ASP	F	216	−17.135	55.874	−34.252	1.00	42.50	B000	C
ATOM	8161	C	ASP	F	216	−15.783	56.113	−34.912	1.00	43.44	B000	C
ATOM	8162	O	ASP	F	216	−15.701	56.251	−36.131	1.00	42.45	B000	O
ATOM	8163	CB	ASP	F	216	−18.241	56.589	−35.029	1.00	40.42	B000	C
ATOM	8164	CG	ASP	F	216	−17.950	58.067	−35.268	1.00	43.85	B000	C
ATOM	8165	OD1	ASP	F	216	−16.970	58.617	−34.703	1.00	43.41	B000	O
ATOM	8166	OD2	ASP	F	216	−18.733	58.690	−36.024	1.00	45.80	B000	O1−
ATOM	8167	N	GLN	F	217	−14.710	56.137	−34.128	1.00	51.10	B000	N
ATOM	8168	CA	GLN	F	217	−13.512	56.817	−34.600	1.00	58.50	B000	C
ATOM	8169	C	GLN	F	217	−12.746	56.030	−35.663	1.00	59.01	B000	C
ATOM	8170	O	GLN	F	217	−11.858	56.600	−36.302	1.00	64.06	B000	O
ATOM	8171	CB	GLN	F	217	−12.653	57.214	−33.385	1.00	60.37	B000	C
ATOM	8172	CG	GLN	F	217	−13.415	58.358	−32.581	1.00	65.68	B000	C
ATOM	8173	CD	GLN	F	217	−12.601	59.087	−31.493	1.00	70.67	B000	C
ATOM	8174	OE1	GLN	F	217	−12.640	58.714	−30.307	1.00	52.11	B000	O
ATOM	8175	NE2	GLN	F	217	−11.925	60.175	−31.884	1.00	67.51	B000	N
ATOM	8176	N	ASN	F	218	−13.108	54.777	−35.930	1.00	52.55	B000	N
ATOM	8177	CA	ASN	F	218	−12.597	54.084	−37.103	1.00	58.15	B000	C
ATOM	8178	C	ASN	F	218	−13.615	53.968	−38.223	1.00	65.45	B000	C
ATOM	8179	O	ASN	F	218	−13.292	53.430	−39.289	1.00	62.69	B000	O
ATOM	8180	CB	ASN	F	218	−12.114	52.698	−36.724	1.00	71.05	B000	C
ATOM	8181	CG	ASN	F	218	−10.817	52.743	−35.976	1.00	81.96	B000	C
ATOM	8182	OD1	ASN	F	218	−10.715	52.221	−34.854	1.00	76.60	B000	O
ATOM	8183	ND2	ASN	F	218	−9.816	53.410	−36.568	1.00	58.18	B000	N
ATOM	8184	N	GLY	F	219	−14.834	54.440	−38.007	1.00	51.95	B000	N
ATOM	8185	CA	GLY	F	219	−15.897	54.245	−38.957	1.00	50.90	B000	C
ATOM	8186	C	GLY	F	219	−17.074	53.561	−38.292	1.00	41.92	B000	C
ATOM	8187	O	GLY	F	219	−18.131	54.156	−38.073	1.00	49.46	B000	O
ATOM	8188	N	PRO	F	220	−16.902	52.297	−37.938	1.00	48.10	B000	N
ATOM	8189	CA	PRO	F	220	−17.984	51.582	−37.251	1.00	50.76	B000	C
ATOM	8190	C	PRO	F	220	−18.125	52.032	−35.803	1.00	45.49	B000	C
ATOM	8191	O	PRO	F	220	−17.137	52.233	−35.095	1.00	50.03	B000	O
ATOM	8192	CB	PRO	F	220	−17.550	50.113	−37.340	1.00	44.33	B000	C
ATOM	8193	CG	PRO	F	220	−16.058	50.172	−37.501	1.00	53.78	B000	C
ATOM	8194	CD	PRO	F	220	−15.762	51.421	−38.268	1.00	48.76	B000	C
ATOM	8195	N	TRP	F	221	−19.371	52.181	−35.365	1.00	42.06	B000	N
ATOM	8196	CA	TRP	F	221	−19.631	52.403	−33.953	1.00	44.69	B000	C
ATOM	8197	C	TRP	F	221	−19.168	51.194	−33.147	1.00	38.24	B000	C
ATOM	8198	O	TRP	F	221	−19.473	50.053	−33.498	1.00	49.53	B000	O
ATOM	8199	CB	TRP	F	221	−21.123	52.668	−33.733	1.00	41.17	B000	C
ATOM	8200	CG	TRP	F	221	−21.529	54.055	−34.121	1.00	43.26	B000	C
ATOM	8201	CD1	TRP	F	221	−22.156	54.450	−35.268	1.00	36.74	B000	C
ATOM	8202	CD2	TRP	F	221	−21.300	55.244	−33.355	1.00	34.96	B000	C
ATOM	8203	NE1	TRP	F	221	−22.336	55.817	−35.259	1.00	35.73	B000	N
ATOM	8204	CE2	TRP	F	221	−21.824	56.322	−34.089	1.00	37.88	B000	C
ATOM	8205	CE3	TRP	F	221	−20.709	55.492	−32.116	1.00	35.21	B000	C
ATOM	8206	CZ2	TRP	F	221	−21.781	57.639	−33.617	1.00	42.62	B000	C
ATOM	8207	CZ3	TRP	F	221	−20.663	56.791	−31.648	1.00	39.03	B000	C
ATOM	8208	CH2	TRP	F	221	−21.194	57.848	−32.395	1.00	38.23	B000	C
ATOM	8209	N	LYS	F	222	−18.432	51.450	−32.065	1.00	41.84	B000	N
ATOM	8210	CA	LYS	F	222	−17.829	50.409	−31.245	1.00	41.88	B000	C
ATOM	8211	C	LYS	F	222	−17.885	50.777	−29.770	1.00	45.01	B000	C
ATOM	8212	O	LYS	F	222	−17.788	51.953	−29.409	1.00	38.97	B000	O
ATOM	8213	CB	LYS	F	222	−16.367	50.176	−31.639	1.00	47.29	B000	C
ATOM	8214	CG	LYS	F	222	−16.184	49.600	−33.033	1.00	60.26	B000	C
ATOM	8215	CD	LYS	F	222	−14.729	49.672	−33.464	1.00	61.80	B000	C
ATOM	8216	CE	LYS	F	222	−14.371	51.081	−33.924	1.00	69.59	B000	C
ATOM	8217	NZ	LYS	F	222	−13.030	51.109	−34.562	1.00	80.69	B000	N1+
ATOM	8218	N	TRP	F	223	−18.007	49.751	−28.918	1.00	43.07	B000	N
ATOM	8219	CA	TRP	F	223	−17.864	49.911	−27.476	1.00	42.29	B000	C
ATOM	8220	C	TRP	F	223	−16.411	49.702	−27.074	1.00	45.99	B000	C
ATOM	8221	O	TRP	F	223	−15.708	48.879	−27.661	1.00	52.22	B000	O
ATOM	8222	CB	TRP	F	223	−18.762	48.940	−26.696	1.00	41.28	B000	C
ATOM	8223	CG	TRP	F	223	−20.258	49.200	−26.825	1.00	43.60	B000	C
ATOM	8224	CD1	TRP	F	223	−21.155	48.512	−27.605	1.00	41.95	B000	C
ATOM	8225	CD2	TRP	F	223	−21.014	50.224	−26.158	1.00	45.65	B000	C
ATOM	8226	NE1	TRP	F	223	−22.422	49.047	−27.462	1.00	42.77	B000	N
ATOM	8227	CE2	TRP	F	223	−22.366	50.089	−26.575	1.00	41.46	B000	C
ATOM	8228	CE3	TRP	F	223	−20.684	51.237	−25.249	1.00	40.03	B000	C
ATOM	8229	CZ2	TRP	F	223	−23.376	50.933	−26.118	1.00	42.16	B000	C
ATOM	8230	CZ3	TRP	F	223	−21.695	52.075	−24.792	1.00	38.55	B000	C
ATOM	8231	CH2	TRP	F	223	−23.023	51.918	−25.225	1.00	39.46	B000	C
ATOM	8232	N	VAL	F	224	−15.966	50.458	−26.065	1.00	39.89	B000	N
ATOM	8233	CA	VAL	F	224	−14.557	50.478	−25.696	1.00	41.43	B000	C
ATOM	8234	C	VAL	F	224	−14.084	49.166	−25.090	1.00	43.72	B000	C
ATOM	8235	O	VAL	F	224	−12.878	48.924	−25.048	1.00	41.80	B000	O
ATOM	8236	CB	VAL	F	224	−14.257	51.635	−24.718	1.00	38.57	B000	C
ATOM	8237	CG1	VAL	F	224	−14.434	52.978	−25.419	1.00	35.91	B000	C
ATOM	8238	CG2	VAL	F	224	−15.154	51.522	−23.509	1.00	37.24	B000	C
ATOM	8239	N	ASP	F	225	−14.978	48.330	−24.572	1.00	44.78	B000	N
ATOM	8240	CA	ASP	F	225	−14.559	47.074	−23.971	1.00	40.21	B000	C
ATOM	8241	C	ASP	F	225	−14.719	45.908	−24.924	1.00	47.22	B000	C
ATOM	8242	O	ASP	F	225	−14.534	44.763	−24.513	1.00	49.29	B000	O
ATOM	8243	CB	ASP	F	225	−15.321	46.788	−22.679	1.00	41.32	B000	C
ATOM	8244	CG	ASP	F	225	−16.790	46.487	−22.914	1.00	46.80	B000	C
ATOM	8245	OD1	ASP	F	225	−17.305	46.755	−24.021	1.00	40.18	B000	O
ATOM	8246	OD2	ASP	F	225	−17.426	45.946	−21.982	1.00	55.82	B000	O1−
ATOM	8247	N	GLY	F	226	−15.078	46.173	−26.181	1.00	46.15	B000	N
ATOM	8248	CA	GLY	F	226	−15.202	45.151	−27.189	1.00	44.93	B000	C
ATOM	8249	C	GLY	F	226	−16.606	44.610	−27.394	1.00	49.56	B000	C
ATOM	8250	O	GLY	F	226	−16.858	43.993	−28.440	1.00	52.14	B000	O
ATOM	8251	N	THR	F	227	−17.522	44.843	−26.443	1.00	45.78	B000	N
ATOM	8252	CA	THR	F	227	−18.938	44.496	−26.585	1.00	38.28	B000	C
ATOM	8253	C	THR	F	227	−19.437	44.781	−27.996	1.00	49.56	B000	C
ATOM	8254	O	THR	F	227	−19.216	45.868	−28.544	1.00	51.44	B000	O
ATOM	8255	CB	THR	F	227	−19.779	45.282	−25.571	1.00	46.77	B000	C
ATOM	8256	OG1	THR	F	227	−19.284	45.062	−24.244	1.00	49.45	B000	O
ATOM	8257	CG2	THR	F	227	−21.244	44.872	−25.628	1.00	32.96	B000	C
ATOM	8258	N	ASP	F	228	−20.089	43.791	−28.594	1.00	48.42	B000	N
ATOM	8259	CA	ASP	F	228	−20.557	43.942	−29.964	1.00	52.56	B000	C
ATOM	8260	C	ASP	F	228	−21.653	44.996	−30.034	1.00	47.16	B000	C
ATOM	8261	O	ASP	F	228	−22.638	44.926	−29.297	1.00	54.76	B000	O
ATOM	8262	CB	ASP	F	228	−21.080	42.609	−30.513	1.00	52.04	B000	C
ATOM	8263	CG	ASP	F	228	−21.620	42.741	−31.938	1.00	51.96	B000	C
ATOM	8264	OD1	ASP	F	228	−20.800	42.871	−32.867	1.00	55.04	B000	O
ATOM	8265	OD2	ASP	F	228	−22.857	42.731	−32.133	1.00	53.62	B000	O1−
ATOM	8266	N	TYR	F	229	−21.480	45.975	−30.926	1.00	49.63	B000	N
ATOM	8267	CA	TYR	F	229	−22.438	47.072	−31.032	1.00	51.91	B000	C
ATOM	8268	C	TYR	F	229	−23.725	46.641	−31.741	1.00	51.02	B000	C
ATOM	8269	O	TYR	F	229	−24.823	47.054	−31.343	1.00	48.95	B000	O
ATOM	8270	CB	TYR	F	229	−21.800	48.280	−31.749	1.00	41.08	B000	C
ATOM	8271	CG	TYR	F	229	−22.801	49.368	−32.155	1.00	42.20	B000	C
ATOM	8272	CD1	TYR	F	229	−23.377	50.216	−31.208	1.00	40.58	B000	C
ATOM	8273	CD2	TYR	F	229	−23.178	49.530	−33.482	1.00	40.58	B000	C
ATOM	8274	CE1	TYR	F	229	−24.293	51.223	−31.586	1.00	37.62	B000	C
ATOM	8275	CE2	TYR	F	229	−24.088	50.511	−33.864	1.00	42.49	B000	C
ATOM	8276	CZ	TYR	F	229	−24.634	51.359	−32.910	1.00	40.45	B000	C
ATOM	8277	OH	TYR	F	229	−25.527	52.323	−33.311	1.00	45.55	B000	O
ATOM	8278	N	GLU	F	230	−23.605	45.833	−32.800	1.00	57.91	B000	N
ATOM	8279	CA	GLU	F	230	−24.743	45.560	−33.679	1.00	55.10	B000	C
ATOM	8280	C	GLU	F	230	−25.831	44.782	−32.956	1.00	53.04	B000	C
ATOM	8281	O	GLU	F	230	−27.014	45.118	−33.055	1.00	52.09	B000	O
ATOM	8282	CB	GLU	F	230	−24.273	44.782	−34.909	1.00	58.23	B000	C
ATOM	8283	CG	GLU	F	230	−25.270	44.727	−36.048	1.00	61.69	B000	C
ATOM	8284	CD	GLU	F	230	−25.912	46.067	−36.325	1.00	76.73	B000	C
ATOM	8285	OE1	GLU	F	230	−27.160	46.119	−36.285	1.00	75.40	B000	O
ATOM	8286	OE2	GLU	F	230	−25.178	47.067	−36.556	1.00	78.82	B000	O1−
ATOM	8287	N	THR	F	231	−25.449	43.767	−32.201	1.00	51.54	B000	N
ATOM	8288	CA	THR	F	231	−26.410	42.954	−31.478	1.00	55.16	B000	C
ATOM	8289	C	THR	F	231	−26.687	43.461	−30.072	1.00	58.68	B000	C
ATOM	8290	O	THR	F	231	−27.516	42.866	−29.371	1.00	54.74	B000	O
ATOM	8291	CB	THR	F	231	−25.922	41.510	−31.415	1.00	49.05	B000	C
ATOM	8292	OG1	THR	F	231	−24.684	41.463	−30.698	1.00	52.11	B000	O
ATOM	8293	CG2	THR	F	231	−25.715	40.964	−32.820	1.00	45.52	B000	C
ATOM	8294	N	GLY	F	232	−26.030	44.546	−29.646	1.00	55.48	B000	N
ATOM	8295	CA	GLY	F	232	−26.155	45.022	−28.285	1.00	46.35	B000	C
ATOM	8296	C	GLY	F	232	−27.303	46.007	−28.088	1.00	42.93	B000	C
ATOM	8297	O	GLY	F	232	−27.997	46.417	−29.016	1.00	45.48	B000	O
ATOM	8298	N	PHE	F	233	−27.484	46.390	−26.830	1.00	40.91	B000	N
ATOM	8299	CA	PHE	F	233	−28.463	47.401	−26.462	1.00	38.08	B000	C
ATOM	8300	C	PHE	F	233	−28.162	48.738	−27.146	1.00	45.77	B000	C
ATOM	8301	O	PHE	F	233	−26.997	49.125	−27.305	1.00	39.98	B000	O
ATOM	8302	CB	PHE	F	233	−28.440	47.548	−24.939	1.00	42.77	B000	C
ATOM	8303	CG	PHE	F	233	−29.411	48.544	−24.406	1.00	46.27	B000	C
ATOM	8304	CD1	PHE	F	233	−30.749	48.224	−24.274	1.00	47.88	B000	C
ATOM	8305	CD2	PHE	F	233	−28.981	49.804	−24.013	1.00	42.70	B000	C
ATOM	8306	CE1	PHE	F	233	−31.650	49.153	−23.777	1.00	51.88	B000	C
ATOM	8307	CE2	PHE	F	233	−29.871	50.726	−23.515	1.00	41.09	B000	C
ATOM	8308	CZ	PHE	F	233	−31.206	50.404	−23.391	1.00	45.56	B000	C
ATOM	8309	N	LYS	F	234	−29.225	49.439	−27.562	1.00	40.43	B000	N
ATOM	8310	CA	LYS	F	234	−29.131	50.788	−28.118	1.00	41.63	B000	C
ATOM	8311	C	LYS	F	234	−30.309	51.634	−27.654	1.00	46.34	B000	C
ATOM	8312	O	LYS	F	234	−31.441	51.156	−27.610	1.00	48.63	B000	O
ATOM	8313	CB	LYS	F	234	−29.123	50.778	−29.649	1.00	44.55	B000	C
ATOM	8314	CG	LYS	F	234	−27.951	50.067	−30.289	1.00	40.30	B000	C
ATOM	8315	CD	LYS	F	234	−28.092	50.103	−31.807	1.00	43.14	B000	C
ATOM	8316	CE	LYS	F	234	−27.123	49.127	−32.446	1.00	48.35	B000	C
ATOM	8317	NZ	LYS	F	234	−27.471	47.729	−32.045	1.00	53.70	B000	N1+
ATOM	8318	N	ASN	F	235	−30.060	52.909	−27.362	1.00	47.83	B000	N
ATOM	8319	CA	ASN	F	235	−31.120	53.815	−26.906	1.00	38.15	B000	C
ATOM	8320	C	ASN	F	235	−30.936	55.217	−27.509	1.00	39.90	B000	C
ATOM	8321	O	ASN	F	235	−30.978	56.235	−26.819	1.00	38.13	B000	O
ATOM	8322	CB	ASN	F	235	−31.154	53.827	−25.376	1.00	37.57	B000	C
ATOM	8323	CG	ASN	F	235	−32.291	54.652	−24.816	1.00	44.55	B000	C
ATOM	8324	OD1	ASN	F	235	−33.337	54.797	−25.445	1.00	47.07	B000	O
ATOM	8325	ND2	ASN	F	235	−32.088	55.204	−23.620	1.00	46.24	B000	N
ATOM	8326	N	TRP	F	236	−30.749	55.278	−28.826	1.00	36.87	B000	N
ATOM	8327	CA	TRP	F	236	−30.517	56.540	−29.518	1.00	38.92	B000	C
ATOM	8328	C	TRP	F	236	−31.753	57.439	−29.510	1.00	41.60	B000	C
ATOM	8329	O	TRP	F	236	−32.890	56.967	−29.580	1.00	44.93	B000	O
ATOM	8330	CB	TRP	F	236	−30.123	56.288	−30.973	1.00	32.28	B000	C
ATOM	8331	CG	TRP	F	236	−28.813	55.606	−31.170	1.00	44.09	B000	C
ATOM	8332	CD1	TRP	F	236	−28.612	54.296	−31.518	1.00	40.32	B000	C
ATOM	8333	CD2	TRP	F	236	−27.511	56.192	−31.037	1.00	41.90	B000	C
ATOM	8334	NE1	TRP	F	236	−27.266	54.034	−31.608	1.00	35.68	B000	N
ATOM	8335	CE2	TRP	F	236	−26.568	55.182	−31.327	1.00	41.49	B000	C
ATOM	8336	CE3	TRP	F	236	−27.051	57.474	−30.700	1.00	37.67	B000	C
ATOM	8337	CZ2	TRP	F	236	−25.183	55.420	−31.300	1.00	41.56	B000	C
ATOM	8338	CZ3	TRP	F	236	−25.686	57.715	−30.683	1.00	37.32	B000	C
ATOM	8339	CH2	TRP	F	236	−24.762	56.689	−30.982	1.00	41.77	B000	C
ATOM	8340	N	ARG	F	237	−31.508	58.757	−29.481	1.00	35.83	B000	N
ATOM	8341	CA	ARG	F	237	−32.537	59.734	−29.801	1.00	44.59	B000	C
ATOM	8342	C	ARG	F	237	−33.103	59.444	−31.181	1.00	48.74	B000	C
ATOM	8343	O	ARG	F	237	−32.434	58.828	−32.017	1.00	49.21	B000	O
ATOM	8344	CB	ARG	F	237	−31.976	61.164	−29.788	1.00	36.97	B000	C
ATOM	8345	CG	ARG	F	237	−31.858	61.766	−28.411	1.00	45.68	B000	C
ATOM	8346	CD	ARG	F	237	−33.080	62.584	−28.086	1.00	53.50	B000	C
ATOM	8347	NE	ARG	F	237	−32.997	63.225	−26.778	1.00	54.24	B000	N
ATOM	8348	CZ	ARG	F	237	−32.798	64.523	−26.580	1.00	66.27	B000	C
ATOM	8349	NH1	ARG	F	237	−32.738	65.003	−25.335	1.00	53.38	B000	N1+
ATOM	8350	NH2	ARG	F	237	−32.650	65.337	−27.621	1.00	69.85	B000	N
ATOM	8351	N	PRO	F	238	−34.326	59.897	−31.447	1.00	53.51	B000	N
ATOM	8352	CA	PRO	F	238	−34.896	59.751	−32.790	1.00	53.89	B000	C
ATOM	8353	C	PRO	F	238	−33.963	60.284	−33.869	1.00	55.90	B000	C
ATOM	8354	O	PRO	F	238	−33.458	61.409	−33.783	1.00	47.93	B000	O
ATOM	8355	CB	PRO	F	238	−36.184	60.577	−32.707	1.00	53.03	B000	C
ATOM	8356	CG	PRO	F	238	−36.568	60.511	−31.263	1.00	50.27	B000	C
ATOM	8357	CD	PRO	F	238	−35.285	60.495	−30.496	1.00	54.51	B000	C
ATOM	8358	N	GLU	F	239	−33.727	59.454	−34.887	1.00	48.36	B000	N
ATOM	8359	CA	GLU	F	239	−32.951	59.792	−36.076	1.00	55.08	B000	C
ATOM	8360	C	GLU	F	239	−31.463	59.925	−35.799	1.00	51.71	B000	C
ATOM	8361	O	GLU	F	239	−30.717	60.378	−36.673	1.00	53.39	B000	O
ATOM	8362	CB	GLU	F	239	−33.471	61.081	−36.715	1.00	54.02	B000	C
ATOM	8363	CG	GLU	F	239	−34.894	60.933	−37.217	1.00	64.17	B000	C
ATOM	8364	CD	GLU	F	239	−35.603	62.267	−37.357	1.00	82.12	B000	C
ATOM	8365	OE1	GLU	F	239	−34.947	63.318	−37.174	1.00	79.31	B000	O
ATOM	8366	OE2	GLU	F	239	−36.828	62.260	−37.609	1.00	90.31	B000	O1−
ATOM	8367	N	GLN	F	240	−31.010	59.539	−34.613	1.00	45.35	B000	N
ATOM	8368	CA	GLN	F	240	−29.594	59.480	−34.313	1.00	45.02	B000	C
ATOM	8369	C	GLN	F	240	−29.207	58.001	−34.305	1.00	40.34	B000	C
ATOM	8370	O	GLN	F	240	−30.041	57.164	−33.989	1.00	38.58	B000	O
ATOM	8371	CB	GLN	F	240	−29.274	60.163	−32.964	1.00	40.27	B000	C
ATOM	8372	CG	GLN	F	240	−29.798	61.588	−32.801	1.00	35.48	B000	C
ATOM	8373	CD	GLN	F	240	−29.552	62.460	−34.038	1.00	52.50	B000	C
ATOM	8374	OE1	GLN	F	240	−28.448	62.496	−34.599	1.00	44.08	B000	O
ATOM	8375	NE2	GLN	F	240	−30.594	63.166	−34.470	1.00	52.73	B000	N
ATOM	8376	N	PRO	F	241	−27.933	57.680	−34.609	1.00	41.65	B000	N
ATOM	8377	CA	PRO	F	241	−26.875	58.646	−34.945	1.00	36.96	B000	C
ATOM	8378	C	PRO	F	241	−27.011	59.145	−36.366	1.00	42.81	B000	C
ATOM	8379	O	PRO	F	241	−27.998	58.769	−37.004	1.00	45.53	B000	O
ATOM	8380	CB	PRO	F	241	−25.586	57.853	−34.749	1.00	38.94	B000	C
ATOM	8381	CG	PRO	F	241	−25.986	56.428	−34.992	1.00	43.27	B000	C
ATOM	8382	CD	PRO	F	241	−27.423	56.298	−34.511	1.00	38.99	B000	C
ATOM	8383	N	ASP	F	242	−26.097	60.013	−36.818	1.00	39.75	B000	N
ATOM	8384	CA	ASP	F	242	−26.139	60.504	−38.190	1.00	36.75	B000	C
ATOM	8385	C	ASP	F	242	−26.229	59.323	−39.143	1.00	43.99	B000	C
ATOM	8386	O	ASP	F	242	−25.504	58.332	−38.991	1.00	46.47	B000	O
ATOM	8387	CB	ASP	F	242	−24.894	61.335	−38.515	1.00	49.95	B000	C
ATOM	8388	CG	ASP	F	242	−24.677	62.473	−37.551	1.00	48.49	B000	C
ATOM	8389	OD1	ASP	F	242	−25.683	63.064	−37.104	1.00	52.88	B000	O
ATOM	8390	OD2	ASP	F	242	−23.497	62.767	−37.248	1.00	50.34	B000	O
ATOM	8391	N	ASP	F	243	−27.147	59.405	−40.097	1.00	38.82	B000	N
ATOM	8392	CA	ASP	F	243	−27.412	58.269	−40.967	1.00	51.83	B000	C
ATOM	8393	C	ASP	F	243	−26.703	58.364	−42.308	1.00	46.33	B000	C
ATOM	8394	O	ASP	F	243	−26.951	57.526	−43.172	1.00	49.46	B000	O
ATOM	8395	CB	ASP	F	243	−28.919	58.079	−41.193	1.00	42.32	B000	C
ATOM	8396	CG	ASP	F	243	−29.605	59.327	−41.786	1.00	64.08	B000	C
ATOM	8397	OD1	ASP	F	243	−28.935	60.346	−42.070	1.00	56.96	B000	O
ATOM	8398	OD2	ASP	F	243	−30.842	59.286	−41.971	1.00	77.59	B000	O
ATOM	8399	N	TRP	F	244	−25.799	59.322	−42.495	1.00	46.94	B000	N
ATOM	8400	CA	TRP	F	244	−25.235	59.541	−43.822	1.00	43.08	B000	C
ATOM	8401	C	TRP	F	244	−24.046	58.643	−44.134	1.00	41.86	B000	C
ATOM	8402	O	TRP	F	244	−23.528	58.721	−45.250	1.00	43.66	B000	O
ATOM	8403	CB	TRP	F	244	−24.765	60.989	−43.994	1.00	49.74	B000	C
ATOM	8404	CG	TRP	F	244	−25.371	61.991	−43.064	1.00	50.88	B000	C
ATOM	8405	CD1	TRP	F	244	−26.695	62.261	−42.902	1.00	52.58	B000	C
ATOM	8406	CD2	TRP	F	244	−24.674	62.891	−42.206	1.00	42.95	B000	C
ATOM	8407	NE1	TRP	F	244	−26.876	63.254	−41.976	1.00	50.24	B000	N
ATOM	8408	CE2	TRP	F	244	−25.650	63.672	−41.536	1.00	51.72	B000	C
ATOM	8409	CE3	TRP	F	244	−23.333	63.117	−41.940	1.00	40.66	B000	C
ATOM	8410	CZ2	TRP	F	244	−25.322	64.660	−40.608	1.00	34.70	B000	C
ATOM	8411	CZ3	TRP	F	244	−23.008	64.096	−41.014	1.00	51.45	B000	C
ATOM	8412	CH2	TRP	F	244	−24.002	64.849	−40.357	1.00	45.14	B000	C
ATOM	8413	N	TYR	F	245	−23.649	57.749	−43.225	1.00	38.07	B000	N
ATOM	8414	CA	TYR	F	245	−22.447	56.950	−43.423	1.00	34.89	B000	C
ATOM	8415	C	TYR	F	245	−22.709	55.483	−43.712	1.00	44.67	B000	C
ATOM	8416	O	TYR	F	245	−21.778	54.779	−44.103	1.00	52.17	B000	O
ATOM	8417	CB	TYR	F	245	−21.529	57.030	−42.191	1.00	38.23	B000	C
ATOM	8418	CG	TYR	F	245	−21.240	58.429	−41.761	1.00	43.82	B000	C
ATOM	8419	CD1	TYR	F	245	−20.344	59.219	−42.479	1.00	42.91	B000	C
ATOM	8420	CD2	TYR	F	245	−21.868	58.976	−40.638	1.00	38.95	B000	C
ATOM	8421	CE1	TYR	F	245	−20.090	60.513	−42.101	1.00	39.31	B000	C
ATOM	8422	CE2	TYR	F	245	−21.616	60.266	−40.249	1.00	40.49	B000	C
ATOM	8423	CZ	TYR	F	245	−20.719	61.032	−40.978	1.00	43.99	B000	C
ATOM	8424	OH	TYR	F	245	−20.449	62.323	−40.589	1.00	46.79	B000	O
ATOM	8425	N	GLY	F	246	−23.918	54.993	−43.508	1.00	42.86	B000	N
ATOM	8426	CA	GLY	F	246	−24.172	53.575	−43.641	1.00	47.08	B000	C
ATOM	8427	C	GLY	F	246	−24.546	52.918	−42.321	1.00	48.63	B000	C
ATOM	8428	O	GLY	F	246	−24.464	53.502	−41.238	1.00	46.31	B000	O
ATOM	8429	N	HIS	F	247	−25.011	51.682	−42.461	1.00	45.64	B000	N
ATOM	8430	CA	HIS	F	247	−25.504	50.908	−41.338	1.00	45.98	B000	C
ATOM	8431	C	HIS	F	247	−24.400	50.682	−40.309	1.00	49.00	B000	C
ATOM	8432	O	HIS	F	247	−23.329	50.161	−40.640	1.00	47.43	B000	O
ATOM	8433	CB	HIS	F	247	−26.052	49.570	−41.836	1.00	48.96	B000	C
ATOM	8434	CG	HIS	F	247	−26.470	48.656	−40.731	1.00	52.43	B000	C
ATOM	8435	ND1	HIS	F	247	−27.650	48.819	−40.037	1.00	52.47	B000	N
ATOM	8436	CD2	HIS	F	247	−25.835	47.606	−40.157	1.00	55.93	B000	C
ATOM	8437	CE1	HIS	F	247	−27.737	47.891	−39.102	1.00	55.95	B000	C
ATOM	8438	NE2	HIS	F	247	−26.649	47.142	−39.154	1.00	65.30	B000	N
ATOM	8439	N	GLY	F	248	−24.656	51.080	−39.063	1.00	45.09	B000	N
ATOM	8440	CA	GLY	F	248	−23.694	50.884	−37.992	1.00	43.43	B000	C
ATOM	8441	C	GLY	F	248	−22.442	51.723	−38.086	1.00	44.64	B000	C
ATOM	8442	O	GLY	F	248	−21.463	51.431	−37.391	1.00	45.17	B000	O
ATOM	8443	N	LEU	F	249	−22.449	52.777	−38.907	1.00	44.92	B000	N
ATOM	8444	CA	LEU	F	249	−21.244	53.532	−39.232	1.00	47.53	B000	C
ATOM	8445	C	LEU	F	249	−21.355	55.001	−38.833	1.00	45.44	B000	C
ATOM	8446	O	LEU	F	249	−22.456	55.561	−38.758	1.00	38.63	B000	O
ATOM	8447	CB	LEU	F	249	−20.942	53.464	−40.737	1.00	45.64	B000	C
ATOM	8448	CG	LEU	F	249	−20.640	52.090	−41.349	1.00	49.29	B000	C
ATOM	8449	CD1	LEU	F	249	−20.212	52.237	−42.809	1.00	41.47	B000	C
ATOM	8450	CD2	LEU	F	249	−19.590	51.359	−40.538	1.00	35.93	B000	C
ATOM	8451	N	GLY	F	250	−20.186	55.619	−38.598	1.00	43.79	B000	N
ATOM	8452	CA	GLY	F	250	−20.033	57.062	−38.423	1.00	40.09	B000	C
ATOM	8453	C	GLY	F	250	−18.890	57.625	−39.262	1.00	46.39	B000	C
ATOM	8454	O	GLY	F	250	−18.312	56.892	−40.068	1.00	46.10	B000	O
ATOM	8455	N	ALA	F	251	−18.553	58.910	−39.081	1.00	38.76	B000	N
ATOM	8456	CA	ALA	F	251	−17.474	59.596	−39.795	1.00	44.18	B000	C
ATOM	8457	C	ALA	F	251	−16.114	59.542	−39.122	1.00	41.29	B000	C
ATOM	8458	O	ALA	F	251	−15.172	60.113	−39.673	1.00	48.88	B000	O
ATOM	8459	CB	ALA	F	251	−17.762	61.085	−39.974	1.00	67.76	B000	C
ATOM	8460	N	GLY	F	252	−15.989	58.946	−37.942	1.00	43.97	B000	N
ATOM	8461	CA	GLY	F	252	−14.714	58.903	−37.255	1.00	44.53	B000	C
ATOM	8462	C	GLY	F	252	−14.440	60.030	−36.276	1.00	47.60	B000	C
ATOM	8463	O	GLY	F	252	−13.427	59.971	−35.575	1.00	55.35	B000	O
ATOM	8464	N	GLU	F	253	−15.306	61.045	−36.183	1.00	45.85	B000	N
ATOM	8465	CA	GLU	F	253	−15.090	62.165	−35.268	1.00	42.89	B000	C
ATOM	8466	C	GLU	F	253	−16.069	62.200	−34.096	1.00	42.96	B000	C
ATOM	8467	O	GLU	F	253	−15.975	63.117	−33.272	1.00	41.71	B000	O
ATOM	8468	CB	GLU	F	253	−15.188	63.512	−36.017	1.00	43.68	B000	C
ATOM	8469	CG	GLU	F	253	−14.363	63.614	−37.321	1.00	57.15	B000	C
ATOM	8470	CD	GLU	F	253	−12.875	63.967	−37.117	1.00	70.88	B000	C
ATOM	8471	OE1	GLU	F	253	−12.568	65.139	−36.771	1.00	71.64	B000	O
ATOM	8472	OE2	GLU	F	253	−12.008	63.079	−37.331	1.00	63.29	B000	O
ATOM	8473	N	ASP	F	254	−17.000	61.242	−33.982	1.00	36.37	B000	N
ATOM	8474	CA	ASP	F	254	−18.107	61.378	−33.045	1.00	37.71	B000	C
ATOM	8475	C	ASP	F	254	−17.988	60.412	−31.877	1.00	36.53	B000	C
ATOM	8476	O	ASP	F	254	−17.374	59.349	−31.973	1.00	36.91	B000	O
ATOM	8477	CB	ASP	F	254	−19.473	61.157	−33.717	1.00	35.74	B000	C
ATOM	8478	CG	ASP	F	254	−20.006	62.400	−34.396	1.00	38.14	B000	C
ATOM	8479	OD2	ASP	F	254	−21.148	62.350	−34.936	1.00	36.55	B000	O
ATOM	8480	OD1	ASP	F	254	−19.280	63.427	−34.386	1.00	41.05	B000	O1−
ATOM	8481	N	CYS	F	255	−18.603	60.799	−30.769	1.00	38.85	B000	N
ATOM	8482	CA	CYS	F	255	−18.733	59.942	−29.606	1.00	28.30	B000	C
ATOM	8483	C	CYS	F	255	−20.176	60.039	−29.135	1.00	32.80	B000	C
ATOM	8484	O	CYS	F	255	−20.878	61.013	−29.418	1.00	34.41	B000	O
ATOM	8485	CB	CYS	F	255	−17.749	60.342	−28.515	1.00	32.19	B000	C
ATOM	8486	SG	CYS	F	255	−15.954	60.090	−28.944	1.00	42.14	B000	S
ATOM	8487	N	ALA	F	256	−20.630	59.006	−28.447	1.00	31.53	B000	N
ATOM	8488	CA	ALA	F	256	−22.004	58.933	−27.991	1.00	30.16	B000	C
ATOM	8489	C	ALA	F	256	−22.096	59.438	−26.562	1.00	34.02	B000	C
ATOM	8490	O	ALA	F	256	−21.281	59.074	−25.706	1.00	31.73	B000	O
ATOM	8491	CB	ALA	F	256	−22.530	57.498	−28.071	1.00	28.94	B000	C
ATOM	8492	N	HIS	F	257	−23.103	60.261	−26.301	1.00	28.80	B000	N
ATOM	8493	CA	HIS	F	257	−23.347	60.726	−24.947	1.00	33.62	B000	C
ATOM	8494	C	HIS	F	257	−24.822	60.589	−24.608	1.00	29.12	B000	C
ATOM	8495	O	HIS	F	257	−25.696	60.659	−25.483	1.00	29.71	B000	O
ATOM	8496	CB	HIS	F	257	−22.895	62.209	−24.730	1.00	31.05	B000	C
ATOM	8497	CG	HIS	F	257	−23.622	63.196	−25.584	1.00	27.54	B000	C
ATOM	8498	ND1	HIS	F	257	−24.699	63.926	−25.124	1.00	35.11	B000	N
ATOM	8499	CD2	HIS	F	257	−23.433	63.578	−26.873	1.00	31.63	B000	C
ATOM	8500	CE1	HIS	F	257	−25.140	64.719	−26.088	1.00	30.09	B000	C
ATOM	8501	NE2	HIS	F	257	−24.389	64.529	−27.160	1.00	34.93	B000	N
ATOM	8502	N	PHE	F	258	−25.083	60.369	−23.324	1.00	31.39	B000	N
ATOM	8503	CA	PHE	F	258	−26.433	60.529	−22.810	1.00	37.72	B000	C
ATOM	8504	C	PHE	F	258	−26.830	61.993	−22.915	1.00	35.33	B000	C
ATOM	8505	O	PHE	F	258	−26.020	62.879	−22.636	1.00	37.08	B000	O
ATOM	8506	CB	PHE	F	258	−26.519	60.088	−21.354	1.00	31.41	B000	C
ATOM	8507	CG	PHE	F	258	−26.032	58.691	−21.094	1.00	30.94	B000	C
ATOM	8508	CD1	PHE	F	258	−26.884	57.598	−21.263	1.00	34.60	B000	C
ATOM	8509	CD2	PHE	F	258	−24.750	58.465	−20.612	1.00	31.04	B000	C
ATOM	8510	CE1	PHE	F	258	−26.449	56.297	−20.988	1.00	35.62	B000	C
ATOM	8511	CE2	PHE	F	258	−24.295	57.160	−20.350	1.00	37.38	B000	C
ATOM	8512	CZ	PHE	F	258	−25.156	56.076	−20.534	1.00	34.44	B000	C
ATOM	8513	N	THR	F	259	−28.072	62.242	−23.340	1.00	39.97	B000	N
ATOM	8514	CA	THR	F	259	−28.683	63.565	−23.297	1.00	37.91	B000	C
ATOM	8515	C	THR	F	259	−29.508	63.699	−22.023	1.00	38.85	B000	C
ATOM	8516	O	THR	F	259	−29.572	62.785	−21.197	1.00	42.20	B000	O
ATOM	8517	CB	THR	F	259	−29.566	63.817	−24.514	1.00	38.22	B000	C
ATOM	8518	OG1	THR	F	259	−30.726	62.979	−24.427	1.00	40.99	B000	O
ATOM	8519	CG2	THR	F	259	−28.812	63.526	−25.789	1.00	35.73	B000	C
ATOM	8520	N	ASP	F	260	−30.176	64.845	−21.874	1.00	41.22	B000	N
ATOM	8521	CA	ASP	F	260	−30.859	65.107	−20.611	1.00	45.54	B000	C
ATOM	8522	C	ASP	F	260	−32.098	64.241	−20.394	1.00	44.40	B000	C
ATOM	8523	O	ASP	F	260	−32.576	64.175	−19.260	1.00	47.44	B000	O
ATOM	8524	CB	ASP	F	260	−31.211	66.595	−20.486	1.00	42.85	B000	C
ATOM	8525	CG	ASP	F	260	−32.026	67.112	−21.654	1.00	50.76	B000	C
ATOM	8526	OD1	ASP	F	260	−32.520	66.298	−22.465	1.00	48.72	B000	O
ATOM	8527	OD2	ASP	F	260	−32.156	68.351	−21.769	1.00	54.59	B000	O1−
ATOM	8528	N	ASP	F	261	−32.598	63.531	−21.406	1.00	42.99	B000	N
ATOM	8529	CA	ASP	F	261	−33.649	62.544	−21.167	1.00	41.51	B000	C
ATOM	8530	C	ASP	F	261	−33.118	61.115	−21.152	1.00	43.32	B000	C
ATOM	8531	O	ASP	F	261	−33.911	60.169	−21.146	1.00	48.34	B000	O
ATOM	8532	CB	ASP	F	261	−34.795	62.676	−22.192	1.00	37.72	B000	C
ATOM	8533	CG	ASP	F	261	−34.432	62.185	−23.606	1.00	50.07	B000	C
ATOM	8534	OD1	ASP	F	261	−33.408	61.504	−23.808	1.00	49.28	B000	O
ATOM	8535	OD2	ASP	F	261	−35.212	62.470	−24.543	1.00	57.06	B000	O1−
ATOM	8536	N	GLY	F	262	−31.801	60.929	−21.192	1.00	37.84	B000	N
ATOM	8537	CA	GLY	F	262	−31.223	59.600	−21.120	1.00	39.30	B000	C
ATOM	8538	C	GLY	F	262	−30.982	58.938	−22.466	1.00	41.80	B000	C
ATOM	8539	O	GLY	F	262	−30.102	58.076	−22.575	1.00	39.59	B000	O
ATOM	8540	N	ARG	F	263	−31.736	59.319	−23.494	1.00	35.33	B000	N
ATOM	8541	CA	ARG	F	263	−31.468	58.795	−24.822	1.00	38.94	B000	C
ATOM	8542	C	ARG	F	263	−30.159	59.370	−25.357	1.00	41.24	B000	C
ATOM	8543	O	ARG	F	263	−29.688	60.429	−24.926	1.00	40.40	B000	O
ATOM	8544	CB	ARG	F	263	−32.646	59.085	−25.760	1.00	39.18	B000	C
ATOM	8545	CG	ARG	F	263	−33.888	58.222	−25.393	1.00	46.56	B000	C
ATOM	8546	CD	ARG	F	263	−35.120	58.506	−26.239	1.00	38.08	B000	C
ATOM	8547	NE	ARG	F	263	−35.507	59.908	−26.134	1.00	51.22	B000	N
ATOM	8548	CZ	ARG	F	263	−36.495	60.464	−26.827	1.00	58.02	B000	C
ATOM	8549	NH1	ARG	F	263	−37.218	59.731	−27.673	1.00	52.64	B000	N1+
ATOM	8550	NH2	ARG	F	263	−36.754	61.756	−26.676	1.00	51.34	B000	N
ATOM	8551	N	TRP	F	264	−29.579	58.655	−26.311	1.00	35.20	B000	N
ATOM	8552	CA	TRP	F	264	−28.211	58.875	−26.746	1.00	33.30	B000	C
ATOM	8553	C	TRP	F	264	−28.146	59.805	−27.951	1.00	36.94	B000	C
ATOM	8554	O	TRP	F	264	−29.059	59.860	−28.785	1.00	39.27	B000	O
ATOM	8555	CB	TRP	F	264	−27.546	57.555	−27.110	1.00	32.18	B000	C
ATOM	8556	CG	TRP	F	264	−27.593	56.508	−26.057	1.00	35.42	B000	C
ATOM	8557	CD1	TRP	F	264	−28.003	56.652	−24.766	1.00	40.13	B000	C
ATOM	8558	CD2	TRP	F	264	−27.196	55.143	−26.203	1.00	36.70	B000	C
ATOM	8559	NE1	TRP	F	264	−27.880	55.459	−24.095	1.00	37.06	B000	N
ATOM	8560	CE2	TRP	F	264	−27.388	54.516	−24.960	1.00	38.24	B000	C
ATOM	8561	CE3	TRP	F	264	−26.688	54.387	−27.270	1.00	40.49	B000	C
ATOM	8562	CZ2	TRP	F	264	−27.101	53.169	−24.756	1.00	35.99	B000	C
ATOM	8563	CZ3	TRP	F	264	−26.407	53.045	−27.061	1.00	32.82	B000	C
ATOM	8564	CH2	TRP	F	264	−26.613	52.457	−25.819	1.00	37.82	B000	C
ATOM	8565	N	ASN	F	265	−27.044	60.540	−28.034	1.00	31.28	B000	N
ATOM	8566	CA	ASN	F	265	−26.763	61.379	−29.187	1.00	33.60	B000	C
ATOM	8567	C	ASN	F	265	−25.275	61.280	−29.513	1.00	33.44	B000	C
ATOM	8568	O	ASN	F	265	−24.446	60.973	−28.645	1.00	29.37	B000	O
ATOM	8569	CB	ASN	F	265	−27.200	62.832	−28.912	1.00	31.57	B000	C
ATOM	8570	CG	ASN	F	265	−26.915	63.768	−30.076	1.00	39.82	B000	C
ATOM	8571	OD1	ASN	F	265	−27.466	63.615	−31.166	1.00	41.22	B000	O
ATOM	8572	ND2	ASN	F	265	−26.003	64.724	−29.856	1.00	36.27	B000	N
ATOM	8573	N	ASP	F	266	−24.950	61.494	−30.786	1.00	31.29	B000	N
ATOM	8574	CA	ASP	F	266	−23.572	61.488	−31.255	1.00	31.23	B000	C
ATOM	8575	C	ASP	F	266	−23.107	62.919	−31.488	1.00	32.82	B000	C
ATOM	8576	O	ASP	F	266	−23.788	63.693	−32.166	1.00	30.42	B000	O
ATOM	8577	CB	ASP	F	266	−23.408	60.650	−32.536	1.00	36.08	B000	C
ATOM	8578	CG	ASP	F	266	−24.411	61.018	−33.661	1.00	40.88	B000	C
ATOM	8579	OD1	ASP	F	266	−25.586	61.367	−33.390	1.00	36.41	B000	O
ATOM	8580	OD2	ASP	F	266	−24.013	60.933	−34.844	1.00	40.99	B000	O1−
ATOM	8581	N	ASP	F	267	−21.943	63.261	−30.935	1.00	35.94	B000	N
ATOM	8582	CA	ASP	F	267	−21.403	64.616	−31.027	1.00	36.54	B000	C
ATOM	8583	C	ASP	F	267	−19.880	64.547	−31.126	1.00	34.86	B000	C
ATOM	8584	O	ASP	F	267	−19.271	63.507	−30.850	1.00	34.33	B000	O
ATOM	8585	CB	ASP	F	267	−21.835	65.470	−29.834	1.00	30.38	B000	C
ATOM	8586	CG	ASP	F	267	−21.905	66.947	−30.180	1.00	43.85	B000	C
ATOM	8587	OD1	ASP	F	267	−21.377	67.294	−31.265	1.00	39.52	B000	O
ATOM	8588	OD2	ASP	F	267	−22.463	67.744	−29.369	1.00	37.84	B000	O1−
ATOM	8589	N	VAL	F	268	−19.263	65.675	−31.519	1.00	30.07	B000	N
ATOM	8590	CA	VAL	F	268	−17.811	65.692	−31.674	1.00	34.19	B000	C
ATOM	8591	C	VAL	F	268	−17.155	65.408	−30.331	1.00	32.91	B000	C
ATOM	8592	O	VAL	F	268	−17.605	65.876	−29.277	1.00	34.33	B000	O
ATOM	8593	CB	VAL	F	268	−17.313	67.013	−32.292	1.00	36.17	B000	C
ATOM	8594	CG1	VAL	F	268	−17.784	67.114	−33.734	1.00	30.93	B000	C
ATOM	8595	CG2	VAL	F	268	−17.786	68.204	−31.515	1.00	29.63	B000	C
ATOM	8596	N	CYS	F	269	−16.096	64.605	−30.366	1.00	30.58	B000	N
ATOM	8597	CA	CYS	F	269	−15.512	64.059	−29.147	1.00	32.39	B000	C
ATOM	8598	C	CYS	F	269	−14.819	65.101	−28.276	1.00	35.95	B000	C
ATOM	8599	O	CYS	F	269	−14.508	64.795	−27.110	1.00	34.91	B000	O
ATOM	8600	CB	CYS	F	269	−14.527	62.940	−29.502	1.00	40.17	B000	C
ATOM	8601	SG	CYS	F	269	−15.360	61.521	−30.340	1.00	50.58	B000	S
ATOM	8602	N	GLN	F	270	−14.605	66.326	−28.768	1.00	30.41	B000	N
ATOM	8603	CA	GLN	F	270	−13.991	67.316	−27.886	1.00	37.36	B000	C
ATOM	8604	C	GLN	F	270	−14.990	68.026	−26.982	1.00	33.95	B000	C
ATOM	8605	O	GLN	F	270	−14.541	68.820	−26.158	1.00	37.08	B000	O
ATOM	8606	CB	GLN	F	270	−13.179	68.371	−28.659	1.00	34.85	B000	C
ATOM	8607	CG	GLN	F	270	−13.560	68.598	−30.097	1.00	52.16	B000	C
ATOM	8608	CD	GLN	F	270	−13.134	67.433	−30.977	1.00	59.41	B000	C
ATOM	8609	OE1	GLN	F	270	−13.911	66.970	−31.818	1.00	54.59	B000	O
ATOM	8610	NE2	GLN	F	270	−11.912	66.916	−30.748	1.00	48.02	B000	N
ATOM	8611	N	ARG	F	271	−16.302	67.744	−27.083	1.00	27.57	B000	N
ATOM	8612	CA	ARG	F	271	−17.274	68.311	−26.158	1.00	29.87	B000	C
ATOM	8613	C	ARG	F	271	−16.853	68.013	−24.720	1.00	34.79	B000	C
ATOM	8614	O	ARG	F	271	−16.512	66.861	−24.400	1.00	30.23	B000	O
ATOM	8615	CB	ARG	F	271	−18.688	67.750	−26.374	1.00	30.54	B000	C
ATOM	8616	CG	ARG	F	271	−19.384	68.131	−27.667	1.00	31.79	B000	C
ATOM	8617	CD	ARG	F	271	−19.505	69.613	−27.794	1.00	33.75	B000	C
ATOM	8618	NE	ARG	F	271	−20.347	70.002	−28.916	1.00	33.09	B000	N
ATOM	8619	CZ	ARG	F	271	−20.385	71.243	−29.388	1.00	38.41	B000	C
ATOM	8620	NH1	ARG	F	271	−19.614	72.177	−28.817	1.00	34.05	B000	N1+
ATOM	8621	NH2	ARG	F	271	−21.173	71.556	−30.417	1.00	29.00	B000	N
ATOM	8622	N	PRO	F	272	−16.862	68.955	−23.879	1.00	32.65	B000	N
ATOM	8623	CA	PRO	F	272	−16.460	68.718	−22.481	1.00	27.76	B000	C
ATOM	8624	C	PRO	F	272	−17.615	68.190	−21.630	1.00	31.78	B000	C
ATOM	8625	O	PRO	F	272	−18.061	68.832	−20.676	1.00	29.70	B000	O
ATOM	8626	CB	PRO	F	272	−15.983	70.111	−22.042	1.00	28.08	B000	C
ATOM	8627	CG	PRO	F	272	−16.860	71.083	−22.841	1.00	28.41	B000	C
ATOM	8628	CD	PRO	F	272	−17.059	70.391	−24.190	1.00	31.14	B000	C
ATOM	8629	N	TYR	F	273	−18.129	67.005	−21.987	1.00	32.02	B000	N
ATOM	8630	CA	TYR	F	273	−19.251	66.438	−21.248	1.00	31.15	B000	C
ATOM	8631	C	TYR	F	273	−18.759	65.726	−19.999	1.00	28.60	B000	C
ATOM	8632	O	TYR	F	273	−17.577	65.427	−19.850	1.00	27.10	B000	O
ATOM	8633	CB	TYR	F	273	−20.061	65.473	−22.113	1.00	28.19	B000	C
ATOM	8634	CG	TYR	F	273	−20.762	66.174	−23.244	1.00	30.22	B000	C
ATOM	8635	CD1	TYR	F	273	−21.111	67.519	−23.133	1.00	29.80	B000	C
ATOM	8636	CD2	TYR	F	273	−21.057	65.512	−24.440	1.00	28.43	B000	C
ATOM	8637	CE1	TYR	F	273	−21.765	68.193	−24.178	1.00	29.36	B000	C
ATOM	8638	CE2	TYR	F	273	−21.695	66.178	−25.493	1.00	26.89	B000	C
ATOM	8639	CZ	TYR	F	273	−22.039	67.519	−25.355	1.00	30.78	B000	C
ATOM	8640	OH	TYR	F	273	−22.668	68.191	−26.375	1.00	33.01	B000	O
ATOM	8641	N	ARG	F	274	−19.688	65.469	−19.083	1.00	31.67	B000	N
ATOM	8642	CA	ARG	F	274	−19.383	64.573	−17.977	1.00	32.33	B000	C
ATOM	8643	C	ARG	F	274	−19.177	63.156	−18.523	1.00	29.48	B000	C
ATOM	8644	O	ARG	F	274	−19.403	62.875	−19.703	1.00	29.20	B000	O
ATOM	8645	CB	ARG	F	274	−20.501	64.618	−16.931	1.00	33.56	B000	C
ATOM	8646	CG	ARG	F	274	−20.639	65.990	−16.246	1.00	34.67	B000	C
ATOM	8647	CD	ARG	F	274	−21.615	65.998	−15.050	1.00	38.53	B000	C
ATOM	8648	NE	ARG	F	274	−21.480	67.235	−14.265	1.00	37.38	B000	N
ATOM	8649	CZ	ARG	F	274	−22.106	67.482	−13.117	1.00	34.94	B000	C
ATOM	8650	NH1	ARG	F	274	−22.944	66.591	−12.600	1.00	33.17	B000	N1+
ATOM	8651	NH2	ARG	F	274	−21.886	68.623	−12.476	1.00	31.06	B000	N
ATOM	8652	N	TRP	F	275	−18.741	62.250	−17.662	1.00	29.84	B000	N
ATOM	8653	CA	TRP	F	275	−18.518	60.878	−18.100	1.00	34.86	B000	C
ATOM	8654	C	TRP	F	275	−18.726	59.935	−16.926	1.00	36.82	B000	C
ATOM	8655	O	TRP	F	275	−18.766	60.351	−15.763	1.00	32.31	B000	O
ATOM	8656	CB	TRP	F	275	−17.112	60.684	−18.679	1.00	28.66	B000	C
ATOM	8657	CG	TRP	F	275	−16.078	60.676	−17.628	1.00	32.25	B000	C
ATOM	8658	CD1	TRP	F	275	−15.531	59.586	−17.019	1.00	34.72	B000	C
ATOM	8659	CD2	TRP	F	275	−15.448	61.826	−17.041	1.00	33.73	B000	C
ATOM	8660	NE1	TRP	F	275	−14.587	59.989	−16.085	1.00	33.65	B000	N
ATOM	8661	CE2	TRP	F	275	−14.521	61.358	−16.087	1.00	32.03	B000	C
ATOM	8662	CE3	TRP	F	275	−15.575	63.203	−17.238	1.00	32.63	B000	C
ATOM	8663	CZ2	TRP	F	275	−13.732	62.217	−15.334	1.00	34.54	B000	C
ATOM	8664	CZ3	TRP	F	275	−14.798	64.057	−16.476	1.00	32.70	B000	C
ATOM	8665	CH2	TRP	F	275	−13.890	63.563	−15.542	1.00	33.77	B000	C
ATOM	8666	N	VAL	F	276	−18.840	58.646	−17.247	1.00	33.42	B000	N
ATOM	8667	CA	VAL	F	276	−19.034	57.591	−16.256	1.00	37.19	B000	C
ATOM	8668	C	VAL	F	276	−17.985	56.504	−16.480	1.00	41.17	B000	C
ATOM	8669	O	VAL	F	276	−17.762	56.073	−17.620	1.00	38.26	B000	O
ATOM	8670	CB	VAL	F	276	−20.454	56.999	−16.338	1.00	37.30	B000	C
ATOM	8671	CG1	VAL	F	276	−20.677	55.983	−15.212	1.00	34.94	B000	C
ATOM	8672	CG2	VAL	F	276	−21.488	58.117	−16.312	1.00	29.37	B000	C
ATOM	8673	N	CYS	F	277	−17.328	56.085	−15.402	1.00	36.51	B000	N
ATOM	8674	CA	CYS	F	277	−16.406	54.958	−15.437	1.00	39.62	B000	C
ATOM	8675	C	CYS	F	277	−17.094	53.700	−14.909	1.00	45.76	B000	C
ATOM	8676	O	CYS	F	277	−17.945	53.759	−14.015	1.00	44.66	B000	O
ATOM	8677	CB	CYS	F	277	−15.146	55.230	−14.605	1.00	40.57	B000	C
ATOM	8678	SG	CYS	F	277	−14.058	56.553	−15.196	1.00	50.52	B000	S
ATOM	8679	N	GLU	F	278	−16.695	52.557	−15.462	1.00	39.15	B000	N
ATOM	8680	CA	GLU	F	278	−17.250	51.260	−15.112	1.00	44.84	B000	C
ATOM	8681	C	GLU	F	278	−16.120	50.256	−14.936	1.00	47.20	B000	C
ATOM	8682	O	GLU	F	278	−15.173	50.230	−15.729	1.00	47.48	B000	O
ATOM	8683	CB	GLU	F	278	−18.203	50.751	−16.194	1.00	38.93	B000	C
ATOM	8684	CG	GLU	F	278	−18.836	49.416	−15.857	1.00	46.64	B000	C
ATOM	8685	CD	GLU	F	278	−19.732	48.897	−16.963	1.00	49.83	B000	C
ATOM	8686	OE1	GLU	F	278	−19.861	49.572	−18.007	1.00	51.92	B000	O
ATOM	8687	OE2	GLU	F	278	−20.316	47.813	−16.790	1.00	61.81	B000	O1−
ATOM	8688	N	THR	F	279	−16.212	49.447	−13.886	1.00	44.44	B000	N
ATOM	8689	CA	THR	F	279	−15.287	48.339	−13.689	1.00	49.01	B000	C
ATOM	8690	C	THR	F	279	−16.035	47.205	−13.000	1.00	55.21	B000	C
ATOM	8691	O	THR	F	279	−17.179	47.359	−12.564	1.00	50.33	B000	O
ATOM	8692	CB	THR	F	279	−14.035	48.775	−12.899	1.00	50.55	B000	C
ATOM	8693	OG1	THR	F	279	−13.019	47.768	−13.000	1.00	60.70	B000	O
ATOM	8694	CG2	THR	F	279	−14.349	49.063	−11.433	1.00	40.44	B000	C
ATOM	8695	N	GLU	F	280	−15.392	46.046	−12.929	1.00	62.33	B000	N
ATOM	8696	CA	GLU	F	280	−16.042	44.856	−12.389	1.00	60.95	B000	C
ATOM	8697	C	GLU	F	280	−15.846	44.774	−10.881	1.00	59.82	B000	C
ATOM	8698	O	GLU	F	280	−14.755	45.070	−10.384	1.00	61.25	B000	O
ATOM	8699	CB	GLU	F	280	−15.489	43.597	−13.056	1.00	64.94	B000	C
ATOM	8700	CG	GLU	F	280	−13.982	43.637	−13.300	1.00	75.16	B000	C
ATOM	8701	CD	GLU	F	280	−13.631	44.136	−14.695	1.00	87.07	B000	C
ATOM	8702	OE1	GLU	F	280	−14.294	43.684	−15.660	1.00	92.63	B000	O
ATOM	8703	OE2	GLU	F	280	−12.707	44.977	−14.825	1.00	87.02	B000	O1−
ATOM	8704	N	GLU	F	281	−16.934	44.447	−10.167	1.00	59.93	B000	N
ATOM	8705	CA	GLU	F	281	−16.960	43.756	−8.848	1.00	67.16	B000	C
ATOM	8706	C	GLU	F	281	−18.241	44.090	−8.095	1.00	67.27	B000	C
ATOM	8707	O	GLU	F	281	−18.257	44.100	−6.862	1.00	68.70	B000	O
ATOM	8708	CB	GLU	F	281	−15.757	44.085	−7.951	1.00	63.68	B000	C
ATOM	8709	CG	GLU	F	281	−15.131	42.885	−7.230	1.00	68.36	B000	C
ATOM	8710	CD	GLU	F	281	−14.442	41.881	−8.172	1.00	83.09	B000	C
ATOM	8711	OE1	GLU	F	281	−15.127	41.287	−9.037	1.00	77.83	B000	O
ATOM	8712	OE2	GLU	F	281	−13.210	41.679	−8.043	1.00	76.05	B000	O
TER
HETATM	9170	C1	GAL	G	401	19.131	84.986	−13.073	1.00	67.87		C
HETATM	9171	O1	GAL	G	401	19.230	83.939	−14.075	1.00	65.01		O
HETATM	9172	C2	GAL	G	401	19.826	84.527	−11.743	1.00	63.05		C
HETATM	9173	O2	GAL	G	401	19.202	83.373	−11.240	1.00	42.62		O
HETATM	9174	C3	GAL	G	401	19.822	85.673	−10.639	1.00	71.79		C
HETATM	9175	O3	GAL	G	401	20.324	85.299	−9.317	1.00	63.98		O
HETATM	9176	C4	GAL	G	401	20.547	86.954	−11.192	1.00	74.66		C
HETATM	9177	O4	GAL	G	401	21.936	86.736	−11.495	1.00	79.63		O
HETATM	9178	C5	GAL	G	401	19.774	87.370	−12.469	1.00	75.84		C
HETATM	9179	O5	GAL	G	401	19.667	86.275	−13.538	1.00	68.13		O
HETATM	9180	C6	GAL	G	401	20.270	88.659	−13.125	1.00	68.64		C
HETATM	9181	O6	GAL	G	401	19.157	89.413	−13.631	1.00	52.02		O
TER
HETATM	9182	C1	GAL	G	402	−25.502	71.256	−32.056	1.00	74.77		C
HETATM	9183	O1	GAL	G	402	−24.812	72.366	−32.713	1.00	60.32		O
HETATM	9184	C2	GAL	G	402	−26.779	71.727	−31.263	1.00	62.62		C
HETATM	9185	O2	GAL	G	402	−26.494	72.728	−30.323	1.00	41.25		O
HETATM	9186	C3	GAL	G	402	−27.470	70.522	−30.515	1.00	66.23		C
HETATM	9187	O3	GAL	G	402	−28.624	70.910	−29.737	1.00	63.41		O
HETATM	9188	C4	GAL	G	402	−27.905	69.432	−31.526	1.00	75.11		C
HETATM	9189	O4	GAL	G	402	−29.064	69.854	−32.279	1.00	80.69		O
HETATM	9190	C5	GAL	G	402	−26.702	69.051	−32.464	1.00	82.81		C
HETATM	9191	O5	GAL	G	402	−25.897	70.216	−33.013	1.00	81.70		O
HETATM	9192	C6	GAL	G	402	−27.102	68.166	−33.664	1.00	85.18		C
HETATM	9193	O6	GAL	G	402	−26.406	68.545	−34.844	1.00	94.12		O
TER
HETATM	9194	CA	CA	H	1	21.469	91.701	−14.212	1.00	79.84		Ca
TER
HETATM	9195	CA	CA	H	2	−26.073	64.419	−34.040	1.00	79.26		Ca
TER
HETATM	9196	CA	CA	H	3	−18.333	61.223	−36.994	1.00	75.64		Ca
HETATM	9197	CA	CA	H	4	18.240	94.784	−21.928	1.00	73.55		Ca
TER

TABLE 10.4
ATOM	1	O	GLN	A	1	−24.853	−26.439	84.334	1.00	39.67		O
ATOM	2	N	GLN	A	1	−23.947	−29.300	85.222	1.00	49.60		N
ATOM	3	CA	GLN	A	1	−24.872	−28.345	85.852	1.00	56.88		C
ATOM	4	C	GLN	A	1	−25.501	−27.209	85.050	1.00	51.47		C
ATOM	5	CB	GLN	A	1	−24.208	−27.745	87.074	1.00	45.63		C
ATOM	6	CG	GLN	A	1	−23.967	−28.823	88.054	1.00	44.21		C
ATOM	7	CD	GLN	A	1	−25.274	−29.457	88.407	1.00	54.28		C
ATOM	8	OE1	GLN	A	1	−26.030	−28.899	89.200	1.00	62.35		O
ATOM	9	NE2	GLN	A	1	−25.592	−30.592	87.778	1.00	57.03		N
ATOM	10	N	VAL	A	2	−26.812	−27.135	85.264	1.00	51.10		N
ATOM	11	CA	VAL	A	2	−27.671	−26.124	84.683	1.00	42.93		C
ATOM	12	C	VAL	A	2	−27.754	−24.968	85.669	1.00	44.75		C
ATOM	13	O	VAL	A	2	−28.236	−25.134	86.793	1.00	42.04		O
ATOM	14	CB	VAL	A	2	−29.061	−26.696	84.378	1.00	39.51		C
ATOM	15	CG1	VAL	A	2	−29.809	−25.773	83.468	1.00	44.64		C
ATOM	16	CG2	VAL	A	2	−28.948	−28.065	83.754	1.00	39.26		C
ATOM	17	N	GLN	A	3	−27.240	−23.812	85.269	1.00	45.15		N
ATOM	18	CA	GLN	A	3	−27.403	−22.586	86.031	1.00	44.60		C
ATOM	19	C	GLN	A	3	−28.455	−21.725	85.355	1.00	34.85		C
ATOM	20	O	GLN	A	3	−28.496	−21.629	84.128	1.00	39.72		O
ATOM	21	CB	GLN	A	3	−26.091	−21.792	86.128	1.00	50.01		C
ATOM	22	CG	GLN	A	3	−24.978	−22.456	86.931	1.00	56.60		C
ATOM	23	CD	GLN	A	3	−23.919	−23.128	86.052	1.00	59.49		C
ATOM	24	OE1	GLN	A	3	−24.036	−23.141	84.811	1.00	56.42		O
ATOM	25	NE2	GLN	A	3	−22.874	−23.691	86.692	1.00	48.31		N
ATOM	26	N	LEU	A	4	−29.296	−21.109	86.161	1.00	34.42		N
ATOM	27	CA	LEU	A	4	−30.179	−20.024	85.752	1.00	31.59		C
ATOM	28	C	LEU	A	4	−29.640	−18.812	86.491	1.00	37.33		C
ATOM	29	O	LEU	A	4	−29.854	−18.673	87.696	1.00	44.24		O
ATOM	30	CB	LEU	A	4	−31.634	−20.283	86.124	1.00	31.99		C
ATOM	31	CG	LEU	A	4	−32.309	−21.572	85.670	1.00	34.73		C
ATOM	32	CD1	LEU	A	4	−33.852	−21.433	85.729	1.00	32.19		C
ATOM	33	CD2	LEU	A	4	−31.838	−21.916	84.287	1.00	30.49		C
ATOM	34	N	GLN	A	5	−28.883	−17.976	85.797	1.00	40.51		N
ATOM	35	CA	GLN	A	5	−28.269	−16.810	86.412	1.00	38.81		C
ATOM	36	C	GLN	A	5	−29.203	−15.614	86.259	1.00	37.64		C
ATOM	37	O	GLN	A	5	−29.714	−15.358	85.170	1.00	41.01		O
ATOM	38	CB	GLN	A	5	−26.911	−16.544	85.768	1.00	38.94		C
ATOM	39	CG	GLN	A	5	−26.103	−17.812	85.595	1.00	46.98		C
ATOM	40	CD	GLN	A	5	−24.690	−17.565	85.045	1.00	61.68		C
ATOM	41	OE1	GLN	A	5	−24.523	−17.011	83.956	1.00	63.24		O
ATOM	42	NE2	GLN	A	5	−23.671	−17.982	85.800	1.00	53.29		N
ATOM	43	N	GLN	A	6	−29.465	−14.912	87.348	1.00	37.71		N
ATOM	44	CA	GLN	A	6	−30.413	−13.810	87.326	1.00	37.43		C
ATOM	45	C	GLN	A	6	−29.670	−12.491	87.484	1.00	41.79		C
ATOM	46	O	GLN	A	6	−28.694	−12.405	88.237	1.00	42.07		O
ATOM	47	CB	GLN	A	6	−31.445	−13.932	88.448	1.00	34.57		C
ATOM	48	CG	GLN	A	6	−32.083	−15.276	88.561	1.00	37.33		C
ATOM	49	CD	GLN	A	6	−33.308	−15.279	89.458	1.00	36.27		C
ATOM	50	OE1	GLN	A	6	−33.695	−16.319	89.966	1.00	30.06		O
ATOM	51	NE2	GLN	A	6	−33.920	−14.117	89.653	1.00	32.89		N
ATOM	52	N	TRP	A	7	−30.144	−11.463	86.785	1.00	36.25		N
ATOM	53	CA	TRP	A	7	−29.729	−10.098	87.059	1.00	33.75		C
ATOM	54	C	TRP	A	7	−30.876	−9.160	86.714	1.00	37.39		C
ATOM	55	O	TRP	A	7	−31.883	−9.557	86.120	1.00	39.47		O
ATOM	56	CB	TRP	A	7	−28.452	−9.723	86.303	1.00	33.51		C
ATOM	57	CG	TRP	A	7	−28.542	−9.763	84.822	1.00	34.91		C
ATOM	58	CD1	TRP	A	7	−28.929	−8.739	83.990	1.00	37.52		C
ATOM	59	CD2	TRP	A	7	−28.206	−10.865	83.970	1.00	37.56		C
ATOM	60	NE1	TRP	A	7	−28.872	−9.149	82.675	1.00	37.51		N
ATOM	61	CE2	TRP	A	7	−28.425	−10.446	82.635	1.00	36.81		C
ATOM	62	CE3	TRP	A	7	−27.737	−12.160	84.204	1.00	43.59		C
ATOM	63	CZ2	TRP	A	7	−28.199	−11.280	81.542	1.00	35.12		C
ATOM	64	CZ3	TRP	A	7	−27.517	−12.993	83.112	1.00	48.14		C
ATOM	65	CH2	TRP	A	7	−27.754	−12.547	81.797	1.00	43.93		C
ATOM	66	N	GLY	A	8	−30.711	−7.909	87.092	1.00	31.94		N
ATOM	67	CA	GLY	A	8	−31.730	−6.894	86.915	1.00	32.15		C
ATOM	68	C	GLY	A	8	−31.597	−6.027	88.146	1.00	36.03		C
ATOM	69	O	GLY	A	8	−31.196	−6.479	89.217	1.00	34.32		O
ATOM	70	N	ALA	A	9	−31.911	−4.745	87.991	1.00	39.30		N
ATOM	71	CA	ALA	A	9	−31.830	−3.844	89.129	1.00	40.16		C
ATOM	72	C	ALA	A	9	−32.853	−4.275	90.168	1.00	41.09		C
ATOM	73	O	ALA	A	9	−34.026	−4.460	89.845	1.00	43.60		O
ATOM	74	CB	ALA	A	9	−32.073	−2.399	88.690	1.00	33.25		C
ATOM	75	N	GLY	A	10	−32.405	−4.458	91.411	1.00	37.64		N
ATOM	76	CA	GLY	A	10	−33.275	−4.938	92.461	1.00	28.47		C
ATOM	77	C	GLY	A	10	−33.861	−3.889	93.382	1.00	36.57		C
ATOM	78	O	GLY	A	10	−34.710	−4.214	94.213	1.00	43.35		O
ATOM	79	N	LEU	A	11	−33.418	−2.638	93.273	1.00	36.99		N
ATOM	80	CA	LEU	A	11	−33.946	−1.533	94.067	1.00	34.54		C
ATOM	81	C	LEU	A	11	−34.748	−0.595	93.168	1.00	35.85		C
ATOM	82	O	LEU	A	11	−34.244	−0.129	92.144	1.00	38.05		O
ATOM	83	CB	LEU	A	11	−32.818	−0.764	94.760	1.00	36.89		C
ATOM	84	CG	LEU	A	11	−33.040	−0.447	96.238	1.00	40.06		C
ATOM	85	CD1	LEU	A	11	−31.989	0.520	96.748	1.00	38.21		C
ATOM	86	CD2	LEU	A	11	−34.443	0.097	96.487	1.00	39.59		C
ATOM	87	N	LEU	A	12	−35.997	−0.333	93.537	1.00	36.22		N
ATOM	88	CA	LEU	A	12	−36.874	0.495	92.724	1.00	38.68		C
ATOM	89	C	LEU	A	12	−37.710	1.388	93.624	1.00	37.27		C
ATOM	90	O	LEU	A	12	−37.955	1.071	94.791	1.00	40.06		O
ATOM	91	CB	LEU	A	12	−37.815	−0.342	91.843	1.00	36.78		C
ATOM	92	CG	LEU	A	12	−37.179	−1.328	90.872	1.00	36.77		C
ATOM	93	CD1	LEU	A	12	−38.285	−2.117	90.244	1.00	42.02		C
ATOM	94	CD2	LEU	A	12	−36.382	−0.610	89.812	1.00	40.37		C
ATOM	95	N	LYS	A	13	−38.164	2.508	93.053	1.00	36.92		N
ATOM	96	CA	LYS	A	13	−39.141	3.391	93.665	1.00	36.42		C
ATOM	97	C	LYS	A	13	−40.505	3.163	93.036	1.00	35.60		C
ATOM	98	O	LYS	A	13	−40.605	2.637	91.921	1.00	39.97		O
ATOM	99	CB	LYS	A	13	−38.711	4.848	93.499	1.00	41.56		C
ATOM	100	CG	LYS	A	13	−37.227	5.088	93.781	1.00	52.81		C
ATOM	101	CD	LYS	A	13	−36.541	5.678	92.538	1.00	68.42		C
ATOM	102	CE	LYS	A	13	−35.056	5.297	92.399	1.00	70.40		C
ATOM	103	NZ	LYS	A	13	−34.516	5.679	91.038	1.00	67.86		N1+
ATOM	104	N	PRO	A	14	−41.587	3.512	93.736	1.00	32.85		N
ATOM	105	CA	PRO	A	14	−42.932	3.257	93.200	1.00	31.49		C
ATOM	106	C	PRO	A	14	−43.114	3.852	91.806	1.00	38.32		C
ATOM	107	O	PRO	A	14	−42.521	4.880	91.465	1.00	35.32		O
ATOM	108	CB	PRO	A	14	−43.852	3.929	94.218	1.00	25.23		C
ATOM	109	CG	PRO	A	14	−43.104	3.927	95.441	1.00	29.72		C
ATOM	110	CD	PRO	A	14	−41.646	4.040	95.105	1.00	33.69		C
ATOM	111	N	SER	A	15	−43.920	3.155	90.996	1.00	36.29		N
ATOM	112	CA	SER	A	15	−44.274	3.500	89.622	1.00	33.19		C
ATOM	113	C	SER	A	15	−43.184	3.147	88.614	1.00	34.56		C
ATOM	114	O	SER	A	15	−43.472	3.106	87.414	1.00	34.31		O
ATOM	115	CB	SER	A	15	−44.597	4.994	89.468	1.00	38.65		C
ATOM	116	OG	SER	A	15	−43.421	5.751	89.168	1.00	34.68		O
ATOM	117	N	GLU	A	16	−41.943	2.899	89.051	1.00	30.66		N
ATOM	118	CA	GLU	A	16	−40.952	2.443	88.083	1.00	28.63		C
ATOM	119	C	GLU	A	16	−41.330	1.055	87.551	1.00	33.32		C
ATOM	120	O	GLU	A	16	−42.281	0.410	88.010	1.00	35.10		O
ATOM	121	CB	GLU	A	16	−39.539	2.437	88.684	1.00	30.89		C
ATOM	122	CG	GLU	A	16	−39.075	3.729	89.360	1.00	31.88		C
ATOM	123	CD	GLU	A	16	−37.549	3.780	89.616	1.00	49.97		C
ATOM	124	OE1	GLU	A	16	−36.907	2.727	89.843	1.00	54.84		O
ATOM	125	OE2	GLU	A	16	−36.967	4.885	89.556	1.00	57.53		O
ATOM	126	N	THR	A	17	−40.583	0.583	86.565	1.00	32.70		N
ATOM	127	CA	THR	A	17	−40.829	−0.744	86.034	1.00	35.01		C
ATOM	128	C	THR	A	17	−39.637	−1.655	86.318	1.00	38.16		C
ATOM	129	O	THR	A	17	−38.473	−1.238	86.259	1.00	36.52		O
ATOM	130	CB	THR	A	17	−41.198	−0.690	84.543	1.00	36.57		C
ATOM	131	OG1	THR	A	17	−40.325	−1.515	83.766	1.00	34.00		O
ATOM	132	CG2	THR	A	17	−41.198	0.711	84.055	1.00	37.19		C
ATOM	133	N	LEU	A	18	−39.955	−2.874	86.733	1.00	35.90		N
ATOM	134	CA	LEU	A	18	−38.969	−3.873	87.100	1.00	33.49		C
ATOM	135	C	LEU	A	18	−38.603	−4.669	85.861	1.00	32.72		C
ATOM	136	O	LEU	A	18	−39.482	−5.056	85.082	1.00	30.94		O
ATOM	137	CB	LEU	A	18	−39.537	−4.770	88.209	1.00	34.34		C
ATOM	138	CG	LEU	A	18	−38.899	−6.037	88.790	1.00	34.31		C
ATOM	139	C1	LEU	A	18	−39.067	−7.231	87.855	1.00	31.61		C
ATOM	140	CD2	LEU	A	18	−37.433	−5.823	89.128	1.00	34.33		C
ATOM	141	N	SER	A	19	−37.309	−4.888	85.660	1.00	31.86		N
ATOM	142	CA	SER	A	19	−36.877	−5.700	84.536	1.00	35.19		C
ATOM	143	C	SER	A	19	−35.754	−6.613	85.001	1.00	31.16		C
ATOM	144	O	SER	A	19	−34.777	−6.145	85.596	1.00	30.06		O
ATOM	145	CB	SER	A	19	−36.449	−4.841	83.346	1.00	33.07		C
ATOM	146	OG	SER	A	19	−35.218	−4.239	83.612	1.00	47.41		O
ATOM	147	N	LEU	A	20	−35.934	−7.916	84.768	1.00	25.55		N
ATOM	148	CA	LEU	A	20	−35.022	−8.962	85.214	1.00	28.53		C
ATOM	149	C	LEU	A	20	−34.777	−9.941	84.074	1.00	27.96		C
ATOM	150	O	LEU	A	20	−35.643	−10.142	83.220	1.00	27.00		O
ATOM	151	CB	LEU	A	20	−35.596	−9.712	86.425	1.00	26.52		C
ATOM	152	CG	LEU	A	20	−35.939	−8.899	87.678	1.00	29.44		C
ATOM	153	CD1	LEU	A	20	−36.684	−9.780	88.650	1.00	34.23		C
ATOM	154	CD2	LEU	A	20	−34.683	−8.369	88.365	1.00	31.36		C
ATOM	155	N	THR	A	21	−33.589	−10.552	84.061	1.00	28.15		N
ATOM	156	CA	THR	A	21	−33.237	−11.526	83.034	1.00	30.18		C
ATOM	157	C	THR	A	21	−32.621	−12.772	83.663	1.00	33.03		C
ATOM	158	O	THR	A	21	−31.918	−12.678	84.673	1.00	38.27		O
ATOM	159	CB	THR	A	21	−32.240	−10.913	82.023	1.00	32.85		C
ATOM	160	OG1	THR	A	21	−32.757	−9.670	81.536	1.00	32.16		O
ATOM	161	CG2	THR	A	21	−31.977	−11.866	80.841	1.00	28.45		C
ATOM	162	N	CYS	A	22	−32.883	−13.939	83.053	1.00	27.52		N
ATOM	163	CA	CYS	A	22	−32.197	−15.190	83.374	1.00	32.00		C
ATOM	164	C	CYS	A	22	−31.452	−15.675	82.149	1.00	29.74		C
ATOM	165	O	CYS	A	22	−31.974	−15.629	81.036	1.00	26.79		O
ATOM	166	CB	CYS	A	22	−33.116	−16.343	83.872	1.00	27.00		C
ATOM	167	SG	CYS	A	22	−33.354	−16.118	85.624	1.00	68.31		S
ATOM	168	N	ALA	A	23	−30.228	−16.135	82.379	1.00	32.24		N
ATOM	169	CA	ALA	A	23	−29.397	−16.762	81.370	1.00	32.34		C
ATOM	170	C	ALA	A	23	−29.311	−18.234	81.721	1.00	30.10		C
ATOM	171	O	ALA	A	23	−29.020	−18.577	82.867	1.00	34.73		O
ATOM	172	CB	ALA	A	23	−28.004	−16.125	81.339	1.00	32.68		C
ATOM	173	N	VAL	A	24	−29.614	−19.093	80.763	1.00	27.15		N
ATOM	174	CA	VAL	A	24	−29.616	−20.533	80.977	1.00	32.40		C
ATOM	175	C	VAL	A	24	−28.371	−21.124	80.342	1.00	32.49		C
ATOM	176	O	VAL	A	24	−28.115	−20.916	79.155	1.00	31.92		O
ATOM	177	CB	VAL	A	24	−30.872	−21.204	80.377	1.00	31.63		C
ATOM	178	CG1	VAL	A	24	−30.833	−22.694	80.642	1.00	23.27		C
ATOM	179	CG2	VAL	A	24	−32.187	−20.590	80.898	1.00	27.72		C
ATOM	180	N	SER	A	25	−27.609	−21.875	81.117	1.00	37.38		N
ATOM	181	CA	SER	A	25	−26.471	−22.620	80.602	1.00	34.69		C
ATOM	182	C	SER	A	25	−26.544	−24.037	81.136	1.00	37.68		C
ATOM	183	O	SER	A	25	−27.107	−24.279	82.206	1.00	45.11		O
ATOM	184	CB	SER	A	25	−25.146	−21.979	81.013	1.00	35.05		C
ATOM	185	OG	SER	A	25	−25.168	−21.665	82.396	1.00	40.52		O
ATOM	186	N	GLY	A	26	−25.978	−24.977	80.405	1.00	31.17		N
ATOM	187	CA	GLY	A	26	−25.970	−26.319	80.939	1.00	34.95		C
ATOM	188	C	GLY	A	26	−26.773	−27.339	80.181	1.00	44.75		C
ATOM	189	O	GLY	A	26	−26.261	−28.422	79.895	1.00	53.93		O
ATOM	190	N	GLY	A	27	−28.035	−27.049	79.897	1.00	43.99		N
ATOM	191	CA	GLY	A	27	−28.827	−28.022	79.179	1.00	39.13		C
ATOM	192	C	GLY	A	27	−29.426	−27.412	77.935	1.00	44.00		C
ATOM	193	O	GLY	A	27	−28.940	−26.394	77.426	1.00	44.61		O
ATOM	194	N	SER	A	28	−30.525	−27.991	77.475	1.00	48.00		N
ATOM	195	CA	SER	A	28	−31.204	−27.507	76.286	1.00	42.16		C
ATOM	196	C	SER	A	28	−32.051	−26.285	76.611	1.00	41.49		C
ATOM	197	O	SER	A	28	−32.302	−25.961	77.778	1.00	37.48		O
ATOM	198	CB	SER	A	28	−32.071	−28.605	75.684	1.00	39.00		C
ATOM	199	OG	SER	A	28	−31.253	−29.679	75.263	1.00	45.34		O
ATOM	200	N	PHE	A	29	−32.448	−25.569	75.552	1.00	39.22		N
ATOM	201	CA	PHE	A	29	−33.327	−24.425	75.695	1.00	34.42		C
ATOM	202	C	PHE	A	29	−34.696	−24.653	75.097	1.00	38.24		C
ATOM	203	O	PHE	A	29	−35.628	−23.923	75.439	1.00	40.29		O
ATOM	204	CB	PHE	A	29	−32.710	−23.181	75.041	1.00	30.96		C
ATOM	205	CG	PHE	A	29	−33.191	−21.874	75.633	1.00	31.50		C
ATOM	206	CD1	PHE	A	29	−33.148	−21.663	77.004	1.00	33.59		C
ATOM	207	CD2	PHE	A	29	−33.660	−20.850	74.823	1.00	28.85		C
ATOM	208	CE1	PHE	A	29	−33.578	−20.450	77.564	1.00	31.05		C
ATOM	209	CE2	PHE	A	29	−34.073	−19.653	75.359	1.00	29.76		C
ATOM	210	CZ	PHE	A	29	−34.042	−19.449	76.740	1.00	30.19		C
ATOM	211	N	ARG	A	30	−34.855	−25.653	74.242	1.00	41.39		N
ATOM	212	CA	ARG	A	30	−36.009	−25.653	73.362	1.00	44.20		C
ATOM	213	C	ARG	A	30	−37.145	−26.551	73.833	1.00	39.55		C
ATOM	214	O	ARG	A	30	−38.265	−26.412	73.331	1.00	42.77		O
ATOM	215	CB	ARG	A	30	−35.568	−26.002	71.939	1.00	31.85		C
ATOM	216	CG	ARG	A	30	−35.075	−27.382	71.728	1.00	39.91		C
ATOM	217	CD	ARG	A	30	−34.814	−27.548	70.245	1.00	43.27		C
ATOM	218	NE	ARG	A	30	−33.604	−28.305	69.892	1.00	49.24		N
ATOM	219	CZ	ARG	A	30	−32.393	−28.213	70.464	1.00	57.67		C
ATOM	220	NH1	ARG	A	30	−31.409	−28.969	69.985	1.00	63.98		N
ATOM	221	NH2	ARG	A	30	−32.135	−27.413	71.512	1.00	54.11		N
ATOM	222	N	TYR	A	31	−36.902	−27.434	74.789	1.00	36.60		N
ATOM	223	CA	TYR	A	31	−37.940	−28.340	75.264	1.00	40.80		C
ATOM	224	C	TYR	A	31	−38.685	−27.821	76.489	1.00	37.66		C
ATOM	225	O	TYR	A	31	−39.628	−28.470	76.946	1.00	36.93		O
ATOM	226	CB	TYR	A	31	−37.334	−29.699	75.619	1.00	37.87		C
ATOM	227	CG	TYR	A	31	−36.422	−30.240	74.573	1.00	39.45		C
ATOM	228	CD1	TYR	A	31	−36.888	−30.500	73.300	1.00	42.59		C
ATOM	229	CD2	TYR	A	31	−35.088	−30.528	74.861	1.00	44.81		C
ATOM	230	CE1	TYR	A	31	−36.047	−31.005	72.325	1.00	45.84		C
ATOM	231	CE2	TYR	A	31	−34.240	−31.049	73.890	1.00	43.49		C
ATOM	232	CZ	TYR	A	31	−34.729	−31.281	72.625	1.00	43.29		C
ATOM	233	OH	TYR	A	31	−33.922	−31.803	71.648	1.00	43.72		O
ATOM	234	N	TYR	A	32	−38.302	−26.677	77.027	1.00	39.36		N
ATOM	235	CA	TYR	A	32	−38.735	−26.280	78.350	1.00	34.43		C
ATOM	236	C	TYR	A	32	−39.587	−25.028	78.263	1.00	38.74		C
ATOM	237	O	TYR	A	32	−39.501	−24.256	77.305	1.00	39.83		O
ATOM	238	CB	TYR	A	32	−37.533	−26.028	79.265	1.00	33.39		C
ATOM	239	CG	TYR	A	32	−36.634	−27.226	79.343	1.00	38.75		C
ATOM	240	CD2	TYR	A	32	−35.377	−27.236	78.750	1.00	32.24		C
ATOM	241	CD1	TYR	A	32	−37.061	−28.368	80.004	1.00	38.64		C
ATOM	242	CE2	TYR	A	32	−34.570	−28.364	78.823	1.00	39.82		C
ATOM	243	CE1	TYR	A	32	−36.270	−29.495	80.088	1.00	40.18		C
ATOM	244	CZ	TYR	A	32	−35.029	−29.505	79.499	1.00	46.72		C
ATOM	245	OH	TYR	A	32	−34.278	−30.668	79.604	1.00	41.88		O
ATOM	246	N	TYR	A	33	−40.420	−24.842	79.282	1.00	31.10		N
ATOM	247	CA	TYR	A	33	−41.042	−23.558	79.529	1.00	30.58		C
ATOM	248	C	TYR	A	33	−40.221	−22.800	80.563	1.00	30.77		C
ATOM	249	O	TYR	A	33	−39.686	−23.392	81.507	1.00	29.88		O
ATOM	250	CB	TYR	A	33	−42.491	−23.726	79.987	1.00	30.38		C
ATOM	251	CG	TYR	A	33	−43.440	−23.801	78.834	1.00	33.35		C
ATOM	252	CD2	TYR	A	33	−44.211	−22.698	78.485	1.00	33.18		C
ATOM	253	CD1	TYR	A	33	−43.550	−24.966	78.059	1.00	33.82		C
ATOM	254	CE2	TYR	A	33	−45.080	−22.746	77.407	1.00	36.40		C
ATOM	255	CE1	TYR	A	33	−44.430	−25.030	76.976	1.00	33.85		C
ATOM	256	CZ	TYR	A	33	−45.186	−23.909	76.655	1.00	39.33		C
ATOM	257	OH	TYR	A	33	−46.051	−23.924	75.590	1.00	39.05		O
ATOM	258	N	TRP	A	34	−40.133	−21.490	80.381	1.00	25.37		N
ATOM	259	CA	TRP	A	34	−39.285	−20.639	81.189	1.00	25.30		C
ATOM	260	C	TRP	A	34	−40.172	−19.666	81.940	1.00	30.32		C
ATOM	261	O	TRP	A	34	−41.013	−18.993	81.328	1.00	28.04		O
ATOM	262	CB	TRP	A	34	−38.242	−19.932	80.310	1.00	27.04		C
ATOM	263	CG	TRP	A	34	−37.375	−20.952	79.641	1.00	28.16		C
ATOM	264	CD1	TRP	A	34	−37.436	−21.371	78.333	1.00	31.12		C
ATOM	265	CD2	TRP	A	34	−36.410	−21.787	80.279	1.00	28.13		C
ATOM	266	NE1	TRP	A	34	−36.525	−22.375	78.110	1.00	27.45		N
ATOM	267	CE2	TRP	A	34	−35.881	−22.653	79.287	1.00	31.81		C
ATOM	268	CE3	TRP	A	34	−35.920	−21.875	81.587	1.00	28.15		C
ATOM	269	CZ2	TRP	A	34	−34.880	−23.591	79.567	1.00	31.29		C
ATOM	270	CZ3	TRP	A	34	−34.911	−22.807	81.864	1.00	29.29		C
ATOM	271	CH2	TRP	A	34	−34.411	−23.654	80.858	1.00	25.81		C
ATOM	272	N	SER	A	35	−39.993	−19.608	83.268	1.00	28.16		N
ATOM	273	CA	SER	A	35	−41.009	−19.048	84.150	1.00	29.83		C
ATOM	274	C	SER	A	35	−40.463	−17.999	85.106	1.00	27.98		C
ATOM	275	O	SER	A	35	−39.266	−17.907	85.361	1.00	25.65		O
ATOM	276	CB	SER	A	35	−41.677	−20.145	84.957	1.00	25.41		C
ATOM	277	OG	SER	A	35	−42.298	−21.049	84.068	1.00	33.06		O
ATOM	278	N	TRP	A	36	−41.388	−17.224	85.655	1.00	26.15		N
ATOM	279	CA	TRP	A	36	−41.091	−16.278	86.712	1.00	23.95		C
ATOM	280	C	TRP	A	36	−42.037	−16.535	87.877	1.00	26.92		C
ATOM	281	O	TRP	A	36	−43.249	−16.680	87.693	1.00	24.36		O
ATOM	282	CB	TRP	A	36	−41.200	−14.847	86.204	1.00	21.96		C
ATOM	283	CG	TRP	A	36	−40.123	−14.545	85.243	1.00	27.15		C
ATOM	284	CD1	TRP	A	36	−40.208	−14.586	83.880	1.00	28.66		C
ATOM	285	CD2	TRP	A	36	−38.764	−14.186	85.550	1.00	30.43		C
ATOM	286	NE1	TRP	A	36	−38.998	−14.263	83.319	1.00	28.45		N
ATOM	287	CE2	TRP	A	36	−38.092	−14.011	84.318	1.00	31.09		C
ATOM	288	CE3	TRP	A	36	−38.051	−13.988	86.744	1.00	26.18		C
ATOM	289	CZ2	TRP	A	36	−36.736	−13.635	84.245	1.00	30.83		C
ATOM	290	CZ3	TRP	A	36	−36.710	−13.624	86.669	1.00	31.94		C
ATOM	291	CH2	TRP	A	36	−36.065	−13.444	85.426	1.00	27.34		C
ATOM	292	N	ILE	A	37	−41.470	−16.623	89.072	1.00	28.61		N
ATOM	293	CA	ILE	A	37	−42.220	−16.887	90.289	1.00	25.71		C
ATOM	294	C	ILE	A	37	−41.703	−15.924	91.344	1.00	26.51		C
ATOM	295	O	ILE	A	37	−40.485	−15.758	91.473	1.00	28.46		O
ATOM	296	CB	ILE	A	37	−42.043	−18.359	90.726	1.00	28.49		C
ATOM	297	CG1	ILE	A	37	−42.496	−19.298	89.602	1.00	20.22		C
ATOM	298	CG2	ILE	A	37	−42.842	−18.657	91.998	1.00	30.40		C
ATOM	299	CD1	ILE	A	37	−41.935	−20.641	89.672	1.00	19.85		C
ATOM	300	N	ARG	A	38	−42.608	−15.271	92.089	1.00	27.82		N
ATOM	301	CA	ARG	A	38	−42.178	−14.383	93.172	1.00	31.79		C
ATOM	302	C	ARG	A	38	−42.654	−14.877	94.535	1.00	29.28		C
ATOM	303	O	ARG	A	38	−43.711	−15.493	94.666	1.00	30.31		O
ATOM	304	CB	ARG	A	38	−42.642	−12.902	92.983	1.00	25.98		C
ATOM	305	CG	ARG	A	38	−44.132	−12.704	92.827	1.00	30.50		C
ATOM	306	CD	ARG	A	38	−44.718	−11.710	93.796	1.00	31.27		C
ATOM	307	NE	ARG	A	38	−44.660	−10.332	93.330	1.00	38.33		N
ATOM	308	CZ	ARG	A	38	−45.723	−9.550	93.118	1.00	40.05		C
ATOM	309	NH1	ARG	A	38	−46.967	−9.987	93.311	1.00	29.85		N1+
ATOM	310	NH2	ARG	A	38	−45.529	−8.307	92.711	1.00	35.67		N
ATOM	311	N	GLN	A	39	−41.874	−14.544	95.561	1.00	29.83		N
ATOM	312	CA	GLN	A	39	−42.189	−14.894	96.940	1.00	29.44		C
ATOM	313	C	GLN	A	39	−42.070	−13.629	97.776	1.00	30.99		C
ATOM	314	O	GLN	A	39	−40.945	−13.189	98.072	1.00	30.65		O
ATOM	315	CB	GLN	A	39	−41.278	−15.997	97.467	1.00	26.80		C
ATOM	316	CG	GLN	A	39	−41.737	−16.561	98.799	1.00	29.10		C
ATOM	317	CD	GLN	A	39	−41.020	−17.825	99.195	1.00	32.69		C
ATOM	318	OE1	GLN	A	39	−39.808	−17.945	99.051	1.00	34.15		O
ATOM	319	NE2	GLN	A	39	−41.773	−18.787	99.702	1.00	36.84		N
ATOM	320	N	PRO	A	40	−43.199	−13.006	98.142	1.00	32.88		N
ATOM	321	CA	PRO	A	40	−43.142	−11.823	99.012	1.00	32.74		C
ATOM	322	C	PRO	A	40	−42.699	−12.202	100.414	1.00	37.01		C
ATOM	323	O	PRO	A	40	−42.970	−13.320	100.883	1.00	37.15		O
ATOM	324	CB	PRO	A	40	−44.590	−11.305	99.005	1.00	28.52		C
ATOM	325	CG	PRO	A	40	−45.230	−11.963	97.786	1.00	33.90		C
ATOM	326	CD	PRO	A	40	−44.566	−13.290	97.668	1.00	32.61		C
ATOM	327	N	PRO	A	41	−42.011	−11.304	101.120	1.00	41.34		N
ATOM	328	CA	PRO	A	41	−41.405	−11.689	102.405	1.00	35.97		C
ATOM	329	C	PRO	A	41	−42.486	−12.089	103.398	1.00	39.15		C
ATOM	330	O	PRO	A	41	−43.499	−11.400	103.564	1.00	39.19		O
ATOM	331	CB	PRO	A	41	−40.643	−10.430	102.834	1.00	35.82		C
ATOM	332	CG	PRO	A	41	−41.378	−9.304	102.151	1.00	36.54		C
ATOM	333	CD	PRO	A	41	−41.862	−9.861	100.839	1.00	32.74		C
ATOM	334	N	GLY	A	42	−42.264	−13.220	104.057	1.00	39.49		N
ATOM	335	CA	GLY	A	42	−43.319	−13.884	104.786	1.00	43.62		C
ATOM	336	C	GLY	A	42	−44.017	−14.964	103.996	1.00	43.06		C
ATOM	337	O	GLY	A	42	−45.137	−15.343	104.347	1.00	44.55		O
ATOM	338	N	LYS	A	43	−43.392	−15.449	102.924	1.00	49.76		N
ATOM	339	CA	LYS	A	43	−43.711	−16.719	102.276	1.00	46.50		C
ATOM	340	C	LYS	A	43	−44.975	−16.606	101.432	1.00	41.59		C
ATOM	341	O	LYS	A	43	−45.732	−15.629	101.536	1.00	39.86		O
ATOM	342	CB	LYS	A	43	−43.844	−17.858	103.320	1.00	55.91		C
ATOM	343	CG	LYS	A	43	−42.513	−18.447	103.914	1.00	45.31		C
ATOM	344	CD	LYS	A	43	−41.860	−19.485	102.968	1.00	46.63		C
ATOM	345	CE	LYS	A	43	−41.212	−20.692	103.684	1.00	40.96		C
ATOM	346	NZ	LYS	A	43	−39.846	−20.507	104.327	1.00	38.05		N
ATOM	347	N	GLY	A	44	−45.192	−17.625	100.601	1.00	39.58		N
ATOM	348	CA	GLY	A	44	−46.241	−17.682	99.609	1.00	36.71		C
ATOM	349	C	GLY	A	44	−45.620	−17.601	98.231	1.00	37.64		C
ATOM	350	O	GLY	A	44	−44.862	−16.666	97.961	1.00	40.33		O
ATOM	351	N	LEU	A	45	−45.870	−18.568	97.359	1.00	32.84		N
ATOM	352	CA	LEU	A	45	−45.302	−18.533	96.019	1.00	31.46		C
ATOM	353	C	LEU	A	45	−46.409	−18.152	95.047	1.00	32.57		C
ATOM	354	O	LEU	A	45	−47.476	−18.773	95.054	1.00	37.03		O
ATOM	355	CB	LEU	A	45	−44.665	−19.877	95.649	1.00	29.61		C
ATOM	356	CG	LEU	A	45	−43.412	−20.297	96.434	1.00	28.20		C
ATOM	357	CD1	LEU	A	45	−43.088	−21.788	96.284	1.00	22.57		C
ATOM	358	CD2	LEU	A	45	−42.235	−19.474	95.976	1.00	25.94		C
ATOM	359	N	GLU	A	46	−46.150	−17.152	94.201	1.00	27.39		N
ATOM	360	CA	GLU	A	46	−47.092	−16.747	93.168	1.00	31.51		C
ATOM	361	C	GLU	A	46	−46.444	−16.851	91.798	1.00	35.34		C
ATOM	362	O	GLU	A	46	−45.360	−16.303	91.565	1.00	32.92		O
ATOM	363	CB	GLU	A	46	−47.602	−15.323	93.347	1.00	29.82		C
ATOM	364	CG	GLU	A	46	−47.130	−14.572	94.552	1.00	39.23		C
ATOM	365	CD	GLU	A	46	−47.805	−13.180	94.638	1.00	55.69		C
ATOM	366	OE1	GLU	A	46	−48.162	−12.613	93.554	1.00	51.35		O
ATOM	367	OE2	GLU	A	46	−48.001	−12.680	95.784	1.00	52.13		O1−
ATOM	368	N	TRP	A	47	−47.137	−17.524	90.893	1.00	29.44		N
ATOM	369	CA	TRP	A	47	−46.647	−17.778	89.551	1.00	30.35		C
ATOM	370	C	TRP	A	47	−46.982	−16.605	88.644	1.00	32.75		C
ATOM	371	O	TRP	A	47	−48.143	−16.202	88.550	1.00	36.68		O
ATOM	372	CB	TRP	A	47	−47.265	−19.068	89.037	1.00	24.36		C
ATOM	373	CG	TRP	A	47	−46.961	−19.432	87.637	1.00	29.61		C
ATOM	374	CD1	TRP	A	47	−45.883	−20.133	87.188	1.00	25.71		C
ATOM	375	CD2	TRP	A	47	−47.784	−19.186	86.495	1.00	28.45		C
ATOM	376	NE1	TRP	A	47	−45.979	−20.319	85.840	1.00	26.95		N
ATOM	377	CE2	TRP	A	47	−47.136	−19.748	85.388	1.00	25.32		C
ATOM	378	CE3	TRP	A	47	−49.001	−18.540	86.303	1.00	25.64		C
ATOM	379	CZ2	TRP	A	47	−47.662	−19.687	84.112	1.00	26.63		C
ATOM	380	CZ3	TRP	A	47	−49.517	−18.479	85.032	1.00	29.15		C
ATOM	381	CH2	TRP	A	47	−48.853	−19.054	83.953	1.00	27.51		C
ATOM	382	N	PHE	A	48	−45.966	−16.059	87.975	1.00	33.76		N
ATOM	383	CA	PHE	A	48	−46.182	−14.896	87.119	1.00	32.37		C
ATOM	384	C	PHE	A	48	−46.601	−15.253	85.708	1.00	32.57		C
ATOM	385	O	PHE	A	48	−47.502	−14.615	85.160	1.00	39.41		O
ATOM	386	CB	PHE	A	48	−44.925	−14.027	87.073	1.00	31.35		C
ATOM	387	CG	PHE	A	48	−44.998	−12.843	87.979	1.00	30.88		C
ATOM	388	CD2	PHE	A	48	−44.484	−11.622	87.593	1.00	32.09		C
ATOM	389	CD1	PHE	A	48	−45.606	−12.952	89.221	1.00	31.12		C
ATOM	390	CE2	PHE	A	48	−44.562	−10.519	88.440	1.00	34.85		C
ATOM	391	CE1	PHE	A	48	−45.695	−11.855	90.073	1.00	34.60		C
ATOM	392	CZ	PHE	A	48	−45.165	−10.639	89.683	1.00	36.89		C
ATOM	393	N	GLY	A	49	−45.982	−16.255	85.111	1.00	31.20		N
ATOM	394	CA	GLY	A	49	−46.195	−16.531	83.707	1.00	30.09		C
ATOM	395	C	GLY	A	49	−45.089	−17.418	83.178	1.00	31.55		C
ATOM	396	O	GLY	A	49	−44.201	−17.849	83.913	1.00	31.30		O
ATOM	397	N	GLU	A	50	−45.176	−17.704	81.881	1.00	28.58		N
ATOM	398	CA	GLU	A	50	−44.233	−18.608	81.247	1.00	27.28		C
ATOM	399	C	GLU	A	50	−44.118	−18.247	79.773	1.00	31.68		C
ATOM	400	O	GLU	A	50	−45.015	−17.630	79.199	1.00	32.98		O
ATOM	401	CB	GLU	A	50	−44.669	−20.060	81.434	1.00	26.85		C
ATOM	402	CG	GLU	A	50	−46.040	−20.348	80.874	1.00	29.78		C
ATOM	403	CD	GLU	A	50	−46.438	−21.812	81.020	1.00	35.37		C
ATOM	404	OE1	GLU	A	50	−47.350	−22.259	80.271	1.00	37.88		O
ATOM	405	OE2	GLU	A	50	−45.834	−22.514	81.875	1.00	28.88		O
ATOM	406	N	ILE	A	51	−42.989	−18.610	79.165	1.00	32.55		N
ATOM	407	CA	ILE	A	51	−42.790	−18.425	77.735	1.00	28.12		C
ATOM	408	C	ILE	A	51	−42.187	−19.702	77.167	1.00	34.07		C
ATOM	409	O	ILE	A	51	−41.470	−20.426	77.867	1.00	29.86		O
ATOM	410	CB	ILE	A	51	−41.917	−17.191	77.464	1.00	29.20		C
ATOM	411	CG1	ILE	A	51	−41.860	−16.866	75.954	1.00	32.21		C
ATOM	412	CG2	ILE	A	51	−40.574	−17.350	78.147	1.00	26.55		C
ATOM	413	CD1	ILE	A	51	−41.585	−15.399	75.639	1.00	26.20		C
ATOM	414	N	SER	A	52	−42.453	−19.969	75.876	1.00	37.40		N
ATOM	415	CA	SER	A	52	−42.398	−21.343	75.378	1.00	41.14		C
ATOM	416	C	SER	A	52	−41.162	−21.701	74.563	1.00	43.60		C
ATOM	417	O	SER	A	52	−40.851	−22.904	74.473	1.00	56.16		O
ATOM	418	CB	SER	A	52	−43.624	−21.655	74.508	1.00	44.90		C
ATOM	419	OG	SER	A	52	−43.499	−21.091	73.211	1.00	42.47		O
ATOM	420	N	HIS	A	53	−40.465	−20.709	73.992	1.00	38.93		N
ATOM	421	CA	HIS	A	53	−39.361	−20.843	73.025	1.00	46.69		C
ATOM	422	C	HIS	A	53	−39.838	−20.322	71.682	1.00	40.68		C
ATOM	423	O	HIS	A	53	−39.045	−19.789	70.908	1.00	48.98		O
ATOM	424	CB	HIS	A	53	−38.827	−22.278	72.833	1.00	47.29		C
ATOM	425	CG	HIS	A	53	−37.623	−22.370	71.938	1.00	50.45		C
ATOM	426	ND1	HIS	A	53	−36.332	−22.400	72.429	1.00	48.68		N
ATOM	427	CD2	HIS	A	53	−37.510	−22.432	70.589	1.00	50.73		C
ATOM	428	CE1	HIS	A	53	−35.477	−22.464	71.421	1.00	44.63		C
ATOM	429	NE2	HIS	A	53	−36.166	−22.483	70.294	1.00	45.11		N
ATOM	430	N	SER	A	54	−41.136	−20.418	71.427	1.00	43.19		N
ATOM	431	CA	SER	A	54	−41.723	−19.986	70.163	1.00	37.71		C
ATOM	432	C	SER	A	54	−41.978	−18.486	69.934	1.00	41.91		C
ATOM	433	O	SER	A	54	−42.167	−18.132	68.783	1.00	58.83		O
ATOM	434	CB	SER	A	54	−43.072	−20.685	69.930	1.00	41.65		C
ATOM	435	OG	SER	A	54	−43.284	−21.786	70.799	1.00	58.13		O
ATOM	436	N	GLY	A	55	−42.077	−17.595	70.928	1.00	41.19		N
ATOM	437	CA	GLY	A	55	−42.199	−17.864	72.342	1.00	37.12		C
ATOM	438	C	GLY	A	55	−43.565	−17.363	72.782	1.00	38.09		C
ATOM	439	O	GLY	A	55	−43.782	−16.170	73.025	1.00	35.63		O
ATOM	440	N	SER	A	56	−44.514	−18.290	72.843	1.00	35.38		N
ATOM	441	CA	SER	A	56	−45.839	−17.960	73.328	1.00	36.92		C
ATOM	442	C	SER	A	56	−45.838	−17.864	74.851	1.00	39.87		C
ATOM	443	O	SER	A	56	−45.057	−18.536	75.536	1.00	38.19		O
ATOM	444	CB	SER	A	56	−46.855	−19.002	72.851	1.00	43.51		C
ATOM	445	OG	SER	A	56	−46.477	−20.320	73.214	1.00	52.12		O
ATOM	446	N	THR	A	57	−46.745	−17.035	75.381	1.00	36.78		N
ATOM	447	CA	THR	A	57	−46.758	−16.688	76.792	1.00	35.49		C
ATOM	448	C	THR	A	57	−48.106	−17.037	77.412	1.00	36.54		C
ATOM	449	O	THR	A	57	−49.129	−17.068	76.738	1.00	36.43		O
ATOM	450	CB	THR	A	57	−46.464	−15.195	77.048	1.00	34.28		C
ATOM	451	OG1	THR	A	57	−47.488	−14.390	76.463	1.00	34.38		O
ATOM	452	CG2	THR	A	57	−45.110	−14.791	76.511	1.00	32.77		C
ATOM	453	N	ASN	A	58	−48.081	−17.324	78.707	1.00	34.99		N
ATOM	454	CA	ASN	A	58	−49.282	−17.540	79.497	1.00	35.60		C
ATOM	455	C	ASN	A	58	−49.013	−16.847	80.812	1.00	38.61		C
ATOM	456	O	ASN	A	58	−48.117	−17.271	81.548	1.00	38.39		O
ATOM	457	CB	ASN	A	58	−49.562	−19.013	79.731	1.00	33.14		C
ATOM	458	CG	ASN	A	58	−49.588	−19.785	78.459	1.00	38.06		C
ATOM	459	OD1	ASN	A	58	−50.518	−19.669	77.673	1.00	42.44		O
ATOM	460	ND2	ASN	A	58	−48.555	−20.583	78.234	1.00	37.72		N
ATOM	461	N	TYR	A	59	−49.778	−15.800	81.101	1.00	35.54		N
ATOM	462	CA	TYR	A	59	−49.557	−14.988	82.281	1.00	36.21		C
ATOM	463	C	TYR	A	59	−50.617	−15.291	83.325	1.00	34.45		C
ATOM	464	O	TYR	A	59	−51.674	−15.857	83.041	1.00	36.30		O
ATOM	465	CB	TYR	A	59	−49.603	−13.498	81.943	1.00	35.28		C
ATOM	466	CG	TYR	A	59	−48.633	−13.043	80.880	1.00	35.74		C
ATOM	467	CD1	TYR	A	59	−47.259	−13.085	81.082	1.00	34.19		C
ATOM	468	CD2	TYR	A	59	−49.101	−12.544	79.678	1.00	35.17		C
ATOM	469	CE1	TYR	A	59	−46.383	−12.644	80.107	1.00	33.92		C
ATOM	470	CE2	TYR	A	59	−48.241	−12.098	78.700	1.00	31.35		C
ATOM	471	CZ	TYR	A	59	−46.888	−12.143	78.912	1.00	37.17		C
ATOM	472	OH	TYR	A	59	−46.055	−11.690	77.915	1.00	33.15		O
ATOM	473	N	ASN	A	60	−50.335	−14.882	84.531	1.00	37.70		N
ATOM	474	CA	ASN	A	60	−51.356	−14.909	85.549	1.00	38.74		C
ATOM	475	C	ASN	A	60	−52.356	−13.791	85.274	1.00	42.68		C
ATOM	476	O	ASN	A	60	−51.962	−12.615	85.220	1.00	41.91		O
ATOM	477	CB	ASN	A	60	−50.706	−14.771	86.911	1.00	35.36		C
ATOM	478	CG	ASN	A	60	−51.663	−15.019	88.031	1.00	37.89		C
ATOM	479	OD1	ASN	A	60	−52.874	−14.862	87.873	1.00	38.66		O
ATOM	480	ND2	ASN	A	60	−51.142	−15.541	89.137	1.00	36.71		N
ATOM	481	N	PRO	A	61	−53.642	−14.102	85.084	1.00	43.65		N
ATOM	482	CA	PRO	A	61	−54.609	−13.045	84.741	1.00	37.57		C
ATOM	483	C	PRO	A	61	−54.670	−11.924	85.762	1.00	40.30		C
ATOM	484	O	PRO	A	61	−54.997	−10.786	85.405	1.00	42.33		O
ATOM	485	CB	PRO	A	61	−55.931	−13.820	84.677	1.00	32.38		C
ATOM	486	CG	PRO	A	61	−55.502	−15.207	84.249	1.00	39.32		C
ATOM	487	CD	PRO	A	61	−54.273	−15.439	85.092	1.00	39.25		C
ATOM	488	N	SER	A	62	−54.321	−12.218	87.016	1.00	40.22		N
ATOM	489	CA	SER	A	62	−54.367	−11.233	88.092	1.00	39.59		C
ATOM	490	C	SER	A	62	−53.386	−10.087	87.868	1.00	45.31		C
ATOM	491	O	SER	A	62	−53.617	−8.957	88.319	1.00	43.39		O
ATOM	492	CB	SER	A	62	−54.058	−11.920	89.419	1.00	40.43		C
ATOM	493	OG	SER	A	62	−53.155	−11.129	90.177	1.00	48.57		O
ATOM	494	N	LEU	A	63	−52.237	−10.383	87.272	1.00	45.35		N
ATOM	495	CA	LEU	A	63	−51.297	−9.329	86.930	1.00	44.69		C
ATOM	496	C	LEU	A	63	−51.894	−8.416	85.869	1.00	53.96		C
ATOM	497	O	LEU	A	63	−51.658	−7.201	85.861	1.00	54.71		O
ATOM	498	CB	LEU	A	63	−50.001	−9.971	86.440	1.00	43.57		C
ATOM	499	CG	LEU	A	63	−49.158	−10.633	87.535	1.00	43.51		C
ATOM	500	CD1	LEU	A	63	−47.844	−11.134	86.978	1.00	40.31		C
ATOM	501	CD2	LEU	A	63	−48.888	−9.663	88.691	1.00	43.97		C
ATOM	502	N	LYS	A	64	−52.663	−9.003	84.955	1.00	58.46		N
ATOM	503	CA	LYS	A	64	−53.324	−8.320	83.854	1.00	58.94		C
ATOM	504	C	LYS	A	64	−52.277	−7.745	82.912	1.00	51.96		C
ATOM	505	O	LYS	A	64	−51.377	−8.460	82.452	1.00	48.34		O
ATOM	506	CB	LYS	A	64	−54.274	−7.204	84.304	1.00	52.16		C
ATOM	507	CG	LYS	A	64	−55.571	−7.258	83.486	1.00	62.77		C
ATOM	508	CD	LYS	A	64	−56.400	−5.965	83.488	1.00	81.85		C
ATOM	509	CE	LYS	A	64	−57.048	−5.593	84.810	1.00	81.71		C
ATOM	510	NZ	LYS	A	64	−57.659	−4.226	84.694	1.00	73.63		N
ATOM	511	N	ALA	A	65	−52.386	−6.444	82.659	1.00	41.71		N
ATOM	512	CA	ALA	A	65	−51.539	−5.768	81.693	1.00	43.20		C
ATOM	513	C	ALA	A	65	−50.168	−5.367	82.231	1.00	38.62		C
ATOM	514	O	ALA	A	65	−49.389	−4.808	81.463	1.00	42.39		O
ATOM	515	CB	ALA	A	65	−52.249	−4.540	81.128	1.00	46.41		C
ATOM	516	N	ARG	A	66	−49.867	−5.542	83.523	1.00	38.64		N
ATOM	517	CA	ARG	A	66	−48.595	−5.016	84.025	1.00	34.40		C
ATOM	518	C	ARG	A	66	−47.377	−5.847	83.627	1.00	36.18		C
ATOM	519	O	ARG	A	66	−46.249	−5.349	83.752	1.00	31.12		O
ATOM	520	CB	ARG	A	66	−48.586	−4.863	85.546	1.00	33.68		C
ATOM	521	CG	ARG	A	66	−49.764	−4.132	86.091	1.00	40.09		C
ATOM	522	CD	ARG	A	66	−49.537	−3.649	87.519	1.00	40.22		C
ATOM	523	NE	ARG	A	66	−49.265	−4.663	88.539	1.00	35.47		N
ATOM	524	CZ	ARG	A	66	−48.148	−4.713	89.268	1.00	34.74		C
ATOM	525	NH1	ARG	A	66	−47.168	−3.842	89.065	1.00	33.41		N1+
ATOM	526	NH2	ARG	A	66	−48.004	−5.640	90.205	1.00	40.56		N
ATOM	527	N	VAL	A	67	−47.559	−7.095	83.188	1.00	34.62		N
ATOM	528	CA	VAL	A	67	−46.463	−8.049	83.084	1.00	36.24		C
ATOM	529	C	VAL	A	67	−46.186	−8.411	81.626	1.00	36.09		C
ATOM	530	O	VAL	A	67	−47.113	−8.575	80.828	1.00	36.24		O
ATOM	531	CB	VAL	A	67	−46.782	−9.292	83.935	1.00	34.93		C
ATOM	532	CG1	VAL	A	67	−47.992	−9.994	83.388	1.00	41.56		C
ATOM	533	CG2	VAL	A	67	−45.596	−10.222	83.981	1.00	36.82		C
ATOM	534	N	THR	A	68	−44.894	−8.531	81.289	1.00	35.40		N
ATOM	535	CA	THR	A	68	−44.405	−8.998	79.998	1.00	33.94		C
ATOM	536	C	THR	A	68	−43.267	−9.973	80.231	1.00	33.46		C
ATOM	537	O	THR	A	68	−42.412	−9.739	81.087	1.00	34.05		O
ATOM	538	CB	THR	A	68	−43.854	−7.882	79.090	1.00	37.93		C
ATOM	539	OG1	THR	A	68	−44.745	−6.763	79.052	1.00	38.69		O
ATOM	540	CG2	THR	A	68	−43.621	−8.423	77.672	1.00	27.13		C
ATOM	541	N	ILE	A	69	−43.262	−11.064	79.471	1.00	35.17		N
ATOM	542	CA	ILE	A	69	−42.163	−12.021	79.455	1.00	31.25		C
ATOM	543	C	ILE	A	69	−41.710	−12.169	78.008	1.00	37.24		C
ATOM	544	O	ILE	A	69	−42.541	−12.313	77.103	1.00	33.89		O
ATOM	545	CB	ILE	A	69	−42.574	−13.382	80.051	1.00	27.84		C
ATOM	546	CG1	ILE	A	69	−42.912	−13.212	81.523	1.00	31.71		C
ATOM	547	CG2	ILE	A	69	−41.468	−14.407	79.896	1.00	25.74		C
ATOM	548	CD1	ILE	A	69	−43.605	−14.385	82.110	1.00	30.41		C
ATOM	549	N	SER	A	70	−40.401	−12.101	77.789	1.00	32.26		N
ATOM	550	CA	SER	A	70	−39.826	−12.197	76.460	1.00	29.37		C
ATOM	551	C	SER	A	70	−38.678	−13.195	76.500	1.00	33.52		C
ATOM	552	O	SER	A	70	−38.103	−13.470	77.557	1.00	32.58		O
ATOM	553	CB	SER	A	70	−39.322	−10.841	75.963	1.00	30.41		C
ATOM	554	OG	SER	A	70	−38.395	−10.282	76.888	1.00	41.93		O
ATOM	555	N	ILE	A	71	−38.333	−13.724	75.331	1.00	30.14		N
ATOM	556	CA	ILE	A	71	−37.327	−14.761	75.222	1.00	29.53		C
ATOM	557	C	ILE	A	71	−36.358	−14.414	74.097	1.00	34.98		C
ATOM	558	O	ILE	A	71	−36.762	−13.926	73.035	1.00	33.60		O
ATOM	559	CB	ILE	A	71	−37.992	−16.132	75.000	1.00	29.32		C
ATOM	560	CG1	ILE	A	71	−37.001	−17.267	75.279	1.00	29.60		C
ATOM	561	CG2	ILE	A	71	−38.575	−16.224	73.606	1.00	30.62		C
ATOM	562	CD1	ILE	A	71	−37.644	−18.637	75.331	1.00	29.78		C
ATOM	563	N	ASP	A	72	−35.076	−14.658	74.339	1.00	33.23		N
ATOM	564	CA	ASP	A	72	−34.016	−14.453	73.355	1.00	32.69		C
ATOM	565	C	ASP	A	72	−33.394	−15.828	73.138	1.00	36.12		C
ATOM	566	O	ASP	A	72	−32.525	−16.242	73.910	1.00	37.95		O
ATOM	567	CB	ASP	A	72	−33.008	−13.415	73.862	1.00	31.36		C
ATOM	568	CG	ASP	A	72	−31.876	−13.113	72.861	1.00	47.78		C
ATOM	569	OD2	ASP	A	72	−31.214	−12.051	73.040	1.00	43.89		O
ATOM	570	OD1	ASP	A	72	−31.629	−13.924	71.921	1.00	48.56		O
ATOM	571	N	THR	A	73	−33.847	−16.547	72.100	1.00	39.39		N
ATOM	572	CA	THR	A	73	−33.375	−17.916	71.888	1.00	36.77		C
ATOM	573	C	THR	A	73	−31.919	−17.989	71.429	1.00	43.07		C
ATOM	574	O	THR	A	73	−31.301	−19.055	71.535	1.00	46.66		O
ATOM	575	CB	THR	A	73	−34.251	−18.621	70.868	1.00	36.60		C
ATOM	576	OG1	THR	A	73	−34.346	−17.803	69.699	1.00	47.78		O
ATOM	577	CG2	THR	A	73	−35.625	−18.860	71.428	1.00	33.19		C
ATOM	578	N	SER	A	74	−31.349	−16.886	70.949	1.00	40.76		N
ATOM	579	CA	SER	A	74	−29.949	−16.891	70.549	1.00	43.57		C
ATOM	580	C	SER	A	74	−29.032	−16.974	71.758	1.00	50.46		C
ATOM	581	O	SER	A	74	−28.083	−17.779	71.784	1.00	52.51		O
ATOM	582	CB	SER	A	74	−29.654	−15.639	69.744	1.00	48.36		C
ATOM	583	OG	SER	A	74	−30.524	−15.613	68.635	1.00	60.90		O
ATOM	584	O	LYS	A	75	−28.334	−16.929	76.160	1.00	39.85		O
ATOM	585	N	LYS	A	75	−29.291	−16.123	72.754	1.00	40.62		N
ATOM	586	CA	LYS	A	75	−28.494	−15.995	73.967	1.00	44.56		C
ATOM	587	C	LYS	A	75	−28.929	−16.951	75.076	1.00	39.19		C
ATOM	588	CB	LYS	A	75	−28.574	−14.552	74.490	1.00	42.65		C
ATOM	589	CG	LYS	A	75	−28.087	−13.508	73.502	1.00	48.05		C
ATOM	590	CD	LYS	A	75	−28.250	−12.099	74.045	1.00	49.13		C
ATOM	591	CE	LYS	A	75	−28.043	−11.079	72.924	1.00	55.25		C
ATOM	592	NZ	LYS	A	75	−27.500	−9.765	73.364	1.00	55.09		N
ATOM	593	N	ASN	A	76	−29.936	−17.793	74.823	1.00	43.17		N
ATOM	594	CA	ASN	A	76	−30.578	−18.625	75.845	1.00	36.87		C
ATOM	595	C	ASN	A	76	−30.949	−17.780	77.073	1.00	35.94		C
ATOM	596	O	ASN	A	76	−30.668	−18.130	78.221	1.00	33.33		O
ATOM	597	CB	ASN	A	76	−29.696	−19.823	76.213	1.00	32.65		C
ATOM	598	CG	ASN	A	76	−29.729	−20.940	75.144	1.00	41.58		C
ATOM	599	OD1	ASN	A	76	−30.207	−20.738	74.016	1.00	42.66		O
ATOM	600	ND2	ASN	A	76	−29.215	−22.117	75.500	1.00	36.55		N
ATOM	601	N	GLN	A	77	−31.635	−16.668	76.813	1.00	29.24		N
ATOM	602	CA	GLN	A	77	−32.064	−15.729	77.828	1.00	28.20		C
ATOM	603	C	GLN	A	77	−33.578	−15.515	77.767	1.00	32.38		C
ATOM	604	O	GLN	A	77	−34.233	−15.760	76.747	1.00	32.97		O
ATOM	605	CB	GLN	A	77	−31.365	−14.391	77.668	1.00	31.15		C
ATOM	606	CG	GLN	A	77	−29.894	−14.376	78.032	1.00	35.97		C
ATOM	607	CD	GLN	A	77	−29.313	−12.956	77.951	1.00	39.65		C
ATOM	608	OE1	GLN	A	77	−29.979	−12.017	77.502	1.00	40.22		O
ATOM	609	NE2	GLN	A	77	−28.096	−12.792	78.433	1.00	41.23		N
ATOM	610	N	PHE	A	78	−34.148	−15.096	78.891	1.00	24.83		N
ATOM	611	CA	PHE	A	78	−35.544	−14.682	78.904	1.00	30.44		C
ATOM	612	C	PHE	A	78	−35.711	−13.657	80.014	1.00	28.14		C
ATOM	613	O	PHE	A	78	−34.863	−13.544	80.899	1.00	29.63		O
ATOM	614	CB	PHE	A	78	−36.519	−15.877	79.038	1.00	27.85		C
ATOM	615	CG	PHE	A	78	−36.399	−16.648	80.334	1.00	29.82		C
ATOM	616	CD1	PHE	A	78	−35.434	−17.641	80.482	1.00	28.03		C
ATOM	617	CD2	PHE	A	78	−37.290	−16.414	81.385	1.00	27.75		C
ATOM	618	CE1	PHE	A	78	−35.334	−18.366	81.658	1.00	28.84		C
ATOM	619	CE2	PHE	A	78	−37.201	−17.127	82.571	1.00	29.25		C
ATOM	620	CZ	PHE	A	78	−36.224	−18.108	82.713	1.00	31.58		C
ATOM	621	N	SER	A	79	−36.779	−12.866	79.933	1.00	27.98		N
ATOM	622	CA	SER	A	79	−36.845	−11.640	80.717	1.00	29.89		C
ATOM	623	C	SER	A	79	−38.230	−11.432	81.299	1.00	27.88		C
ATOM	624	O	SER	A	79	−39.225	−11.992	80.827	1.00	27.43		O
ATOM	625	CB	SER	A	79	−36.437	−10.410	79.881	1.00	27.31		C
ATOM	626	OG	SER	A	79	−35.076	−10.523	79.495	1.00	33.81		O
ATOM	627	N	LEU	A	80	−38.270	−10.585	82.327	1.00	24.79		N
ATOM	628	CA	LEU	A	80	−39.503	−10.224	82.998	1.00	25.66		C
ATOM	629	C	LEU	A	80	−39.605	−8.711	83.069	1.00	30.62		C
ATOM	630	O	LEU	A	80	−38.669	−8.045	83.525	1.00	32.93		O
ATOM	631	CB	LEU	A	80	−39.563	−10.806	84.409	1.00	30.64		C
ATOM	632	CG	LEU	A	80	−40.803	−10.348	85.179	1.00	29.58		C
ATOM	633	CD2	LEU	A	80	−40.702	−10.668	86.648	1.00	29.00		C
ATOM	634	CD1	LEU	A	80	−42.002	−11.007	84.558	1.00	27.41		C
ATOM	635	N	LYS	A	81	−40.750	−8.174	82.655	1.00	30.10		N
ATOM	636	CA	LYS	A	81	−41.086	−6.769	82.845	1.00	30.96		C
ATOM	637	C	LYS	A	81	−42.340	−6.677	83.705	1.00	30.22		C
ATOM	638	O	LYS	A	81	−43.320	−7.382	83.453	1.00	32.80		O
ATOM	639	CB	LYS	A	81	−41.299	−6.065	81.499	1.00	30.39		C
ATOM	640	CG	LYS	A	81	−40.033	−5.832	80.708	1.00	30.35		C
ATOM	641	CD	LYS	A	81	−39.381	−4.518	81.077	1.00	41.11		C
ATOM	642	CE	LYS	A	81	−38.053	−4.352	80.368	1.00	43.35		C
ATOM	643	NZ	LYS	A	81	−38.187	−4.617	78.920	1.00	51.59		N
ATOM	644	N	LEU	A	82	−42.298	−5.837	84.739	1.00	30.39		N
ATOM	645	CA	LEU	A	82	−43.450	−5.573	85.601	1.00	29.80		C
ATOM	646	C	LEU	A	82	−43.573	−4.071	85.755	1.00	32.85		C
ATOM	647	O	LEU	A	82	−42.697	−3.440	86.352	1.00	31.95		O
ATOM	648	CB	LEU	A	82	−43.304	−6.239	86.968	1.00	32.00		C
ATOM	649	CG	LEU	A	82	−44.442	−6.002	87.959	1.00	32.12		C
ATOM	650	CD1	LEU	A	82	−45.711	−6.714	87.526	1.00	26.83		C
ATOM	651	CD2	LEU	A	82	−44.016	−6.435	89.349	1.00	28.77		C
ATOM	652	N	ARG	A	83	−44.645	−3.505	85.209	1.00	35.72		N
ATOM	653	CA	ARG	A	83	−44.790	−2.062	85.113	1.00	33.38		C
ATOM	654	C	ARG	A	83	−45.506	−1.514	86.344	1.00	34.77		C
ATOM	655	O	ARG	A	83	−46.221	−2.234	87.051	1.00	37.08		O
ATOM	656	CB	ARG	A	83	−45.556	−1.686	83.838	1.00	30.94		C
ATOM	657	CG	ARG	A	83	−44.709	−1.827	82.572	1.00	31.53		C
ATOM	658	CD	ARG	A	83	−45.526	−1.799	81.301	1.00	34.78		C
ATOM	659	NE	ARG	A	83	−46.273	−3.036	81.049	1.00	36.35		N
ATOM	660	CZ	ARG	A	83	−45.806	−4.149	80.484	1.00	32.43		C
ATOM	661	NH1	ARG	A	83	−46.625	−5.178	80.327	1.00	35.09		N
ATOM	662	NH2	ARG	A	83	−44.550	−4.257	80.084	1.00	29.31		N
ATOM	663	N	SER	A	84	−45.335	−0.214	86.571	1.00	37.19		N
ATOM	664	CA	SER	A	84	−46.105	0.534	87.573	1.00	35.36		C
ATOM	665	C	SER	A	84	−46.068	−0.152	88.936	1.00	39.37		C
ATOM	666	O	SER	A	84	−47.092	−0.470	89.546	1.00	39.10		O
ATOM	667	CB	SER	A	84	−47.548	0.713	87.111	1.00	33.54		C
ATOM	668	OG	SER	A	84	−47.598	1.374	85.864	1.00	48.40		O
ATOM	669	N	VAL	A	85	−44.868	−0.296	89.432	1.00	35.87		N
ATOM	670	CA	VAL	A	85	−44.588	−1.159	90.568	1.00	36.45		C
ATOM	671	C	VAL	A	85	−44.889	−0.417	91.872	1.00	34.18		C
ATOM	672	O	VAL	A	85	−44.767	0.807	91.943	1.00	36.97		O
ATOM	673	CB	VAL	A	85	−43.117	−1.606	90.424	1.00	35.38		C
ATOM	674	CG1	VAL	A	85	−42.214	−0.855	91.349	1.00	36.25		C
ATOM	675	CG2	VAL	A	85	−42.981	−3.082	90.543	1.00	34.41		C
ATOM	676	N	THR	A	86	−45.346	−1.130	92.907	1.00	36.49		N
ATOM	677	CA	THR	A	86	−45.612	−0.502	94.212	1.00	32.44		C
ATOM	678	C	THR	A	86	−44.908	−1.279	95.326	1.00	33.48		C
ATOM	679	O	THR	A	86	−44.209	−2.271	95.087	1.00	34.30		O
ATOM	680	CB	THR	A	86	−47.107	−0.413	94.556	1.00	32.14		C
ATOM	681	OG1	THR	A	86	−47.526	−1.616	95.204	1.00	36.59		O
ATOM	682	CG2	THR	A	86	−47.956	−0.200	93.321	1.00	27.41		C
ATOM	683	N	ALA	A	87	−45.082	−0.810	96.565	1.00	35.31		N
ATOM	684	CA	ALA	A	87	−44.442	−1.484	97.698	1.00	33.73		C
ATOM	685	C	ALA	A	87	−44.927	−2.921	97.822	1.00	31.88		C
ATOM	686	O	ALA	A	87	−44.184	−3.798	98.273	1.00	31.04		O
ATOM	687	CB	ALA	A	87	−44.701	−0.719	98.996	1.00	25.59		C
ATOM	688	N	ALA	A	88	−46.161	−3.186	97.408	1.00	30.13		N
ATOM	689	CA	ALA	A	88	−46.689	−4.537	97.438	1.00	27.33		C
ATOM	690	C	ALA	A	88	−45.962	−5.482	96.487	1.00	29.67		C
ATOM	691	O	ALA	A	88	−46.226	−6.681	96.532	1.00	32.42		O
ATOM	692	CB	ALA	A	88	−48.185	−4.510	97.113	1.00	20.61		C
ATOM	693	N	ASP	A	89	−45.073	−4.987	95.628	1.00	29.86		N
ATOM	694	CA	ASP	A	89	−44.275	−5.840	94.756	1.00	27.31		C
ATOM	695	C	ASP	A	89	−42.892	−6.166	95.332	1.00	29.16		C
ATOM	696	O	ASP	A	89	−42.057	−6.737	94.618	1.00	28.53		O
ATOM	697	CB	ASP	A	89	−44.141	−5.200	93.359	1.00	31.57		C
ATOM	698	CG	ASP	A	89	−45.504	−4.988	92.660	1.00	35.37		C
ATOM	699	OD1	ASP	A	89	−46.204	−5.990	92.421	1.00	36.17		O
ATOM	700	OD2	ASP	A	89	−45.880	−3.830	92.332	1.00	34.69		O1−
ATOM	701	N	THR	A	90	−42.616	−5.798	96.590	1.00	31.96		N
ATOM	702	CA	THR	A	90	−41.400	−6.246	97.270	1.00	27.24		C
ATOM	703	C	THR	A	90	−41.440	−7.754	97.476	1.00	25.30		C
ATOM	704	O	THR	A	90	−42.379	−8.277	98.074	1.00	30.54		O
ATOM	705	CB	THR	A	90	−41.237	−5.541	98.604	1.00	25.80		C
ATOM	706	OG1	THR	A	90	−40.966	−4.159	98.369	1.00	34.42		O
ATOM	707	CG2	THR	A	90	−40.111	−6.162	99.391	1.00	23.83		C
ATOM	708	N	ALA	A	91	−40.460	−8.455	96.928	1.00	26.62		N
ATOM	709	CA	ALA	A	91	−40.455	−9.906	96.947	1.00	26.31		C
ATOM	710	C	ALA	A	91	−39.136	−10.402	96.385	1.00	31.03		C
ATOM	711	O	ALA	A	91	−38.386	−9.658	95.738	1.00	27.14		O
ATOM	712	CB	ALA	A	91	−41.605	−10.497	96.134	1.00	25.43		C
ATOM	713	N	VAL	A	92	−38.876	−11.680	96.632	1.00	31.34		N
ATOM	714	CA	VAL	A	92	−37.860	−12.385	95.875	1.00	31.22		C
ATOM	715	C	VAL	A	92	−38.510	−12.880	94.591	1.00	32.03		C
ATOM	716	O	VAL	A	92	−39.615	−13.429	94.616	1.00	32.99		O
ATOM	717	CB	VAL	A	92	−37.243	−13.525	96.695	1.00	25.83		C
ATOM	718	CG1	VAL	A	92	−36.306	−14.333	95.817	1.00	27.86		C
ATOM	719	CG2	VAL	A	92	−36.479	−12.962	97.892	1.00	20.30		C
ATOM	720	N	TYR	A	93	−37.871	−12.596	93.460	1.00	31.17		N
ATOM	721	CA	TYR	A	93	−38.321	−13.013	92.141	1.00	25.61		C
ATOM	722	C	TYR	A	93	−37.385	−14.112	91.680	1.00	27.44		C
ATOM	723	O	TYR	A	93	−36.167	−13.932	91.702	1.00	29.84		O
ATOM	724	CB	TYR	A	93	−38.327	−11.832	91.166	1.00	24.64		C
ATOM	725	CG	TYR	A	93	−39.424	−10.852	91.484	1.00	26.39		C
ATOM	726	CD1	TYR	A	93	−39.346	−10.047	92.606	1.00	24.17		C
ATOM	727	CD2	TYR	A	93	−40.556	−10.756	90.675	1.00	29.39		C
ATOM	728	CE1	TYR	A	93	−40.360	−9.180	92.927	1.00	30.45		C
ATOM	729	CE2	TYR	A	93	−41.573	−9.886	90.974	1.00	28.95		C
ATOM	730	CZ	TYR	A	93	−41.470	−9.096	92.108	1.00	30.87		C
ATOM	731	OH	TYR	A	93	−42.478	−8.228	92.442	1.00	29.44		O
ATOM	732	N	TYR	A	94	−37.946	−15.271	91.356	1.00	27.38		N
ATOM	733	CA	TYR	A	94	−37.195	−16.387	90.803	1.00	27.27		C
ATOM	734	C	TYR	A	94	−37.582	−16.602	89.347	1.00	27.79		C
ATOM	735	O	TYR	A	94	−38.728	−16.360	88.943	1.00	25.82		O
ATOM	736	CB	TYR	A	94	−37.453	−17.695	91.544	1.00	24.75		C
ATOM	737	CG	TYR	A	94	−37.170	−17.737	92.995	1.00	23.43		C
ATOM	738	CD1	TYR	A	94	−35.885	−17.935	93.462	1.00	28.16		C
ATOM	739	CD2	TYR	A	94	−38.199	−17.643	93.910	1.00	25.00		C
ATOM	740	CE1	TYR	A	94	−35.621	−18.000	94.820	1.00	32.06		C
ATOM	741	CE2	TYR	A	94	−37.955	−17.702	95.271	1.00	29.99		C
ATOM	742	CZ	TYR	A	94	−36.666	−17.881	95.720	1.00	33.84		C
ATOM	743	OH	TYR	A	94	−36.428	−17.954	97.069	1.00	39.80		O
ATOM	744	N	CYS	A	95	−36.618	−17.046	88.560	1.00	23.05		N
ATOM	745	CA	CYS	A	95	−36.940	−17.717	87.319	1.00	26.62		C
ATOM	746	C	CYS	A	95	−36.809	−19.212	87.547	1.00	27.72		C
ATOM	747	O	CYS	A	95	−36.050	−19.661	88.416	1.00	27.65		O
ATOM	748	CB	CYS	A	95	−36.029	−17.289	86.177	1.00	33.36		C
ATOM	749	SG	CYS	A	95	−34.315	−17.693	86.436	1.00	42.59		S
ATOM	750	N	ALA	A	96	−37.549	−19.988	86.766	1.00	25.63		N
ATOM	751	CA	ALA	A	96	−37.488	−21.432	86.941	1.00	24.92		C
ATOM	752	C	ALA	A	96	−37.693	−22.118	85.603	1.00	23.67		C
ATOM	753	O	ALA	A	96	−38.234	−21.545	84.650	1.00	22.72		O
ATOM	754	CB	ALA	A	96	−38.514	−21.933	87.971	1.00	20.77		C
ATOM	755	N	ARG	A	97	−37.232	−23.359	85.549	1.00	29.65		N
ATOM	756	CA	ARG	A	97	−37.442	−24.222	84.397	1.00	27.16		C
ATOM	757	C	ARG	A	97	−38.707	−25.049	84.601	1.00	25.26		C
ATOM	758	O	ARG	A	97	−38.796	−25.837	85.543	1.00	26.21		O
ATOM	759	CB	ARG	A	97	−36.241	−25.141	84.199	1.00	28.02		C
ATOM	760	CG	ARG	A	97	−36.333	−25.943	82.927	1.00	30.37		C
ATOM	761	CD	ARG	A	97	−35.057	−26.647	82.678	1.00	30.79		C
ATOM	762	NE	ARG	A	97	−35.199	−28.067	82.916	1.00	37.06		N
ATOM	763	CZ	ARG	A	97	−34.181	−28.869	83.182	1.00	41.04		C
ATOM	764	NH1	ARG	A	97	−32.962	−28.358	83.257	1.00	44.36		N
ATOM	765	NH2	ARG	A	97	−34.378	−30.172	83.387	1.00	43.81		N
ATOM	766	N	ASP	A	98	−39.663	−24.894	83.701	1.00	28.03		N
ATOM	767	CA	ASP	A	98	−40.928	−25.608	83.765	1.00	28.42		C
ATOM	768	C	ASP	A	98	−40.781	−26.830	82.871	1.00	29.02		C
ATOM	769	O	ASP	A	98	−40.568	−26.690	81.661	1.00	30.24		O
ATOM	770	CB	ASP	A	98	−42.074	−24.693	83.315	1.00	28.02		C
ATOM	771	CG	ASP	A	98	−43.460	−25.253	83.615	1.00	32.08		C
ATOM	772	OD2	ASP	A	98	−44.210	−24.615	84.387	1.00	34.95		O
ATOM	773	OD1	ASP	A	98	−43.837	−26.292	83.050	1.00	33.28		O
ATOM	774	N	TYR	A	99	−40.940	−28.023	83.458	1.00	30.78		N
ATOM	775	CA	TYR	A	99	−40.738	−29.329	82.815	1.00	30.04		C
ATOM	776	C	TYR	A	99	−41.625	−30.324	83.561	1.00	33.93		C
ATOM	777	O	TYR	A	99	−41.159	−31.204	84.293	1.00	38.31		O
ATOM	778	CB	TYR	A	99	−39.272	−29.767	82.827	1.00	29.21		C
ATOM	779	CG	TYR	A	99	−38.929	−30.840	81.794	1.00	34.85		C
ATOM	780	CD1	TYR	A	99	−39.322	−30.698	80.458	1.00	35.04		C
ATOM	781	CD2	TYR	A	99	−38.133	−31.940	82.127	1.00	32.30		C
ATOM	782	CE1	TYR	A	99	−38.982	−31.651	79.496	1.00	36.24		C
ATOM	783	CE2	TYR	A	99	−37.783	−32.896	81.172	1.00	28.54		C
ATOM	784	CZ	TYR	A	99	−38.209	−32.749	79.865	1.00	35.98		C
ATOM	785	OH	TYR	A	99	−37.874	−33.692	78.917	1.00	34.12		O
ATOM	786	N	GLY	A	100	−42.933	−30.172	83.358	1.00	28.51		N
ATOM	787	CA	GLY	A	100	−43.910	−30.735	84.262	1.00	24.10		C
ATOM	788	C	GLY	A	100	−44.030	−29.821	85.465	1.00	27.81		C
ATOM	789	O	GLY	A	100	−44.871	−28.922	85.491	1.00	27.49		O
ATOM	790	N	ALA	A	101	−43.179	−30.038	86.462	1.00	27.49		N
ATOM	791	CA	ALA	A	101	−43.007	−29.155	87.602	1.00	27.47		C
ATOM	792	C	ALA	A	101	−41.783	−28.256	87.421	1.00	30.09		C
ATOM	793	O	ALA	A	101	−41.094	−28.287	86.395	1.00	27.64		O
ATOM	794	CB	ALA	A	101	−42.895	−29.967	88.884	1.00	25.99		C
ATOM	795	N	PHE	A	102	−41.526	−27.427	88.434	1.00	23.58		N
ATOM	796	CA	PHE	A	102	−40.378	−26.521	88.429	1.00	29.82		C
ATOM	797	C	PHE	A	102	−39.181	−27.242	89.042	1.00	28.21		C
ATOM	798	O	PHE	A	102	−39.007	−27.255	90.268	1.00	26.65		O
ATOM	799	CB	PHE	A	102	−40.704	−25.241	89.185	1.00	24.30		C
ATOM	800	CG	PHE	A	102	−41.831	−24.469	88.585	1.00	29.71		C
ATOM	801	CD1	PHE	A	102	−41.705	−23.921	87.306	1.00	27.01		C
ATOM	802	CD2	PHE	A	102	−43.012	−24.265	89.297	1.00	28.29		C
ATOM	803	CE1	PHE	A	102	−42.719	−23.201	86.752	1.00	23.76		C
ATOM	804	CE2	PHE	A	102	−44.047	−23.538	88.738	1.00	27.29		C
ATOM	805	CZ	PHE	A	102	−43.897	−23.010	87.461	1.00	27.69		C
ATOM	806	N	ASP	A	103	−38.333	−27.818	88.179	1.00	24.44		N
ATOM	807	CA	ASP	A	103	−37.235	−28.648	88.657	1.00	28.27		C
ATOM	808	C	ASP	A	103	−35.943	−27.887	88.873	1.00	27.03		C
ATOM	809	O	ASP	A	103	−35.131	−28.306	89.693	1.00	37.49		O
ATOM	810	CB	ASP	A	103	−36.989	−29.838	87.721	1.00	31.73		C
ATOM	811	CG	ASP	A	103	−36.673	−29.436	86.302	1.00	39.51		C
ATOM	812	OD1	ASP	A	103	−36.346	−28.251	86.038	1.00	36.08		O
ATOM	813	OD2	ASP	A	103	−36.735	−30.340	85.438	1.00	44.53		O1−
ATOM	814	N	ILE	A	104	−35.734	−26.768	88.205	1.00	32.07		N
ATOM	815	CA	ILE	A	104	−34.562	−25.951	88.461	1.00	32.48		C
ATOM	816	C	ILE	A	104	−35.014	−24.530	88.674	1.00	30.55		C
ATOM	817	O	ILE	A	104	−35.832	−24.011	87.910	1.00	32.04		O
ATOM	818	CB	ILE	A	104	−33.537	−25.999	87.318	1.00	33.95		C
ATOM	819	CG1	ILE	A	104	−33.052	−27.421	87.124	1.00	31.05		C
ATOM	820	CG2	ILE	A	104	−32.357	−25.103	87.642	1.00	29.90		C
ATOM	821	CD1	ILE	A	104	−32.035	−27.491	86.097	1.00	37.82		C
ATOM	822	N	TRP	A	105	−34.437	−23.891	89.678	1.00	30.90		N
ATOM	823	CA	TRP	A	105	−34.761	−22.534	90.062	1.00	29.84		C
ATOM	824	C	TRP	A	105	−33.493	−21.703	90.002	1.00	35.42		C
ATOM	825	O	TRP	A	105	−32.384	−22.226	90.145	1.00	32.10		O
ATOM	826	CB	TRP	A	105	−35.340	−22.469	91.479	1.00	30.72		C
ATOM	827	CG	TRP	A	105	−36.660	−23.174	91.650	1.00	28.36		C
ATOM	828	CD1	TRP	A	105	−36.900	−24.508	91.535	1.00	26.86		C
ATOM	829	CD2	TRP	A	105	−37.906	−22.570	92.029	1.00	27.83		C
ATOM	830	NE1	TRP	A	105	−38.221	−24.775	91.787	1.00	26.76		N
ATOM	831	CE2	TRP	A	105	−38.862	−23.601	92.093	1.00	27.46		C
ATOM	832	CE3	TRP	A	105	−38.306	−21.246	92.305	1.00	24.64		C
ATOM	833	CZ2	TRP	A	105	−40.203	−23.359	92.425	1.00	26.14		C
ATOM	834	CZ3	TRP	A	105	−39.632	−21.002	92.628	1.00	26.09		C
ATOM	835	CH2	TRP	A	105	−40.569	−22.052	92.682	1.00	27.22		C
ATOM	836	N	GLY	A	106	−33.675	−20.409	89.739	1.00	36.95		N
ATOM	837	CA	GLY	A	106	−32.621	−19.444	89.932	1.00	30.80		C
ATOM	838	C	GLY	A	106	−32.355	−19.129	91.400	1.00	35.16		C
ATOM	839	O	GLY	A	106	−33.108	−19.455	92.312	1.00	36.82		O
ATOM	840	N	GLN	A	107	−31.218	−18.464	91.603	1.00	47.39		N
ATOM	841	CA	GLN	A	107	−30.810	−17.934	92.899	1.00	36.74		C
ATOM	842	C	GLN	A	107	−31.901	−17.089	93.533	1.00	39.96		C
ATOM	843	O	GLN	A	107	−32.042	−17.063	94.766	1.00	42.16		O
ATOM	844	CB	GLN	A	107	−29.557	−17.093	92.676	1.00	42.92		C
ATOM	845	CG	GLN	A	107	−29.167	−17.061	91.154	1.00	49.03		C
ATOM	846	CD	GLN	A	107	−28.508	−15.762	90.696	1.00	54.29		C
ATOM	847	OE1	GLN	A	107	−28.954	−14.661	91.047	1.00	58.14		O
ATOM	848	NE2	GLN	A	107	−27.442	−15.886	89.898	1.00	50.79		N
ATOM	849	N	GLY	A	108	−32.681	−16.410	92.707	1.00	31.86		N
ATOM	850	CA	GLY	A	108	−33.598	−15.378	93.128	1.00	27.03		C
ATOM	851	C	GLY	A	108	−32.949	−14.010	93.074	1.00	30.24		C
ATOM	852	O	GLY	A	108	−31.729	−13.864	93.142	1.00	37.43		O
ATOM	853	N	THR	A	109	−33.797	−12.994	92.950	1.00	25.96		N
ATOM	854	CA	THR	A	109	−33.387	−11.598	92.963	1.00	27.32		C
ATOM	855	C	THR	A	109	−34.249	−10.910	94.000	1.00	31.41		C
ATOM	856	O	THR	A	109	−35.475	−10.935	93.890	1.00	32.07		O
ATOM	857	CB	THR	A	109	−33.582	−10.910	91.604	1.00	34.49		C
ATOM	858	OG1	THR	A	109	−32.815	−11.575	90.587	1.00	40.25		O
ATOM	859	CG2	THR	A	109	−33.151	−9.449	91.696	1.00	26.29		C
ATOM	860	N	MET	A	110	−33.618	−10.317	95.010	1.00	34.98		N
ATOM	861	CA	MET	A	110	−34.341	−9.610	96.058	1.00	32.57		C
ATOM	862	C	MET	A	110	−34.744	−8.234	95.546	1.00	36.42		C
ATOM	863	O	MET	A	110	−33.881	−7.407	95.236	1.00	38.21		O
ATOM	864	CB	MET	A	110	−33.471	−9.495	97.301	1.00	32.17		C
ATOM	865	CG	MET	A	110	−34.222	−9.231	98.593	1.00	40.32		C
ATOM	866	SD	MET	A	110	−33.067	−9.017	99.988	1.00	67.95		S
ATOM	867	CE	MET	A	110	−31.758	−10.224	99.627	1.00	33.01		C
ATOM	868	N	VAL	A	111	−36.046	−7.977	95.455	1.00	33.03		N
ATOM	869	CA	VAL	A	111	−36.549	−6.745	94.860	1.00	33.46		C
ATOM	870	C	VAL	A	111	−37.261	−5.962	95.940	1.00	32.80		C
ATOM	871	O	VAL	A	111	−38.250	−6.441	96.502	1.00	34.50		O
ATOM	872	CB	VAL	A	111	−37.500	−7.004	93.679	1.00	34.14		C
ATOM	873	CG1	VAL	A	111	−38.216	−5.736	93.323	1.00	25.66		C
ATOM	874	CG2	VAL	A	111	−36.748	−7.559	92.470	1.00	30.59		C
ATOM	875	N	THR	A	112	−36.777	−4.756	96.211	1.00	33.30		N
ATOM	876	CA	THR	A	112	−37.383	−3.856	97.176	1.00	31.95		C
ATOM	877	C	THR	A	112	−37.950	−2.664	96.425	1.00	36.12		C
ATOM	878	O	THR	A	112	−37.249	−2.038	95.621	1.00	37.45		O
ATOM	879	CB	THR	A	112	−36.362	−3.387	98.207	1.00	31.08		C
ATOM	880	OG1	THR	A	112	−35.660	−4.523	98.708	1.00	33.39		O
ATOM	881	CG2	THR	A	112	−37.042	−2.661	99.366	1.00	29.77		C
ATOM	882	N	VAL	A	113	−39.210	−2.344	96.684	1.00	31.43		N
ATOM	883	CA	VAL	A	113	−39.827	−1.173	96.089	1.00	36.35		C
ATOM	884	C	VAL	A	113	−40.215	−0.226	97.216	1.00	36.75		C
ATOM	885	O	VAL	A	113	−41.039	−0.569	98.072	1.00	39.18		O
ATOM	886	CB	VAL	A	113	−41.043	−1.550	95.234	1.00	34.86		C
ATOM	887	CG1	VAL	A	113	−41.651	−0.305	94.602	1.00	34.99		C
ATOM	888	CG2	VAL	A	113	−40.631	−2.533	94.188	1.00	34.01		C
ATOM	889	N	SER	A	114	−39.653	0.974	97.192	1.00	36.38		N
ATOM	890	CA	SER	A	114	−39.797	1.848	98.340	1.00	36.28		C
ATOM	891	C	SER	A	114	−39.395	3.273	97.977	1.00	40.12		C
ATOM	892	O	SER	A	114	−38.525	3.507	97.123	1.00	40.70		O
ATOM	893	CB	SER	A	114	−38.954	1.341	99.507	1.00	31.28		C
ATOM	894	OG	SER	A	114	−38.863	2.336	100.505	1.00	39.09		O
ATOM	895	N	SER	A	115	−40.017	4.217	98.672	1.00	38.69		N
ATOM	896	CA	SER	A	115	−39.621	5.613	98.576	1.00	42.10		C
ATOM	897	C	SER	A	115	−38.296	5.892	99.267	1.00	46.74		C
ATOM	898	O	SER	A	115	−37.675	6.920	98.973	1.00	42.92		O
ATOM	899	CB	SER	A	115	−40.717	6.490	99.162	1.00	39.28		C
ATOM	900	OG	SER	A	115	−41.885	6.392	98.349	1.00	47.59		O
ATOM	901	N	ALA	A	116	−37.853	5.008	100.168	1.00	39.54		N
ATOM	902	CA	ALA	A	116	−36.656	5.257	100.954	1.00	35.81		C
ATOM	903	C	ALA	A	116	−35.417	5.270	100.067	1.00	37.57		C
ATOM	904	O	ALA	A	116	−35.411	4.730	98.963	1.00	38.65		O
ATOM	905	CB	ALA	A	116	−36.507	4.199	102.035	1.00	35.27		C
ATOM	906	N	SER	A	117	−34.347	5.880	100.571	1.00	38.00		N
ATOM	907	CA	SER	A	117	−33.079	5.924	99.855	1.00	40.96		C
ATOM	908	C	SER	A	117	−32.040	5.082	100.572	1.00	39.82		C
ATOM	909	O	SER	A	117	−32.108	4.893	101.790	1.00	40.84		O
ATOM	910	CB	SER	A	117	−32.561	7.352	99.715	1.00	38.33		C
ATOM	911	OG	SER	A	117	−33.448	8.084	98.896	1.00	52.15		O
ATOM	912	N	THR	A	118	−31.078	4.576	99.803	1.00	34.77		N
ATOM	913	CA	THR	A	118	−30.059	3.709	100.378	1.00	35.77		C
ATOM	914	C	THR	A	118	−29.387	4.392	101.560	1.00	40.75		C
ATOM	915	O	THR	A	118	−29.127	5.595	101.535	1.00	45.66		O
ATOM	916	CB	THR	A	118	−29.030	3.346	99.320	1.00	33.58		C
ATOM	917	OG1	THR	A	118	−29.662	2.534	98.320	1.00	42.35		O
ATOM	918	CG2	THR	A	118	−27.854	2.607	99.941	1.00	35.40		C
ATOM	919	N	LYS	A	119	−29.152	3.629	102.621	1.00	37.56		N
ATOM	920	CA	LYS	A	119	−28.635	4.215	103.848	1.00	36.23		C
ATOM	921	C	LYS	A	119	−28.000	3.126	104.697	1.00	36.78		C
ATOM	922	O	LYS	A	119	−28.629	2.100	104.959	1.00	31.04		O
ATOM	923	CB	LYS	A	119	−29.742	4.904	104.631	1.00	36.08		C
ATOM	924	CG	LYS	A	119	−29.224	5.571	105.867	1.00	32.45		C
ATOM	925	CD	LYS	A	119	−30.331	6.005	106.761	1.00	36.11		C
ATOM	926	CE	LYS	A	119	−29.719	6.656	107.950	1.00	41.55		C
ATOM	927	NZ	LYS	A	119	−28.719	5.693	108.485	1.00	40.27		N1+
ATOM	928	N	GLY	A	120	−26.761	3.351	105.115	1.00	32.34		N
ATOM	929	CA	GLY	A	120	−26.058	2.407	105.937	1.00	32.74		C
ATOM	930	C	GLY	A	120	−26.563	2.417	107.364	1.00	33.41		C
ATOM	931	O	GLY	A	120	−27.264	3.331	107.801	1.00	34.70		O
ATOM	932	N	PRO	A	121	−26.210	1.393	108.120	1.00	31.38		N
ATOM	933	CA	PRO	A	121	−26.705	1.283	109.493	1.00	36.27		C
ATOM	934	C	PRO	A	121	−25.863	2.075	110.478	1.00	29.36		C
ATOM	935	O	PRO	A	121	−24.723	2.442	110.213	1.00	28.70		O
ATOM	936	CB	PRO	A	121	−26.592	−0.217	109.784	1.00	32.75		C
ATOM	937	CG	PRO	A	121	−25.450	−0.653	108.950	1.00	31.60		C
ATOM	938	CD	PRO	A	121	−25.485	0.190	107.692	1.00	31.22		C
ATOM	939	N	SER	A	122	−26.481	2.365	111.614	1.00	28.35		N
ATOM	940	CA	SER	A	122	−25.790	2.748	112.834	1.00	27.65		C
ATOM	941	C	SER	A	122	−25.766	1.529	113.743	1.00	28.89		C
ATOM	942	O	SER	A	122	−26.780	0.843	113.874	1.00	33.72		O
ATOM	943	CB	SER	A	122	−26.490	3.915	113.528	1.00	27.60		C
ATOM	944	OG	SER	A	122	−26.537	5.035	112.665	1.00	32.84		O
ATOM	945	N	VAL	A	123	−24.615	1.239	114.341	1.00	30.13		N
ATOM	946	CA	VAL	A	123	−24.439	0.062	115.188	1.00	29.26		C
ATOM	947	C	VAL	A	123	−24.266	0.513	116.638	1.00	28.50		C
ATOM	948	O	VAL	A	123	−23.290	1.188	116.982	1.00	36.71		O
ATOM	949	CB	VAL	A	123	−23.257	−0.800	114.713	1.00	29.30		C
ATOM	950	CG1	VAL	A	123	−23.161	−2.079	115.535	1.00	32.16		C
ATOM	951	CG2	VAL	A	123	−23.421	−1.143	113.243	1.00	29.73		C
ATOM	952	N	PHE	A	124	−25.204	0.154	117.477	1.00	29.11		N
ATOM	953	CA	PHE	A	124	−25.117	0.453	118.892	1.00	30.43		C
ATOM	954	C	PHE	A	124	−24.914	−0.818	119.710	1.00	30.05		C
ATOM	955	O	PHE	A	124	−25.432	−1.871	119.341	1.00	28.55		O
ATOM	956	CB	PHE	A	124	−26.387	1.149	119.375	1.00	29.02		C
ATOM	957	CG	PHE	A	124	−26.765	2.328	118.559	1.00	31.89		C
ATOM	958	CD1	PHE	A	124	−25.952	3.448	118.525	1.00	37.36		C
ATOM	959	CD2	PHE	A	124	−27.948	2.345	117.848	1.00	33.36		C
ATOM	960	CE1	PHE	A	124	−26.309	4.550	117.784	1.00	33.03		C
ATOM	961	CE2	PHE	A	124	−28.307	3.451	117.112	1.00	32.67		C
ATOM	962	CZ	PHE	A	124	−27.486	4.548	117.085	1.00	31.27		C
ATOM	963	N	PRO	A	125	−24.212	−0.744	120.845	1.00	34.75		N
ATOM	964	CA	PRO	A	125	−23.997	−1.942	121.663	1.00	33.50		C
ATOM	965	C	PRO	A	125	−25.209	−2.306	122.514	1.00	33.10		C
ATOM	966	O	PRO	A	125	−25.956	−1.452	122.991	1.00	31.28		O
ATOM	967	CB	PRO	A	125	−22.808	−1.549	122.546	1.00	27.55		C
ATOM	968	CG	PRO	A	125	−22.913	−0.105	122.656	1.00	24.38		C
ATOM	969	CD	PRO	A	125	−23.459	0.407	121.378	1.00	30.67		C
ATOM	970	N	LEU	A	126	−25.395	−3.609	122.688	1.00	29.05		N
ATOM	971	CA	LEU	A	126	−26.264	−4.145	123.724	1.00	31.66		C
ATOM	972	C	LEU	A	126	−25.315	−4.627	124.801	1.00	33.65		C
ATOM	973	O	LEU	A	126	−24.728	−5.701	124.688	1.00	37.65		O
ATOM	974	CB	LEU	A	126	−27.167	−5.249	123.195	1.00	30.81		C
ATOM	975	CG	LEU	A	126	−27.997	−4.672	122.052	1.00	29.82		C
ATOM	976	CD1	LEU	A	126	−28.827	−5.730	121.357	1.00	26.48		C
ATOM	977	CD2	LEU	A	126	−28.860	−3.574	122.603	1.00	30.33		C
ATOM	978	N	ALA	A	127	−25.143	−3.805	125.835	1.00	38.61		N
ATOM	979	CA	ALA	A	127	−24.053	−4.011	126.768	1.00	36.09		C
ATOM	980	C	ALA	A	127	−24.399	−5.128	127.738	1.00	40.57		C
ATOM	981	O	ALA	A	127	−25.510	−5.137	128.289	1.00	36.21		O
ATOM	982	CB	ALA	A	127	−23.763	−2.733	127.529	1.00	35.02		C
ATOM	983	N	PRO	A	128	−23.478	−6.062	127.986	1.00	38.34		N
ATOM	984	CA	PRO	A	128	−23.759	−7.137	128.941	1.00	45.51		C
ATOM	985	C	PRO	A	128	−24.091	−6.569	130.309	1.00	56.56		C
ATOM	986	O	PRO	A	128	−23.360	−5.736	130.865	1.00	52.82		O
ATOM	987	CB	PRO	A	128	−22.463	−7.953	128.968	1.00	43.58		C
ATOM	988	CG	PRO	A	128	−21.433	−7.043	128.440	1.00	45.25		C
ATOM	989	CD	PRO	A	128	−22.124	−6.162	127.441	1.00	39.79		C
ATOM	990	N	SER	A	129	−25.212	−7.049	130.837	1.00	66.36		N
ATOM	991	CA	SER	A	129	−25.759	−6.677	132.128	1.00	72.65		C
ATOM	992	C	SER	A	129	−24.673	−6.810	133.195	1.00	76.84		C
ATOM	993	O	SER	A	129	−24.175	−7.914	133.453	1.00	78.41		O
ATOM	994	CB	SER	A	129	−26.983	−7.568	132.406	1.00	69.58		C
ATOM	995	OG	SER	A	129	−27.910	−7.001	133.309	1.00	70.69		O
ATOM	996	N	SER	A	130	−24.252	−5.681	133.776	1.00	77.98		N
ATOM	997	CA	SER	A	130	−23.377	−5.731	134.943	1.00	85.61		C
ATOM	998	C	SER	A	130	−23.994	−6.604	136.037	1.00	90.91		C
ATOM	999	O	SER	A	130	−23.273	−7.223	136.835	1.00	87.54		O
ATOM	1000	CB	SER	A	130	−23.089	−4.307	135.444	1.00	90.00		C
ATOM	1001	OG	SER	A	130	−24.274	−3.529	135.594	1.00	85.47		O
ATOM	1002	N	LYS	A	131	−25.331	−6.708	136.043	1.00	95.09		N
ATOM	1003	CA	LYS	A	131	−26.101	−7.524	136.974	1.00	92.61		C
ATOM	1004	C	LYS	A	131	−26.337	−8.936	136.436	1.00	92.99		C
ATOM	1005	O	LYS	A	131	−27.391	−9.540	136.695	1.00	88.38		O
ATOM	1006	CB	LYS	A	131	−27.436	−6.839	137.284	1.00	84.94		C
ATOM	1007	CG	LYS	A	131	−27.308	−5.523	138.053	1.00	86.39		C
ATOM	1008	CD	LYS	A	131	−28.673	−4.977	138.437	1.00	85.07		C
ATOM	1009	CE	LYS	A	131	−28.583	−4.070	139.646	1.00	74.74		C
ATOM	1010	NZ	LYS	A	131	−29.939	−3.594	140.022	1.00	70.33		N1+
ATOM	1011	N	SER	A	132	−25.386	−9.453	135.655	1.00	91.67		N
ATOM	1012	CA	SER	A	132	−25.423	−10.837	135.210	1.00	89.98		C
ATOM	1013	C	SER	A	132	−25.152	−11.744	136.398	1.00	95.97		C
ATOM	1014	O	SER	A	132	−24.296	−11.439	137.237	1.00	97.89		O
ATOM	1015	CB	SER	A	132	−24.366	−11.076	134.130	1.00	80.08		C
ATOM	1016	OG	SER	A	132	−24.779	−10.567	132.876	1.00	75.09		O
ATOM	1017	N	THR	A	133	−25.903	−12.846	136.495	1.00	96.88		N
ATOM	1018	CA	THR	A	133	−25.589	−13.828	137.529	1.00	94.98		C
ATOM	1019	C	THR	A	133	−24.133	−14.276	137.346	1.00	90.31		C
ATOM	1020	O	THR	A	133	−23.836	−15.107	136.480	1.00	81.64		O
ATOM	1021	CB	THR	A	133	−26.595	−15.001	137.481	1.00	90.13		C
ATOM	1022	OG1	THR	A	133	−26.943	−15.313	136.117	1.00	86.99		O
ATOM	1023	CG2	THR	A	133	−27.872	−14.664	138.271	1.00	77.20		C
ATOM	1024	N	SER	A	134	−23.219	−13.722	138.160	1.00	93.80		N
ATOM	1025	CA	SER	A	134	−21.784	−13.900	137.935	1.00	90.34		C
ATOM	1026	C	SER	A	134	−21.364	−15.323	138.275	1.00	87.03		C
ATOM	1027	O	SER	A	134	−21.597	−15.802	139.389	1.00	88.65		O
ATOM	1028	CB	SER	A	134	−20.971	−12.892	138.748	1.00	81.79		C
ATOM	1029	OG	SER	A	134	−19.872	−12.426	137.986	1.00	69.79		O
ATOM	1030	N	GLY	A	135	−20.701	−15.981	137.329	1.00	83.14		N
ATOM	1031	CA	GLY	A	135	−20.552	−17.418	137.366	1.00	79.97		C
ATOM	1032	C	GLY	A	135	−21.634	−18.150	136.607	1.00	75.17		C
ATOM	1033	O	GLY	A	135	−21.672	−19.387	136.643	1.00	70.13		O
ATOM	1034	N	GLY	A	136	−22.531	−17.411	135.954	1.00	73.84		N
ATOM	1035	CA	GLY	A	136	−23.577	−17.924	135.095	1.00	61.25		C
ATOM	1036	C	GLY	A	136	−23.388	−17.420	133.676	1.00	63.22		C
ATOM	1037	O	GLY	A	136	−22.265	−17.397	133.152	1.00	56.06		O
ATOM	1038	N	THR	A	137	−24.476	−16.996	133.040	1.00	59.59		N
ATOM	1039	CA	THR	A	137	−24.446	−16.674	131.626	1.00	48.48		C
ATOM	1040	C	THR	A	137	−24.845	−15.227	131.387	1.00	51.06		C
ATOM	1041	O	THR	A	137	−25.789	−14.712	132.002	1.00	56.26		O
ATOM	1042	CB	THR	A	137	−25.342	−17.624	130.849	1.00	47.89		C
ATOM	1043	OG1	THR	A	137	−24.756	−18.935	130.893	1.00	52.57		O
ATOM	1044	CG2	THR	A	137	−25.461	−17.182	129.398	1.00	39.41		C
ATOM	1045	N	ALA	A	138	−24.088	−14.574	130.510	1.00	44.74		N
ATOM	1046	CA	ALA	A	138	−24.313	−13.195	130.117	1.00	41.78		C
ATOM	1047	C	ALA	A	138	−24.782	−13.142	128.670	1.00	43.49		C
ATOM	1048	O	ALA	A	138	−24.337	−13.933	127.833	1.00	41.75		O
ATOM	1049	CB	ALA	A	138	−23.036	−12.369	130.273	1.00	44.03		C
ATOM	1050	N	ALA	A	139	−25.689	−12.215	128.384	1.00	43.46		N
ATOM	1051	CA	ALA	A	139	−26.067	−11.872	127.022	1.00	39.95		C
ATOM	1052	C	ALA	A	139	−25.455	−10.522	126.665	1.00	35.35		C
ATOM	1053	O	ALA	A	139	−25.393	−9.618	127.504	1.00	31.47		O
ATOM	1054	CB	ALA	A	139	−27.593	−11.827	126.865	1.00	27.83		C
ATOM	1055	N	LEU	A	140	−25.005	−10.399	125.419	1.00	30.62		N
ATOM	1056	CA	LEU	A	140	−24.563	−9.129	124.863	1.00	32.63		C
ATOM	1057	C	LEU	A	140	−24.915	−9.129	123.382	1.00	32.74		C
ATOM	1058	O	LEU	A	140	−25.288	−10.161	122.824	1.00	33.31		O
ATOM	1059	CB	LEU	A	140	−23.067	−8.925	125.098	1.00	36.31		C
ATOM	1060	CG	LEU	A	140	−22.182	−10.012	124.493	1.00	33.45		C
ATOM	1061	CD1	LEU	A	140	−21.538	−9.500	123.223	1.00	31.90		C
ATOM	1062	CD2	LEU	A	140	−21.146	−10.511	125.497	1.00	33.92		C
ATOM	1063	N	GLY	A	141	−24.839	−7.966	122.745	1.00	31.54		N
ATOM	1064	CA	GLY	A	141	−25.151	−7.940	121.332	1.00	28.33		C
ATOM	1065	C	GLY	A	141	−24.948	−6.589	120.690	1.00	27.25		C
ATOM	1066	O	GLY	A	141	−24.461	−5.640	121.304	1.00	31.88		O
ATOM	1067	N	CYS	A	142	−25.353	−6.529	119.428	1.00	25.30		N
ATOM	1068	CA	CYS	A	142	−25.336	−5.319	118.623	1.00	28.40		C
ATOM	1069	C	CYS	A	142	−26.729	−5.018	118.105	1.00	27.36		C
ATOM	1070	O	CYS	A	142	−27.484	−5.930	117.757	1.00	27.52		O
ATOM	1071	CB	CYS	A	142	−24.402	−5.447	117.435	1.00	30.69		C
ATOM	1072	SG	CYS	A	142	−22.691	−5.228	117.879	1.00	51.18		S
ATOM	1073	N	LEU	A	143	−27.056	−3.735	118.049	1.00	27.56		N
ATOM	1074	CA	LEU	A	143	−28.293	−3.248	117.460	1.00	27.81		C
ATOM	1075	C	LEU	A	143	−27.931	−2.565	116.145	1.00	27.63		C
ATOM	1076	O	LEU	A	143	−27.155	−1.613	116.136	1.00	31.79		O
ATOM	1077	CB	LEU	A	143	−28.985	−2.274	118.406	1.00	31.36		C
ATOM	1078	CG	LEU	A	143	−30.346	−1.766	117.963	1.00	31.23		C
ATOM	1079	CD1	LEU	A	143	−31.250	−2.954	117.862	1.00	28.10		C
ATOM	1080	CD2	LEU	A	143	−30.899	−0.706	118.886	1.00	32.28		C
ATOM	1081	N	VAL	A	144	−28.436	−3.083	115.036	1.00	30.74		N
ATOM	1082	CA	VAL	A	144	−28.101	−2.590	113.702	1.00	27.82		C
ATOM	1083	C	VAL	A	144	−29.311	−1.800	113.216	1.00	30.66		C
ATOM	1084	O	VAL	A	144	−30.289	−2.381	112.744	1.00	30.67		O
ATOM	1085	CB	VAL	A	144	−27.732	−3.744	112.769	1.00	28.14		C
ATOM	1086	CG1	VAL	A	144	−27.347	−3.252	111.375	1.00	23.30		C
ATOM	1087	CG2	VAL	A	144	−26.591	−4.541	113.411	1.00	25.34		C
ATOM	1088	N	LYS	A	145	−29.269	−0.470	113.374	1.00	33.19		N
ATOM	1089	CA	LYS	A	145	−30.446	0.383	113.245	1.00	31.94		C
ATOM	1090	C	LYS	A	145	−30.392	1.292	112.020	1.00	34.55		C
ATOM	1091	O	LYS	A	145	−29.322	1.758	111.612	1.00	32.70		O
ATOM	1092	CB	LYS	A	145	−30.637	1.229	114.504	1.00	34.83		C
ATOM	1093	CG	LYS	A	145	−32.055	1.752	114.654	1.00	39.24		C
ATOM	1094	CD	LYS	A	145	−32.309	2.302	116.035	1.00	37.76		C
ATOM	1095	CE	LYS	A	145	−33.802	2.550	116.282	1.00	47.55		C
ATOM	1096	NZ	LYS	A	145	−34.483	3.453	115.296	1.00	48.57		N1+
ATOM	1097	N	ASP	A	146	−31.564	1.494	111.414	1.00	35.65		N
ATOM	1098	CA	ASP	A	146	−31.815	2.517	110.399	1.00	31.21		C
ATOM	1099	C	ASP	A	146	−30.985	2.308	109.134	1.00	34.08		C
ATOM	1100	O	ASP	A	146	−30.204	3.170	108.721	1.00	35.04		O
ATOM	1101	CB	ASP	A	146	−31.568	3.919	110.960	1.00	31.93		C
ATOM	1102	CG	ASP	A	146	−32.501	4.276	112.097	1.00	39.35		C
ATOM	1103	OD1	ASP	A	146	−33.621	3.731	112.154	1.00	37.78		O
ATOM	1104	OD2	ASP	A	146	−32.150	5.184	112.878	1.00	48.93		O1−
ATOM	1105	N	TYR	A	147	−31.184	1.169	108.490	1.00	35.70		N
ATOM	1106	CA	TYR	A	147	−30.527	0.965	107.205	1.00	32.13		C
ATOM	1107	C	TYR	A	147	−31.548	0.662	106.127	1.00	30.25		C
ATOM	1108	O	TYR	A	147	−32.711	0.385	106.401	1.00	34.62		O
ATOM	1109	CB	TYR	A	147	−29.480	−0.146	107.270	1.00	29.22		C
ATOM	1110	CG	TYR	A	147	−30.026	−1.497	107.584	1.00	31.09		C
ATOM	1111	CD1	TYR	A	147	−30.476	−2.344	106.572	1.00	34.27		C
ATOM	1112	CD2	TYR	A	147	−30.068	−1.953	108.896	1.00	31.93		C
ATOM	1113	CE1	TYR	A	147	−30.965	−3.615	106.863	1.00	33.60		C
ATOM	1114	CE2	TYR	A	147	−30.547	−3.216	109.201	1.00	34.30		C
ATOM	1115	CZ	TYR	A	147	−30.998	−4.039	108.186	1.00	35.75		C
ATOM	1116	OH	TYR	A	147	−31.474	−5.283	108.511	1.00	33.90		O
ATOM	1117	N	PHE	A	148	−31.087	0.720	104.889	1.00	36.14		N
ATOM	1118	CA	PHE	A	148	−31.931	0.444	103.740	1.00	36.37		C
ATOM	1119	C	PHE	A	148	−31.063	0.353	102.506	1.00	35.17		C
ATOM	1120	O	PHE	A	148	−30.171	1.168	102.324	1.00	40.37		O
ATOM	1121	CB	PHE	A	148	−32.994	1.533	103.573	1.00	35.29		C
ATOM	1122	CG	PHE	A	148	−33.914	1.300	102.429	1.00	38.94		C
ATOM	1123	CD2	PHE	A	148	−33.582	1.733	101.154	1.00	37.28		C
ATOM	1124	CD1	PHE	A	148	−35.116	0.633	102.619	1.00	43.66		C
ATOM	1125	CE2	PHE	A	148	−34.431	1.509	100.090	1.00	40.33		C
ATOM	1126	CE1	PHE	A	148	−35.980	0.405	101.558	1.00	40.99		C
ATOM	1127	CZ	PHE	A	148	−35.632	0.843	100.288	1.00	41.29		C
ATOM	1128	N	PRO	A	149	−31.317	−0.641	101.646	1.00	38.61		N
ATOM	1129	CA	PRO	A	149	−32.320	−1.693	101.818	1.00	36.40		C
ATOM	1130	C	PRO	A	149	−31.736	−2.913	102.534	1.00	32.84		C
ATOM	1131	O	PRO	A	149	−30.607	−2.867	103.010	1.00	32.70		O
ATOM	1132	CB	PRO	A	149	−32.679	−2.036	100.378	1.00	36.43		C
ATOM	1133	CG	PRO	A	149	−31.331	−1.921	99.683	1.00	33.06		C
ATOM	1134	CD	PRO	A	149	−30.649	−0.743	100.332	1.00	34.54		C
ATOM	1135	N	GLU	A	150	−32.499	−3.995	102.601	1.00	33.19		N
ATOM	1136	CA	GLU	A	150	−31.952	−5.302	102.970	1.00	32.31		C
ATOM	1137	C	GLU	A	150	−30.980	−5.788	101.891	1.00	29.80		C
ATOM	1138	O	GLU	A	150	−31.160	−5.456	100.713	1.00	29.74		O
ATOM	1139	CB	GLU	A	150	−33.087	−6.301	103.166	1.00	28.58		C
ATOM	1140	CG	GLU	A	150	−33.977	−6.000	104.360	1.00	29.38		C
ATOM	1141	CD	GLU	A	150	−33.563	−6.767	105.602	1.00	39.48		C
ATOM	1142	OE1	GLU	A	150	−34.378	−7.590	106.099	1.00	41.15		O
ATOM	1143	OE2	GLU	A	150	−32.413	−6.566	106.065	1.00	41.49		O1−
ATOM	1144	N	PRO	A	151	−29.992	−6.630	102.263	1.00	31.91		N
ATOM	1145	CA	PRO	A	151	−29.735	−7.230	103.581	1.00	31.76		C
ATOM	1146	C	PRO	A	151	−28.502	−6.701	104.317	1.00	35.19		C
ATOM	1147	O	PRO	A	151	−27.684	−5.998	103.713	1.00	34.57		O
ATOM	1148	CB	PRO	A	151	−29.510	−8.690	103.223	1.00	23.34		C
ATOM	1149	CG	PRO	A	151	−28.788	−8.605	101.939	1.00	20.46		C
ATOM	1150	CD	PRO	A	151	−29.218	−7.334	101.225	1.00	25.12		C
ATOM	1151	N	VAL	A	152	−28.379	−7.046	105.602	1.00	30.30		N
ATOM	1152	CA	VAL	A	152	−27.128	−6.911	106.335	1.00	29.66		C
ATOM	1153	C	VAL	A	152	−26.726	−8.297	106.815	1.00	33.28		C
ATOM	1154	O	VAL	A	152	−27.580	−9.147	107.078	1.00	31.82		O
ATOM	1155	CB	VAL	A	152	−27.221	−5.959	107.550	1.00	31.08		C
ATOM	1156	CG1	VAL	A	152	−27.344	−4.523	107.116	1.00	36.88		C
ATOM	1157	CG2	VAL	A	152	−28.382	−6.349	108.403	1.00	32.42		C
ATOM	1158	N	THR	A	153	−25.419	−8.509	106.967	1.00	32.49		N
ATOM	1159	CA	THR	A	153	−24.873	−9.711	107.585	1.00	31.87		C
ATOM	1160	C	THR	A	153	−24.123	−9.336	108.858	1.00	33.40		C
ATOM	1161	O	THR	A	153	−23.517	−8.264	108.952	1.00	35.81		O
ATOM	1162	CB	THR	A	153	−23.924	−10.442	106.644	1.00	27.89		C
ATOM	1163	OG1	THR	A	153	−22.904	−9.528	106.239	1.00	36.53		O
ATOM	1164	CG2	THR	A	153	−24.676	−10.910	105.408	1.00	29.45		C
ATOM	1165	N	VAL	A	154	−24.189	−10.213	109.852	1.00	24.86		N
ATOM	1166	CA	VAL	A	154	−23.508	−10.013	111.116	1.00	27.57		C
ATOM	1167	C	VAL	A	154	−22.745	−11.281	111.472	1.00	29.28		C
ATOM	1168	O	VAL	A	154	−23.316	−12.374	111.480	1.00	35.29		O
ATOM	1169	CB	VAL	A	154	−24.499	−9.646	112.240	1.00	30.65		C
ATOM	1170	CG1	VAL	A	154	−23.770	−9.393	113.542	1.00	30.74		C
ATOM	1171	CG2	VAL	A	154	−25.312	−8.454	111.849	1.00	29.70		C
ATOM	1172	N	SER	A	155	−21.463	−11.137	111.766	1.00	29.75		N
ATOM	1173	CA	SER	A	155	−20.720	−12.183	112.446	1.00	32.79		C
ATOM	1174	C	SER	A	155	−20.100	−11.604	113.711	1.00	36.14		C
ATOM	1175	O	SER	A	155	−20.134	−10.393	113.961	1.00	34.64		O
ATOM	1176	CB	SER	A	155	−19.648	−12.800	111.550	1.00	28.09		C
ATOM	1177	OG	SER	A	155	−18.682	−11.839	111.164	1.00	32.25		O
ATOM	1178	N	TRP	A	156	−19.522	−12.495	114.504	1.00	28.20		N
ATOM	1179	CA	TRP	A	156	−18.940	−12.149	115.781	1.00	30.93		C
ATOM	1180	C	TRP	A	156	−17.495	−12.610	115.807	1.00	35.40		C
ATOM	1181	O	TRP	A	156	−17.202	−13.750	115.427	1.00	34.28		O
ATOM	1182	CB	TRP	A	156	−19.731	−12.786	116.913	1.00	30.86		C
ATOM	1183	CG	TRP	A	156	−20.988	−12.046	117.160	1.00	32.29		C
ATOM	1184	CD1	TRP	A	156	−22.184	−12.252	116.553	1.00	32.31		C
ATOM	1185	CD2	TRP	A	156	−21.168	−10.939	118.048	1.00	31.77		C
ATOM	1186	NE1	TRP	A	156	−23.106	−11.348	117.012	1.00	33.15		N
ATOM	1187	CE2	TRP	A	156	−22.508	−10.529	117.933	1.00	31.90		C
ATOM	1188	CE3	TRP	A	156	−20.325	−10.253	118.929	1.00	33.09		C
ATOM	1189	CZ2	TRP	A	156	−23.037	−9.477	118.679	1.00	29.54		C
ATOM	1190	CZ3	TRP	A	156	−20.852	−9.197	119.665	1.00	34.64		C
ATOM	1191	CH2	TRP	A	156	−22.199	−8.828	119.539	1.00	31.80		C
ATOM	1192	N	ASN	A	157	−16.603	−11.723	116.262	1.00	28.12		N
ATOM	1193	CA	ASN	A	157	−15.185	−12.020	116.346	1.00	27.84		C
ATOM	1194	C	ASN	A	157	−14.675	−12.543	115.010	1.00	31.80		C
ATOM	1195	O	ASN	A	157	−13.925	−13.515	114.956	1.00	33.84		O
ATOM	1196	CB	ASN	A	157	−14.888	−13.031	117.461	1.00	29.77		C
ATOM	1197	CG	ASN	A	157	−15.039	−12.460	118.845	1.00	26.46		C
ATOM	1198	OD1	ASN	A	157	−15.346	−11.294	119.024	1.00	30.29		O
ATOM	1199	ND2	ASN	A	157	−14.823	−13.294	119.842	1.00	33.06		N
ATOM	1200	N	SER	A	158	−15.102	−11.898	113.922	1.00	31.97		N
ATOM	1201	CA	SER	A	158	−14.661	−12.248	112.570	1.00	33.51		C
ATOM	1202	C	SER	A	158	−14.956	−13.699	112.215	1.00	36.13		C
ATOM	1203	O	SER	A	158	−14.224	−14.307	111.438	1.00	42.62		O
ATOM	1204	CB	SER	A	158	−13.170	−11.972	112.375	1.00	28.57		C
ATOM	1205	OG	SER	A	158	−12.839	−10.678	112.818	1.00	41.72		O
ATOM	1206	N	GLY	A	159	−16.007	−14.278	112.791	1.00	36.17		N
ATOM	1207	CA	GLY	A	159	−16.371	−15.654	112.532	1.00	30.18		C
ATOM	1208	C	GLY	A	159	−15.840	−16.648	113.540	1.00	32.92		C
ATOM	1209	O	GLY	A	159	−16.226	−17.823	113.497	1.00	29.97		O
ATOM	1210	N	ALA	A	160	−14.960	−16.217	114.437	1.00	37.02		N
ATOM	1211	CA	ALA	A	160	−14.420	−17.132	115.431	1.00	32.79		C
ATOM	1212	C	ALA	A	160	−15.442	−17.476	116.505	1.00	34.92		C
ATOM	1213	O	ALA	A	160	−15.345	−18.540	117.121	1.00	48.32		O
ATOM	1214	CB	ALA	A	160	−13.164	−16.532	116.061	1.00	28.82		C
ATOM	1215	N	LEU	A	161	−16.416	−16.617	116.751	1.00	35.16		N
ATOM	1216	CA	LEU	A	161	−17.432	−16.878	117.759	1.00	33.95		C
ATOM	1217	C	LEU	A	161	−18.713	−17.278	117.047	1.00	32.88		C
ATOM	1218	O	LEU	A	161	−19.239	−16.519	116.234	1.00	35.85		O
ATOM	1219	CB	LEU	A	161	−17.653	−15.658	118.648	1.00	30.18		C
ATOM	1220	CG	LEU	A	161	−18.778	−15.719	119.683	1.00	35.02		C
ATOM	1221	CD1	LEU	A	161	−18.826	−17.042	120.432	1.00	28.23		C
ATOM	1222	CD2	LEU	A	161	−18.673	−14.517	120.661	1.00	33.30		C
ATOM	1223	N	THR	A	162	−19.233	−18.450	117.394	1.00	39.79		N
ATOM	1224	CA	THR	A	162	−20.298	−19.078	116.630	1.00	33.54		C
ATOM	1225	C	THR	A	162	−21.336	−19.691	117.569	1.00	32.35		C
ATOM	1226	O	THR	A	162	−22.541	−19.506	117.391	1.00	30.46		O
ATOM	1227	CB	THR	A	162	−19.662	−20.099	115.669	1.00	33.49		C
ATOM	1228	OG1	THR	A	162	−19.956	−19.724	114.318	1.00	27.42		O
ATOM	1229	CG2	THR	A	162	−20.098	−21.543	115.959	1.00	34.98		C
ATOM	1230	N	SER	A	163	−20.885	−20.391	118.598	1.00	34.58		N
ATOM	1231	CA	SER	A	163	−21.813	−20.925	119.583	1.00	35.61		C
ATOM	1232	C	SER	A	163	−22.538	−19.785	120.301	1.00	35.40		C
ATOM	1233	O	SER	A	163	−21.925	−18.781	120.681	1.00	37.87		O
ATOM	1234	CB	SER	A	163	−21.044	−21.799	120.578	1.00	35.71		C
ATOM	1235	OG	SER	A	163	−21.864	−22.247	121.633	1.00	43.49		O
ATOM	1236	N	GLY	A	164	−23.856	−19.911	120.442	1.00	28.98		N
ATOM	1237	CA	GLY	A	164	−24.625	−18.958	121.206	1.00	25.01		C
ATOM	1238	C	GLY	A	164	−25.128	−17.744	120.446	1.00	33.29		C
ATOM	1239	O	GLY	A	164	−25.869	−16.946	121.031	1.00	33.20		O
ATOM	1240	N	VAL	A	165	−24.754	−17.576	119.160	1.00	30.78		N
ATOM	1241	CA	VAL	A	165	−25.156	−16.414	118.374	1.00	25.26		C
ATOM	1242	C	VAL	A	165	−26.588	−16.586	117.885	1.00	31.13		C
ATOM	1243	O	VAL	A	165	−26.998	−17.679	117.480	1.00	36.05		O
ATOM	1244	CB	VAL	A	165	−24.189	−16.187	117.195	1.00	24.24		C
ATOM	1245	CG1	VAL	A	165	−24.660	−15.030	116.320	1.00	26.94		C
ATOM	1246	CG2	VAL	A	165	−22.806	−15.872	117.701	1.00	26.51		C
ATOM	1247	N	HIS	A	166	−27.368	−15.507	117.975	1.00	30.95		N
ATOM	1248	CA	HIS	A	166	−28.639	−15.358	117.275	1.00	27.16		C
ATOM	1249	C	HIS	A	166	−28.634	−14.011	116.567	1.00	29.61		C
ATOM	1250	O	HIS	A	166	−28.486	−12.968	117.218	1.00	28.82		O
ATOM	1251	CB	HIS	A	166	−29.841	−15.434	118.225	1.00	26.50		C
ATOM	1252	CG	HIS	A	166	−29.913	−16.697	119.017	1.00	29.14		C
ATOM	1253	ND1	HIS	A	166	−30.069	−17.932	118.430	1.00	31.57		N
ATOM	1254	CD2	HIS	A	166	−29.894	−16.914	120.349	1.00	29.50		C
ATOM	1255	CE1	HIS	A	166	−30.123	−18.859	119.368	1.00	30.30		C
ATOM	1256	NE2	HIS	A	166	−30.025	−18.267	120.541	1.00	29.10		N
ATOM	1257	N	THR	A	167	−28.765	−14.030	115.242	1.00	32.27		N
ATOM	1258	CA	THR	A	167	−29.023	−12.828	114.457	1.00	30.55		C
ATOM	1259	C	THR	A	167	−30.473	−12.820	113.997	1.00	29.36		C
ATOM	1260	O	THR	A	167	−30.914	−13.738	113.306	1.00	34.07		O
ATOM	1261	CB	THR	A	167	−28.089	−12.737	113.264	1.00	24.74		C
ATOM	1262	OG1	THR	A	167	−26.740	−12.697	113.745	1.00	35.43		O
ATOM	1263	CG2	THR	A	167	−28.377	−11.481	112.509	1.00	23.22		C
ATOM	1264	N	PHE	A	168	−31.182	−11.797	114.351	1.00	28.41		N
ATOM	1265	CA	PHE	A	168	−32.626	−11.776	114.226	1.00	28.58		C
ATOM	1266	C	PHE	A	168	−33.064	−11.245	112.869	1.00	30.77		C
ATOM	1267	O	PHE	A	168	−32.304	−10.564	112.176	1.00	31.27		O
ATOM	1268	CB	PHE	A	168	−33.222	−10.953	115.358	1.00	22.95		C
ATOM	1269	CG	PHE	A	168	−33.164	−11.654	116.672	1.00	28.82		C
ATOM	1270	CD1	PHE	A	168	−34.177	−12.526	117.052	1.00	30.01		C
ATOM	1271	CD2	PHE	A	168	−32.089	−11.484	117.521	1.00	26.59		C
ATOM	1272	CE1	PHE	A	168	−34.120	−13.192	118.269	1.00	26.13		C
ATOM	1273	CE2	PHE	A	168	−32.034	−12.153	118.738	1.00	24.89		C
ATOM	1274	CZ	PHE	A	168	−33.047	−12.999	119.109	1.00	25.58		C
ATOM	1275	N	PRO	A	169	−34.268	−11.613	112.428	1.00	30.91		N
ATOM	1276	CA	PRO	A	169	−34.825	−10.991	111.221	1.00	28.45		C
ATOM	1277	C	PRO	A	169	−35.017	−9.500	111.445	1.00	30.28		C
ATOM	1278	O	PRO	A	169	−35.392	−9.063	112.534	1.00	26.91		O
ATOM	1279	CB	PRO	A	169	−36.166	−11.705	111.036	1.00	21.98		C
ATOM	1280	CG	PRO	A	169	−36.064	−12.951	111.870	1.00	25.73		C
ATOM	1281	CD	PRO	A	169	−35.157	−12.642	112.999	1.00	24.24		C
ATOM	1282	N	ALA	A	170	−34.718	−8.713	110.419	1.00	29.94		N
ATOM	1283	CA	ALA	A	170	−34.909	−7.277	110.530	1.00	28.66		C
ATOM	1284	C	ALA	A	170	−36.397	−6.962	110.631	1.00	24.51		C
ATOM	1285	O	ALA	A	170	−37.231	−7.715	110.147	1.00	20.86		O
ATOM	1286	CB	ALA	A	170	−34.289	−6.564	109.326	1.00	28.82		C
ATOM	1287	N	VAL	A	171	−36.725	−5.833	111.264	1.00	25.89		N
ATOM	1288	CA	VAL	A	171	−38.070	−5.279	111.200	1.00	24.76		C
ATOM	1289	C	VAL	A	171	−38.012	−4.012	110.358	1.00	28.48		C
ATOM	1290	O	VAL	A	171	−36.997	−3.307	110.326	1.00	27.98		O
ATOM	1291	CB	VAL	A	171	−38.700	−4.967	112.577	1.00	27.45		C
ATOM	1292	CG1	VAL	A	171	−38.882	−6.245	113.387	1.00	27.65		C
ATOM	1293	CG2	VAL	A	171	−37.913	−3.890	113.334	1.00	27.22		C
ATOM	1294	N	LEU	A	172	−39.111	−3.745	109.653	1.00	25.17		N
ATOM	1295	CA	LEU	A	172	−39.301	−2.534	108.867	1.00	27.51		C
ATOM	1296	C	LEU	A	172	−40.092	−1.517	109.692	1.00	31.05		C
ATOM	1297	O	LEU	A	172	−41.270	−1.730	109.995	1.00	33.68		O
ATOM	1298	CB	LEU	A	172	−40.015	−2.862	107.565	1.00	27.53		C
ATOM	1299	CG	LEU	A	172	−40.360	−1.652	106.713	1.00	31.73		C
ATOM	1300	CD1	LEU	A	172	−39.092	−0.851	106.423	1.00	31.62		C
ATOM	1301	CD2	LEU	A	172	−41.011	−2.118	105.405	1.00	28.68		C
ATOM	1302	N	GLN	A	173	−39.439	−0.422	110.052	1.00	25.80		N
ATOM	1303	CA	GLN	A	173	−40.029	0.612	110.877	1.00	31.71		C
ATOM	1304	C	GLN	A	173	−40.841	1.595	110.033	1.00	34.79		C
ATOM	1305	O	GLN	A	173	−40.706	1.669	108.805	1.00	31.87		O
ATOM	1306	CB	GLN	A	173	−38.945	1.372	111.634	1.00	33.05		C
ATOM	1307	CG	GLN	A	173	−37.969	0.495	112.392	1.00	33.17		C
ATOM	1308	CD	GLN	A	173	−36.669	1.222	112.686	1.00	35.50		C
ATOM	1309	OE1	GLN	A	173	−36.309	1.424	113.850	1.00	39.44		O
ATOM	1310	NE2	GLN	A	173	−35.960	1.626	111.629	1.00	33.32		N
ATOM	1311	N	SER	A	174	−41.681	2.378	110.726	1.00	34.71		N
ATOM	1312	CA	SER	A	174	−42.563	3.323	110.049	1.00	30.21		C
ATOM	1313	C	SER	A	174	−41.773	4.343	109.245	1.00	31.66		C
ATOM	1314	O	SER	A	174	−42.322	4.937	108.314	1.00	34.94		O
ATOM	1315	CB	SER	A	174	−43.461	4.017	111.063	1.00	31.49		C
ATOM	1316	OG	SER	A	174	−42.708	4.905	111.882	1.00	40.96		O
ATOM	1317	N	SER	A	175	−40.480	4.495	109.533	1.00	29.45		N
ATOM	1318	CA	SER	A	175	−39.594	5.363	108.769	1.00	29.62		C
ATOM	1319	C	SER	A	175	−39.270	4.831	107.374	1.00	37.39		C
ATOM	1320	O	SER	A	175	−38.665	5.564	106.581	1.00	35.03		O
ATOM	1321	CB	SER	A	175	−38.288	5.558	109.531	1.00	26.45		C
ATOM	1322	OG	SER	A	175	−37.522	4.366	109.537	1.00	33.35		O
ATOM	1323	N	GLY	A	176	−39.610	3.574	107.068	1.00	33.52		N
ATOM	1324	CA	GLY	A	176	−39.139	2.922	105.865	1.00	26.71		C
ATOM	1325	C	GLY	A	176	−37.767	2.308	105.988	1.00	28.94		C
ATOM	1326	O	GLY	A	176	−37.323	1.632	105.061	1.00	33.48		O
ATOM	1327	N	LEU	A	177	−37.105	2.482	107.118	1.00	31.53		N
ATOM	1328	CA	LEU	A	177	−35.796	1.912	107.374	1.00	32.69		C
ATOM	1329	C	LEU	A	177	−35.924	0.601	108.155	1.00	33.78		C
ATOM	1330	O	LEU	A	177	−36.839	0.412	108.965	1.00	27.20		O
ATOM	1331	CB	LEU	A	177	−34.937	2.932	108.138	1.00	30.37		C
ATOM	1332	CG	LEU	A	177	−34.691	4.252	107.381	1.00	31.43		C
ATOM	1333	CD1	LEU	A	177	−33.897	5.220	108.180	1.00	29.09		C
ATOM	1334	CD2	LEU	A	177	−33.948	4.024	106.072	1.00	32.81		C
ATOM	1335	N	TYR	A	178	−34.979	−0.299	107.915	1.00	32.33		N
ATOM	1336	CA	TYR	A	178	−34.938	−1.580	108.601	1.00	31.28		C
ATOM	1337	C	TYR	A	178	−34.061	−1.480	109.848	1.00	31.26		C
ATOM	1338	O	TYR	A	178	−33.221	−0.589	109.975	1.00	30.90		O
ATOM	1339	CB	TYR	A	178	−34.399	−2.679	107.681	1.00	30.14		C
ATOM	1340	CG	TYR	A	178	−35.311	−3.040	106.535	1.00	29.91		C
ATOM	1341	CD2	TYR	A	178	−35.140	−2.470	105.275	1.00	30.71		C
ATOM	1342	CD1	TYR	A	178	−36.324	−3.960	106.703	1.00	28.37		C
ATOM	1343	CE2	TYR	A	178	−35.966	−2.793	104.226	1.00	32.21		C
ATOM	1344	CE1	TYR	A	178	−37.160	−4.287	105.667	1.00	29.97		C
ATOM	1345	CZ	TYR	A	178	−36.984	−3.704	104.426	1.00	34.62		C
ATOM	1346	OH	TYR	A	178	−37.822	−4.043	103.385	1.00	35.36		O
ATOM	1347	N	SER	A	179	−34.265	−2.425	110.764	1.00	31.86		N
ATOM	1348	CA	SER	A	179	−33.513	−2.503	112.007	1.00	29.05		C
ATOM	1349	C	SER	A	179	−33.405	−3.960	112.453	1.00	30.76		C
ATOM	1350	O	SER	A	179	−34.418	−4.660	112.534	1.00	31.95		O
ATOM	1351	CB	SER	A	179	−34.185	−1.669	113.086	1.00	29.95		C
ATOM	1352	OG	SER	A	179	−33.208	−1.108	113.936	1.00	40.38		O
ATOM	1353	N	LEU	A	180	−32.192	−4.427	112.737	1.00	28.38		N
ATOM	1354	CA	LEU	A	180	−32.044	−5.768	113.282	1.00	31.63		C
ATOM	1355	C	LEU	A	180	−31.118	−5.768	114.492	1.00	29.92		C
ATOM	1356	O	LEU	A	180	−30.388	−4.810	114.763	1.00	25.79		O
ATOM	1357	CB	LEU	A	180	−31.555	−6.783	112.224	1.00	30.26		C
ATOM	1358	CG	LEU	A	180	−30.143	−7.049	111.701	1.00	31.57		C
ATOM	1359	CD1	LEU	A	180	−29.103	−7.464	112.770	1.00	28.74		C
ATOM	1360	CD2	LEU	A	180	−30.291	−8.158	110.658	1.00	28.38		C
ATOM	1361	N	SER	A	181	−31.159	−6.872	115.228	1.00	25.89		N
ATOM	1362	CA	SER	A	181	−30.261	−7.060	116.348	1.00	29.69		C
ATOM	1363	C	SER	A	181	−29.651	−8.454	116.283	1.00	34.25		C
ATOM	1364	O	SER	A	181	−30.228	−9.383	115.710	1.00	28.49		O
ATOM	1365	CB	SER	A	181	−30.972	−6.840	117.680	1.00	32.18		C
ATOM	1366	OG	SER	A	181	−31.900	−7.868	117.927	1.00	34.51		O
ATOM	1367	N	SER	A	182	−28.451	−8.572	116.852	1.00	34.33		N
ATOM	1368	CA	SER	A	182	−27.720	−9.826	116.939	1.00	31.79		C
ATOM	1369	C	SER	A	182	−27.166	−9.956	118.351	1.00	29.53		C
ATOM	1370	O	SER	A	182	−26.634	−8.992	118.899	1.00	29.22		O
ATOM	1371	CB	SER	A	182	−26.589	−9.875	115.889	1.00	28.22		C
ATOM	1372	OG	SER	A	182	−25.793	−11.040	116.033	1.00	32.19		O
ATOM	1373	N	VAL	A	183	−27.302	−11.140	118.946	1.00	31.33		N
ATOM	1374	CA	VAL	A	183	−26.891	−11.353	120.329	1.00	32.43		C
ATOM	1375	C	VAL	A	183	−26.090	−12.648	120.461	1.00	34.27		C
ATOM	1376	O	VAL	A	183	−26.118	−13.530	119.599	1.00	34.59		O
ATOM	1377	CB	VAL	A	183	−28.100	−11.386	121.290	1.00	34.07		C
ATOM	1378	CG1	VAL	A	183	−28.915	−10.138	121.139	1.00	30.31		C
ATOM	1379	CG2	VAL	A	183	−28.962	−12.619	121.027	1.00	34.20		C
ATOM	1380	N	VAL	A	184	−25.370	−12.750	121.567	1.00	30.31		N
ATOM	1381	CA	VAL	A	184	−24.615	−13.950	121.895	1.00	34.88		C
ATOM	1382	C	VAL	A	184	−24.629	−14.101	123.409	1.00	36.21		C
ATOM	1383	O	VAL	A	184	−24.549	−13.112	124.145	1.00	36.42		O
ATOM	1384	CB	VAL	A	184	−23.172	−13.893	121.322	1.00	36.52		C
ATOM	1385	CG1	VAL	A	184	−22.405	−12.622	121.770	1.00	28.53		C
ATOM	1386	CG2	VAL	A	184	−22.413	−15.146	121.668	1.00	28.44		C
ATOM	1387	N	THR	A	185	−24.800	−15.335	123.876	1.00	37.42		N
ATOM	1388	CA	THR	A	185	−24.681	−15.649	125.290	1.00	33.86		C
ATOM	1389	C	THR	A	185	−23.296	−16.235	125.522	1.00	36.91		C
ATOM	1390	O	THR	A	185	−22.829	−17.074	124.744	1.00	36.01		O
ATOM	1391	CB	THR	A	185	−25.772	−16.614	125.758	1.00	36.45		C
ATOM	1392	OG1	THR	A	185	−25.864	−17.719	124.850	1.00	42.60		O
ATOM	1393	CG2	THR	A	185	−27.110	−15.912	125.804	1.00	34.96		C
ATOM	1394	N	VAL	A	186	−22.632	−15.755	126.567	1.00	40.17		N
ATOM	1395	CA	VAL	A	186	−21.268	−16.144	126.917	1.00	38.85		C
ATOM	1396	C	VAL	A	186	−21.196	−16.288	128.432	1.00	47.21		C
ATOM	1397	O	VAL	A	186	−22.080	−15.806	129.155	1.00	45.09		O
ATOM	1398	CB	VAL	A	186	−20.244	−15.102	126.425	1.00	36.70		C
ATOM	1399	CG1	VAL	A	186	−20.351	−14.919	124.902	1.00	33.73		C
ATOM	1400	CG2	VAL	A	186	−20.485	−13.768	127.107	1.00	35.85		C
ATOM	1401	N	PRO	A	187	−20.161	−16.964	128.944	1.00	47.74		N
ATOM	1402	CA	PRO	A	187	−20.031	−17.090	130.404	1.00	46.98		C
ATOM	1403	C	PRO	A	187	−19.776	−15.738	131.058	1.00	48.85		C
ATOM	1404	O	PRO	A	187	−19.016	−14.922	130.538	1.00	46.36		O
ATOM	1405	CB	PRO	A	187	−18.830	−18.026	130.571	1.00	43.33		C
ATOM	1406	CG	PRO	A	187	−18.751	−18.759	129.303	1.00	39.13		C
ATOM	1407	CD	PRO	A	187	−19.170	−17.794	128.244	1.00	43.58		C
ATOM	1408	N	SER	A	188	−20.423	−15.509	132.208	1.00	50.33		N
ATOM	1409	CA	SER	A	188	−20.194	−14.283	132.972	1.00	47.34		C
ATOM	1410	C	SER	A	188	−18.715	−14.066	133.275	1.00	55.46		C
ATOM	1411	O	SER	A	188	−18.208	−12.942	133.158	1.00	49.43		O
ATOM	1412	CB	SER	A	188	−21.001	−14.310	134.262	1.00	52.91		C
ATOM	1413	OG	SER	A	188	−22.363	−14.112	133.973	1.00	59.47		O
ATOM	1414	N	SER	A	189	−18.010	−15.127	133.685	1.00	55.39		N
ATOM	1415	CA	SER	A	189	−16.590	−15.005	134.003	1.00	55.76		C
ATOM	1416	C	SER	A	189	−15.769	−14.513	132.811	1.00	58.34		C
ATOM	1417	O	SER	A	189	−14.681	−13.951	133.002	1.00	59.39		O
ATOM	1418	CB	SER	A	189	−16.042	−16.351	134.478	1.00	56.17		C
ATOM	1419	OG	SER	A	189	−16.101	−17.316	133.435	1.00	52.74		O
ATOM	1420	N	SER	A	190	−16.276	−14.687	131.590	1.00	53.51		N
ATOM	1421	CA	SER	A	190	−15.528	−14.312	130.396	1.00	56.22		C
ATOM	1422	C	SER	A	190	−15.594	−12.816	130.086	1.00	54.08		C
ATOM	1423	O	SER	A	190	−14.802	−12.330	129.265	1.00	51.28		O
ATOM	1424	CB	SER	A	190	−16.020	−15.138	129.197	1.00	51.36		C
ATOM	1425	OG	SER	A	190	−17.368	−14.852	128.863	1.00	46.74		O
ATOM	1426	N	LEU	A	191	−16.523	−12.081	130.693	1.00	53.01		N
ATOM	1427	CA	LEU	A	191	−16.577	−10.644	130.464	1.00	53.09		C
ATOM	1428	C	LEU	A	191	−15.339	−9.981	131.058	1.00	54.27		C
ATOM	1429	O	LEU	A	191	−14.790	−10.428	132.071	1.00	58.30		O
ATOM	1430	CB	LEU	A	191	−17.839	−10.054	131.081	1.00	38.62		C
ATOM	1431	CG	LEU	A	191	−19.093	−10.795	130.646	1.00	45.96		C
ATOM	1432	CD1	LEU	A	191	−20.297	−10.313	131.431	1.00	42.60		C
ATOM	1433	CD2	LEU	A	191	−19.308	−10.675	129.131	1.00	40.49		C
ATOM	1434	N	GLY	A	192	−14.896	−8.905	130.421	1.00	50.04		N
ATOM	1435	CA	GLY	A	192	−13.722	−8.196	130.886	1.00	59.39		C
ATOM	1436	C	GLY	A	192	−12.384	−8.841	130.570	1.00	59.35		C
ATOM	1437	O	GLY	A	192	−11.382	−8.120	130.468	1.00	65.09		O
ATOM	1438	N	THR	A	193	−12.332	−10.163	130.376	1.00	50.42		N
ATOM	1439	CA	THR	A	193	−11.152	−10.830	129.835	1.00	51.34		C
ATOM	1440	C	THR	A	193	−11.269	−11.178	128.350	1.00	53.60		C
ATOM	1441	O	THR	A	193	−10.257	−11.147	127.651	1.00	57.09		O
ATOM	1442	CB	THR	A	193	−10.822	−12.109	130.622	1.00	56.32		C
ATOM	1443	OG1	THR	A	193	−11.943	−12.512	131.418	1.00	57.77		O
ATOM	1444	CG2	THR	A	193	−9.595	−11.892	131.523	1.00	48.53		C
ATOM	1445	N	GLN	A	194	−12.451	−11.519	127.838	1.00	53.81		N
ATOM	1446	CA	GLN	A	194	−12.619	−11.879	126.431	1.00	47.52		C
ATOM	1447	C	GLN	A	194	−13.238	−10.716	125.660	1.00	45.35		C
ATOM	1448	O	GLN	A	194	−14.169	−10.066	126.142	1.00	47.02		O
ATOM	1449	CB	GLN	A	194	−13.512	−13.111	126.292	1.00	46.52		C
ATOM	1450	CG	GLN	A	194	−13.761	−13.550	124.857	1.00	46.74		C
ATOM	1451	CD	GLN	A	194	−12.496	−13.985	124.141	1.00	53.73		C
ATOM	1452	OE1	GLN	A	194	−12.011	−13.301	123.239	1.00	52.18		O
ATOM	1453	NE2	GLN	A	194	−11.967	−15.148	124.528	1.00	50.74		N
ATOM	1454	N	THR	A	195	−12.745	−10.462	124.453	1.00	44.88		N
ATOM	1455	CA	THR	A	195	−13.244	−9.345	123.657	1.00	46.31		C
ATOM	1456	C	THR	A	195	−14.325	−9.802	122.680	1.00	43.67		C
ATOM	1457	O	THR	A	195	−14.211	−10.862	122.057	1.00	41.58		O
ATOM	1458	CB	THR	A	195	−12.104	−8.651	122.909	1.00	53.06		C
ATOM	1459	OG1	THR	A	195	−11.441	−7.742	123.803	1.00	57.28		O
ATOM	1460	CG2	THR	A	195	−12.631	−7.884	121.694	1.00	42.53		C
ATOM	1461	N	TYR	A	196	−15.393	−9.007	122.579	1.00	43.78		N
ATOM	1462	CA	TYR	A	196	−16.551	−9.321	121.750	1.00	36.48		C
ATOM	1463	C	TYR	A	196	−16.798	−8.201	120.755	1.00	34.63		C
ATOM	1464	O	TYR	A	196	−17.090	−7.066	121.139	1.00	34.38		O
ATOM	1465	CB	TYR	A	196	−17.769	−9.564	122.621	1.00	32.34		C
ATOM	1466	CG	TYR	A	196	−17.567	−10.773	123.470	1.00	38.36		C
ATOM	1467	CD1	TYR	A	196	−17.517	−12.036	122.900	1.00	36.90		C
ATOM	1468	CD2	TYR	A	196	−17.359	−10.655	124.830	1.00	39.09		C
ATOM	1469	CE1	TYR	A	196	−17.316	−13.151	123.676	1.00	37.95		C
ATOM	1470	CE2	TYR	A	196	−17.147	−11.755	125.605	1.00	39.61		C
ATOM	1471	CZ	TYR	A	196	−17.129	−13.001	125.028	1.00	39.92		C
ATOM	1472	OH	TYR	A	196	−16.921	−14.098	125.825	1.00	47.25		O
ATOM	1473	N	ILE	A	197	−16.653	−8.516	119.478	1.00	35.82		N
ATOM	1474	CA	ILE	A	197	−16.831	−7.548	118.405	1.00	36.37		C
ATOM	1475	C	ILE	A	197	−17.841	−8.108	117.422	1.00	30.22		C
ATOM	1476	O	ILE	A	197	−17.783	−9.287	117.065	1.00	32.67		O
ATOM	1477	CB	ILE	A	197	−15.496	−7.222	117.702	1.00	32.39		C
ATOM	1478	CG1	ILE	A	197	−14.528	−6.609	118.709	1.00	32.03		C
ATOM	1479	CG2	ILE	A	197	−15.722	−6.302	116.521	1.00	28.21		C
ATOM	1480	CD1	ILE	A	197	−13.138	−6.617	118.246	1.00	30.83		C
ATOM	1481	N	CYS	A	198	−18.784	−7.287	117.016	1.00	34.51		N
ATOM	1482	CA	CYS	A	198	−19.717	−7.687	115.984	1.00	35.67		C
ATOM	1483	C	CYS	A	198	−19.346	−7.002	114.676	1.00	33.53		C
ATOM	1484	O	CYS	A	198	−19.039	−5.805	114.645	1.00	32.08		O
ATOM	1485	CB	CYS	A	198	−21.157	−7.379	116.404	1.00	36.62		C
ATOM	1486	SG	CYS	A	198	−21.662	−5.699	116.191	1.00	46.42		S
ATOM	1487	N	ASN	A	199	−19.373	−7.777	113.598	1.00	31.00		N
ATOM	1488	CA	ASN	A	199	−18.952	−7.325	112.279	1.00	34.62		C
ATOM	1489	C	ASN	A	199	−20.212	−7.179	111.438	1.00	30.03		C
ATOM	1490	O	ASN	A	199	−20.926	−8.157	111.205	1.00	33.61		O
ATOM	1491	CB	ASN	A	199	−17.969	−8.322	111.669	1.00	30.80		C
ATOM	1492	CG	ASN	A	199	−16.998	−8.861	112.691	1.00	33.45		C
ATOM	1493	OD1	ASN	A	199	−17.071	−10.028	113.087	1.00	30.25		O
ATOM	1494	ND2	ASN	A	199	−16.090	−8.004	113.146	1.00	31.39		N
ATOM	1495	N	VAL	A	200	−20.530	−5.961	111.036	1.00	25.18		N
ATOM	1496	CA	VAL	A	200	−21.753	−5.699	110.295	1.00	31.02		C
ATOM	1497	C	VAL	A	200	−21.346	−5.394	108.868	1.00	31.80		C
ATOM	1498	O	VAL	A	200	−20.402	−4.632	108.642	1.00	32.16		O
ATOM	1499	CB	VAL	A	200	−22.581	−4.546	110.896	1.00	26.09		C
ATOM	1500	CG1	VAL	A	200	−23.862	−4.409	110.130	1.00	31.91		C
ATOM	1501	CG2	VAL	A	200	−22.900	−4.792	112.348	1.00	27.12		C
ATOM	1502	N	ASN	A	201	−22.022	−6.016	107.910	1.00	31.12		N
ATOM	1503	CA	ASN	A	201	−21.800	−5.693	106.511	1.00	34.13		C
ATOM	1504	C	ASN	A	201	−23.127	−5.341	105.866	1.00	32.42		C
ATOM	1505	O	ASN	A	201	−24.065	−6.141	105.883	1.00	35.02		O
ATOM	1506	CB	ASN	A	201	−21.122	−6.839	105.767	1.00	36.09		C
ATOM	1507	CG	ASN	A	201	−20.557	−6.390	104.457	1.00	39.19		C
ATOM	1508	OD1	ASN	A	201	−20.860	−5.296	104.000	1.00	43.01		O
ATOM	1509	ND2	ASN	A	201	−19.730	−7.218	103.844	1.00	44.41		N
ATOM	1510	N	HIS	A	202	−23.222	−4.123	105.361	1.00	34.15		N
ATOM	1511	CA	HIS	A	202	−24.349	−3.682	104.561	1.00	33.64		C
ATOM	1512	C	HIS	A	202	−23.801	−3.403	103.168	1.00	39.81		C
ATOM	1513	O	HIS	A	202	−23.463	−2.264	102.836	1.00	37.99		O
ATOM	1514	CB	HIS	A	202	−25.001	−2.473	105.147	1.00	31.71		C
ATOM	1515	CG	HIS	A	202	−26.244	−2.052	104.425	1.00	37.75		C
ATOM	1516	ND1	HIS	A	202	−26.419	−0.780	103.917	1.00	38.12		N
ATOM	1517	CD2	HIS	A	202	−27.377	−2.735	104.129	1.00	32.94		C
ATOM	1518	CE1	HIS	A	202	−27.607	−0.699	103.344	1.00	37.74		C
ATOM	1519	NE2	HIS	A	202	−28.210	−1.871	103.463	1.00	34.91		N
ATOM	1520	N	LYS	A	203	−23.690	−4.461	102.359	1.00	34.79		N
ATOM	1521	CA	LYS	A	203	−23.249	−4.285	100.978	1.00	35.75		C
ATOM	1522	C	LYS	A	203	−24.071	−3.261	100.195	1.00	39.45		C
ATOM	1523	O	LYS	A	203	−23.482	−2.573	99.346	1.00	38.28		O
ATOM	1524	CB	LYS	A	203	−23.166	−5.647	100.266	1.00	29.77		C
ATOM	1525	CG	LYS	A	203	−21.879	−6.425	100.649	1.00	40.20		C
ATOM	1526	CD	LYS	A	203	−20.652	−5.726	99.988	1.00	63.25		C
ATOM	1527	CE	LYS	A	203	−19.279	−6.000	100.660	1.00	68.58		C
ATOM	1528	NZ	LYS	A	203	−18.938	−7.439	100.898	1.00	69.85		N1+
ATOM	1529	N	PRO	A	204	−25.392	−3.108	100.390	1.00	41.00		N
ATOM	1530	CA	PRO	A	204	−26.120	−2.121	99.566	1.00	38.96		C
ATOM	1531	C	PRO	A	204	−25.629	−0.681	99.705	1.00	40.45		C
ATOM	1532	O	PRO	A	204	−25.839	0.114	98.782	1.00	44.07		O
ATOM	1533	CB	PRO	A	204	−27.568	−2.272	100.043	1.00	36.97		C
ATOM	1534	CG	PRO	A	204	−27.647	−3.652	100.563	1.00	35.26		C
ATOM	1535	CD	PRO	A	204	−26.327	−3.952	101.168	1.00	33.30		C
ATOM	1536	N	SER	A	205	−25.061	−0.287	100.845	1.00	42.01		N
ATOM	1537	CA	SER	A	205	−24.455	1.034	100.993	1.00	40.43		C
ATOM	1538	C	SER	A	205	−22.931	0.956	101.094	1.00	39.05		C
ATOM	1539	O	SER	A	205	−22.279	1.963	101.369	1.00	37.64		O
ATOM	1540	CB	SER	A	205	−25.052	1.778	102.195	1.00	35.25		C
ATOM	1541	OG	SER	A	205	−24.659	1.213	103.424	1.00	36.65		O
ATOM	1542	N	ASN	A	206	−22.354	−0.219	100.868	1.00	42.36		N
ATOM	1543	CA	ASN	A	206	−20.919	−0.449	101.017	1.00	44.31		C
ATOM	1544	C	ASN	A	206	−20.414	0.021	102.382	1.00	46.67		C
ATOM	1545	O	ASN	A	206	−19.385	0.680	102.506	1.00	50.37		O
ATOM	1546	CB	ASN	A	206	−20.146	0.208	99.880	1.00	49.52		C
ATOM	1547	CG	ASN	A	206	−19.229	−0.766	99.187	1.00	61.70		C
ATOM	1548	OD1	ASN	A	206	−19.323	−1.979	99.401	1.00	67.47		O
ATOM	1549	ND2	ASN	A	206	−18.336	−0.253	98.352	1.00	70.26		N
ATOM	1550	N	THR	A	207	−21.150	−0.352	103.423	1.00	45.98		N
ATOM	1551	CA	THR	A	207	−20.861	0.041	104.792	1.00	36.87		C
ATOM	1552	C	THR	A	207	−20.417	−1.180	105.574	1.00	37.03		C
ATOM	1553	O	THR	A	207	−21.118	−2.192	105.590	1.00	41.13		O
ATOM	1554	CB	THR	A	207	−22.100	0.626	105.457	1.00	42.00		C
ATOM	1555	OG1	THR	A	207	−22.616	1.689	104.649	1.00	45.30		O
ATOM	1556	CG2	THR	A	207	−21.767	1.132	106.876	1.00	42.01		C
ATOM	1557	N	LYS	A	208	−19.263	−1.088	106.210	1.00	36.32		N
ATOM	1558	CA	LYS	A	208	−18.793	−2.110	107.127	1.00	32.74		C
ATOM	1559	C	LYS	A	208	−18.511	−1.465	108.478	1.00	34.61		C
ATOM	1560	O	LYS	A	208	−18.088	−0.307	108.545	1.00	39.61		O
ATOM	1561	CB	LYS	A	208	−17.552	−2.827	106.585	1.00	40.21		C
ATOM	1562	CG	LYS	A	208	−17.865	−3.863	105.502	1.00	39.11		C
ATOM	1563	CD	LYS	A	208	−16.707	−4.821	105.239	1.00	34.67		C
ATOM	1564	CE	LYS	A	208	−15.518	−4.128	104.606	1.00	49.09		C
ATOM	1565	NZ	LYS	A	208	−14.349	−5.076	104.456	1.00	57.65		N1+
ATOM	1566	N	VAL	A	209	−18.846	−2.174	109.552	1.00	32.84		N
ATOM	1567	CA	VAL	A	209	−18.671	−1.684	110.917	1.00	32.20		C
ATOM	1568	C	VAL	A	209	−18.247	−2.844	111.797	1.00	34.40		C
ATOM	1569	O	VAL	A	209	−18.906	−3.889	111.817	1.00	38.11		O
ATOM	1570	CB	VAL	A	209	−19.960	−1.054	111.491	1.00	31.14		C
ATOM	1571	CG1	VAL	A	209	−19.816	−0.826	112.974	1.00	27.96		C
ATOM	1572	CG2	VAL	A	209	−20.276	0.252	110.810	1.00	26.07		C
ATOM	1573	N	ASP	A	210	−17.195	−2.642	112.574	1.00	36.64		N
ATOM	1574	CA	ASP	A	210	−16.821	−3.545	113.659	1.00	33.62		C
ATOM	1575	C	ASP	A	210	−17.053	−2.791	114.962	1.00	30.39		C
ATOM	1576	O	ASP	A	210	−16.490	−1.718	115.159	1.00	32.48		O
ATOM	1577	CB	ASP	A	210	−15.360	−3.980	113.548	1.00	32.01		C
ATOM	1578	CG	ASP	A	210	−15.084	−4.843	112.325	1.00	42.55		C
ATOM	1579	OD1	ASP	A	210	−15.829	−5.839	112.124	1.00	46.60		O
ATOM	1580	OD2	ASP	A	210	−14.119	−4.527	111.570	1.00	34.51		O1−
ATOM	1581	N	LYS	A	211	−17.904	−3.319	115.827	1.00	34.41		N
ATOM	1582	CA	LYS	A	211	−18.270	−2.654	117.073	1.00	28.87		C
ATOM	1583	C	LYS	A	211	−17.832	−3.519	118.243	1.00	33.13		C
ATOM	1584	O	LYS	A	211	−18.283	−4.661	118.374	1.00	31.45		O
ATOM	1585	CB	LYS	A	211	−19.775	−2.409	117.155	1.00	30.56		C
ATOM	1586	CG	LYS	A	211	−20.246	−1.799	118.460	1.00	33.07		C
ATOM	1587	CD	LYS	A	211	−19.646	−0.430	118.618	1.00	36.20		C
ATOM	1588	CE	LYS	A	211	−20.539	0.467	119.407	1.00	33.18		C
ATOM	1589	NZ	LYS	A	211	−20.169	1.877	119.156	1.00	35.41		N1+
ATOM	1590	N	LYS	A	212	−16.962	−2.972	119.094	1.00	35.68		N
ATOM	1591	CA	LYS	A	212	−16.654	−3.617	120.354	1.00	28.26		C
ATOM	1592	C	LYS	A	212	−17.806	−3.349	121.296	1.00	30.86		C
ATOM	1593	O	LYS	A	212	−18.409	−2.271	121.278	1.00	33.51		O
ATOM	1594	CB	LYS	A	212	−15.341	−3.112	120.955	1.00	31.23		C
ATOM	1595	CG	LYS	A	212	−14.740	−4.080	121.984	1.00	38.53		C
ATOM	1596	CD	LYS	A	212	−13.567	−3.503	122.778	1.00	42.63		C
ATOM	1597	CE	LYS	A	212	−13.088	−4.492	123.847	1.00	44.88		C
ATOM	1598	NZ	LYS	A	212	−12.001	−3.960	124.723	1.00	52.61		N1+
ATOM	1599	N	VAL	A	213	−18.175	−4.376	122.039	1.00	30.30		N
ATOM	1600	CA	VAL	A	213	−19.246	−4.322	123.012	1.00	34.60		C
ATOM	1601	C	VAL	A	213	−18.589	−4.663	124.336	1.00	35.78		C
ATOM	1602	O	VAL	A	213	−18.141	−5.795	124.530	1.00	39.34		O
ATOM	1603	CB	VAL	A	213	−20.380	−5.300	122.667	1.00	36.86		C
ATOM	1604	CG1	VAL	A	213	−21.521	−5.226	123.700	1.00	37.67		C
ATOM	1605	CG2	VAL	A	213	−20.903	−5.028	121.278	1.00	27.28		C
ATOM	1606	N	GLU	A	214	−18.489	−3.687	125.228	1.00	43.48		N
ATOM	1607	CA	GLU	A	214	−17.839	−3.878	126.521	1.00	42.79		C
ATOM	1608	C	GLU	A	214	−18.866	−3.868	127.636	1.00	39.79		C
ATOM	1609	O	GLU	A	214	−19.925	−3.250	127.508	1.00	39.59		O
ATOM	1610	CB	GLU	A	214	−16.795	−2.787	126.788	1.00	42.03		C
ATOM	1611	CG	GLU	A	214	−15.715	−2.770	125.730	1.00	53.61		C
ATOM	1612	CD	GLU	A	214	−14.732	−1.636	125.888	1.00	60.49		C
ATOM	1613	OE1	GLU	A	214	−13.614	−1.878	126.391	1.00	64.12		O
ATOM	1614	OE2	GLU	A	214	−15.085	−0.500	125.505	1.00	65.45		O1−
ATOM	1615	N	PRO	A	215	−18.599	−4.573	128.724	1.00	42.19		N
ATOM	1616	CA	PRO	A	215	−19.495	−4.496	129.882	1.00	47.10		C
ATOM	1617	C	PRO	A	215	−19.546	−3.089	130.452	1.00	54.06		C
ATOM	1618	O	PRO	A	215	−18.521	−2.414	130.566	1.00	56.58		O
ATOM	1619	CB	PRO	A	215	−18.885	−5.492	130.874	1.00	49.68		C
ATOM	1620	CG	PRO	A	215	−17.567	−5.950	130.264	1.00	48.26		C
ATOM	1621	CD	PRO	A	215	−17.651	−5.695	128.809	1.00	45.54		C
ATOM	1622	N	LYS	A	216	−20.760	−2.636	130.768	1.00	59.07		N
ATOM	1623	CA	LYS	A	216	−21.008	−1.289	131.272	1.00	66.58		C
ATOM	1624	C	LYS	A	216	−21.516	−1.355	132.710	1.00	80.80		C
ATOM	1625	O	LYS	A	216	−22.468	−2.092	133.005	1.00	75.99		O
ATOM	1626	CB	LYS	A	216	−22.036	−0.555	130.408	1.00	66.80		C
ATOM	1627	CG	LYS	A	216	−22.360	0.859	130.899	1.00	73.54		C
ATOM	1628	CD	LYS	A	216	−23.096	1.653	129.834	1.00	77.62		C
ATOM	1629	CE	LYS	A	216	−23.325	3.092	130.255	1.00	75.50		C
ATOM	1630	NZ	LYS	A	216	−23.769	3.921	129.103	1.00	65.88		N1+
ATOM	1631	N	SER	A	217	−20.927	−0.528	133.580	1.00	90.64		N
ATOM	1632	CA	SER	A	217	−21.323	−0.451	134.994	1.00	92.77		C
ATOM	1633	C	SER	A	217	−22.109	0.829	135.282	1.00	85.80		C
ATOM	1634	O	SER	A	217	−23.332	0.797	135.455	1.00	82.11		O
ATOM	1635	CB	SER	A	217	−20.096	−0.528	135.915	1.00	84.71		C
ATOM	1636	OG	SER	A	217	−19.239	0.585	135.722	1.00	86.75		O
TER
ATOM	1637	N	GLU	B	1	−59.401	−19.548	88.941	1.00	32.61		N
ATOM	1638	CA	GLU	B	1	−58.164	−20.286	89.135	1.00	32.73		C
ATOM	1639	C	GLU	B	1	−58.344	−21.415	90.159	1.00	39.88		C
ATOM	1640	O	GLU	B	1	−59.196	−21.331	91.040	1.00	39.29		O
ATOM	1641	CB	GLU	B	1	−57.054	−19.366	89.613	1.00	32.87		C
ATOM	1642	CG	GLU	B	1	−57.037	−19.224	91.116	1.00	33.91		C
ATOM	1643	CD	GLU	B	1	−56.083	−18.160	91.599	1.00	44.88		C
ATOM	1644	OE1	GLU	B	1	−56.022	−17.970	92.832	1.00	55.17		O
ATOM	1645	OE2	GLU	B	1	−55.378	−17.536	90.763	1.00	44.77		O1−
ATOM	1646	N	ILE	B	2	−57.536	−22.470	90.052	1.00	36.20		N
ATOM	1647	CA	ILE	B	2	−57.589	−23.542	91.037	1.00	31.00		C
ATOM	1648	C	ILE	B	2	−56.950	−23.074	92.339	1.00	27.84		C
ATOM	1649	O	ILE	B	2	−55.774	−22.694	92.370	1.00	27.28		O
ATOM	1650	CB	ILE	B	2	−56.893	−24.797	90.521	1.00	30.83		C
ATOM	1651	CG1	ILE	B	2	−57.571	−25.303	89.259	1.00	24.03		C
ATOM	1652	CG2	ILE	B	2	−56.832	−25.856	91.649	1.00	24.77		C
ATOM	1653	CD1	ILE	B	2	−56.866	−26.508	88.716	1.00	24.00		C
ATOM	1654	N	VAL	B	3	−57.718	−23.116	93.424	1.00	28.01		N
ATOM	1655	CA	VAL	B	3	−57.227	−22.750	94.748	1.00	31.60		C
ATOM	1656	C	VAL	B	3	−56.810	−24.011	95.498	1.00	30.30		C
ATOM	1657	O	VAL	B	3	−57.580	−24.976	95.602	1.00	30.30		O
ATOM	1658	CB	VAL	B	3	−58.287	−21.965	95.535	1.00	30.01		C
ATOM	1659	CG1	VAL	B	3	−57.782	−21.724	96.916	1.00	23.45		C
ATOM	1660	CG2	VAL	B	3	−58.637	−20.645	94.815	1.00	24.87		C
ATOM	1661	N	LEU	B	4	−55.591	−24.017	96.006	1.00	27.66		N
ATOM	1662	CA	LEU	B	4	−55.047	−25.168	96.709	1.00	27.72		C
ATOM	1663	C	LEU	B	4	−54.941	−24.793	98.170	1.00	30.07		C
ATOM	1664	O	LEU	B	4	−54.281	−23.805	98.509	1.00	34.25		O
ATOM	1665	CB	LEU	B	4	−53.677	−25.570	96.165	1.00	31.34		C
ATOM	1666	CG	LEU	B	4	−53.596	−26.025	94.711	1.00	30.78		C
ATOM	1667	CD1	LEU	B	4	−52.155	−26.475	94.361	1.00	29.60		C
ATOM	1668	CD2	LEU	B	4	−54.571	−27.161	94.511	1.00	23.79		C
ATOM	1669	N	THR	B	5	−55.591	−25.568	99.026	1.00	26.39		N
ATOM	1670	CA	THR	B	5	−55.586	−25.330	100.458	1.00	23.07		C
ATOM	1671	C	THR	B	5	−54.765	−26.407	101.130	1.00	26.07		C
ATOM	1672	O	THR	B	5	−55.089	−27.591	101.034	1.00	29.54		O
ATOM	1673	CB	THR	B	5	−57.007	−25.330	101.019	1.00	23.58		C
ATOM	1674	OG1	THR	B	5	−57.813	−24.424	100.256	1.00	25.83		O
ATOM	1675	CG2	THR	B	5	−56.992	−24.892	102.458	1.00	18.31		C
ATOM	1676	N	GLN	B	6	−53.731	−26.003	101.830	1.00	23.61		N
ATOM	1677	CA	GLN	B	6	−52.920	−26.943	102.569	1.00	25.57		C
ATOM	1678	C	GLN	B	6	−53.328	−26.929	104.024	1.00	24.28		C
ATOM	1679	O	GLN	B	6	−53.585	−25.871	104.592	1.00	28.38		O
ATOM	1680	CB	GLN	B	6	−51.432	−26.623	102.442	1.00	21.43		C
ATOM	1681	CG	GLN	B	6	−50.866	−27.125	101.172	1.00	25.09		C
ATOM	1682	CD	GLN	B	6	−49.406	−26.785	101.003	1.00	29.92		C
ATOM	1683	OE1	GLN	B	6	−49.065	−25.856	100.258	1.00	30.10		O
ATOM	1684	NE2	GLN	B	6	−48.529	−27.542	101.671	1.00	23.00		N
ATOM	1685	N	SER	B	7	−53.388	−28.113	104.609	1.00	28.46		N
ATOM	1686	CA	SER	B	7	−53.526	−28.273	106.046	1.00	32.14		C
ATOM	1687	C	SER	B	7	−52.626	−29.410	106.541	1.00	32.52		C
ATOM	1688	O	SER	B	7	−52.238	−30.294	105.774	1.00	31.45		O
ATOM	1689	CB	SER	B	7	−54.960	−28.558	106.404	1.00	26.70		C
ATOM	1690	OG	SER	B	7	−55.208	−29.883	106.045	1.00	39.01		O
ATOM	1691	N	PRO	B	8	−52.242	−29.367	107.816	1.00	35.79		N
ATOM	1692	CA	PRO	B	8	−52.444	−28.237	108.728	1.00	32.17		C
ATOM	1693	C	PRO	B	8	−51.456	−27.142	108.349	1.00	33.18		C
ATOM	1694	O	PRO	B	8	−50.550	−27.465	107.590	1.00	35.18		O
ATOM	1695	CB	PRO	B	8	−52.119	−28.837	110.103	1.00	26.39		C
ATOM	1696	CG	PRO	B	8	−51.061	−29.854	109.786	1.00	33.66		C
ATOM	1697	CD	PRO	B	8	−51.426	−30.438	108.422	1.00	30.11		C
ATOM	1698	N	GLY	B	9	−51.584	−25.920	108.877	1.00	35.12		N
ATOM	1699	CA	GLY	B	9	−50.583	−24.899	108.603	1.00	25.91		C
ATOM	1700	C	GLY	B	9	−49.249	−25.202	109.264	1.00	27.68		C
ATOM	1701	O	GLY	B	9	−48.196	−25.015	108.661	1.00	27.97		O
ATOM	1702	N	THR	B	10	−49.274	−25.726	110.487	1.00	26.27		N
ATOM	1703	CA	THR	B	10	−48.056	−26.118	111.179	1.00	27.02		C
ATOM	1704	C	THR	B	10	−48.197	−27.524	111.746	1.00	26.07		C
ATOM	1705	O	THR	B	10	−49.251	−27.890	112.264	1.00	30.58		O
ATOM	1706	CB	THR	B	10	−47.725	−25.143	112.310	1.00	26.29		C
ATOM	1707	OG1	THR	B	10	−47.699	−23.812	111.789	1.00	30.87		O
ATOM	1708	CG2	THR	B	10	−46.368	−25.480	112.929	1.00	18.58		C
ATOM	1709	N	LEU	B	11	−47.117	−28.296	111.669	1.00	28.05		N
ATOM	1710	CA	LEU	B	11	−47.057	−29.670	112.156	1.00	27.74		C
ATOM	1711	C	LEU	B	11	−45.839	−29.819	113.059	1.00	29.19		C
ATOM	1712	O	LEU	B	11	−44.706	−29.647	112.600	1.00	31.16		O
ATOM	1713	CB	LEU	B	11	−46.954	−30.632	110.978	1.00	33.49		C
ATOM	1714	CG	LEU	B	11	−47.842	−31.847	110.756	1.00	40.86		C
ATOM	1715	CD1	LEU	B	11	−47.188	−32.642	109.625	1.00	33.69		C
ATOM	1716	CD2	LEU	B	11	−47.976	−32.687	112.003	1.00	34.11		C
ATOM	1717	N	SER	B	12	−46.055	−30.135	114.336	1.00	32.77		N
ATOM	1718	CA	SER	B	12	−44.956	−30.381	115.271	1.00	30.27		C
ATOM	1719	C	SER	B	12	−44.851	−31.873	115.562	1.00	30.86		C
ATOM	1720	O	SER	B	12	−45.793	−32.475	116.083	1.00	35.59		O
ATOM	1721	CB	SER	B	12	−45.145	−29.592	116.560	1.00	27.94		C
ATOM	1722	OG	SER	B	12	−45.372	−28.227	116.236	1.00	38.87		O
ATOM	1723	N	LEU	B	13	−43.694	−32.453	115.245	1.00	31.96		N
ATOM	1724	CA	LEU	B	13	−43.453	−33.887	115.299	1.00	32.10		C
ATOM	1725	C	LEU	B	13	−42.010	−34.098	115.707	1.00	30.66		C
ATOM	1726	O	LEU	B	13	−41.159	−33.231	115.489	1.00	31.40		O
ATOM	1727	CB	LEU	B	13	−43.690	−34.572	113.949	1.00	32.81		C
ATOM	1728	CG	LEU	B	13	−45.087	−34.460	113.332	1.00	34.52		C
ATOM	1729	CD1	LEU	B	13	−45.085	−35.018	111.924	1.00	32.83		C
ATOM	1730	CD2	LEU	B	13	−46.110	−35.164	114.189	1.00	26.42		C
ATOM	1731	N	SER	B	14	−41.745	−35.232	116.316	1.00	28.88		N
ATOM	1732	CA	SER	B	14	−40.359	−35.534	116.639	1.00	32.75		C
ATOM	1733	C	SER	B	14	−39.649	−36.161	115.442	1.00	28.56		C
ATOM	1734	O	SER	B	14	−40.281	−36.766	114.580	1.00	31.22		O
ATOM	1735	CB	SER	B	14	−40.292	−36.469	117.838	1.00	36.49		C
ATOM	1736	OG	SER	B	14	−40.626	−35.749	119.019	1.00	44.98		O
ATOM	1737	N	PRO	B	15	−38.341	−36.015	115.345	1.00	29.37		N
ATOM	1738	CA	PRO	B	15	−37.609	−36.799	114.341	1.00	28.36		C
ATOM	1739	C	PRO	B	15	−37.846	−38.290	114.566	1.00	33.54		C
ATOM	1740	O	PRO	B	15	−37.877	−38.770	115.702	1.00	39.74		O
ATOM	1741	CB	PRO	B	15	−36.149	−36.404	114.575	1.00	31.85		C
ATOM	1742	CG	PRO	B	15	−36.230	−35.042	115.265	1.00	27.05		C
ATOM	1743	CD	PRO	B	15	−37.481	−35.086	116.097	1.00	29.92		C
ATOM	1744	N	GLY	B	16	−37.994	−39.032	113.467	1.00	34.12		N
ATOM	1745	CA	GLY	B	16	−38.362	−40.428	113.500	1.00	30.27		C
ATOM	1746	C	GLY	B	16	−39.837	−40.693	113.284	1.00	32.66		C
ATOM	1747	O	GLY	B	16	−40.204	−41.796	112.862	1.00	38.35		O
ATOM	1748	N	GLU	B	17	−40.690	−39.722	113.549	1.00	28.58		N
ATOM	1749	CA	GLU	B	17	−42.105	−39.947	113.346	1.00	27.09		C
ATOM	1750	C	GLU	B	17	−42.502	−39.762	111.878	1.00	32.66		C
ATOM	1751	O	GLU	B	17	−41.728	−39.318	111.016	1.00	27.01		O
ATOM	1752	CB	GLU	B	17	−42.923	−39.013	114.220	1.00	26.44		C
ATOM	1753	CG	GLU	B	17	−42.896	−39.366	115.689	1.00	35.87		C
ATOM	1754	CD	GLU	B	17	−43.872	−38.506	116.494	1.00	50.33		C
ATOM	1755	OE1	GLU	B	17	−43.659	−37.269	116.602	1.00	47.95		O
ATOM	1756	OE2	GLU	B	17	−44.862	−39.066	117.011	1.00	67.19		O1−
ATOM	1757	N	ARG	B	18	−43.757	−40.098	111.626	1.00	28.24		N
ATOM	1758	CA	ARG	B	18	−44.377	−40.060	110.321	1.00	29.25		C
ATOM	1759	C	ARG	B	18	−45.174	−38.768	110.187	1.00	31.06		C
ATOM	1760	O	ARG	B	18	−45.801	−38.322	111.151	1.00	28.90		O
ATOM	1761	CB	ARG	B	18	−45.273	−41.278	110.169	1.00	28.93		C
ATOM	1762	CG	ARG	B	18	−46.000	−41.420	108.875	1.00	35.84		C
ATOM	1763	CD	ARG	B	18	−46.955	−42.591	109.004	1.00	33.74		C
ATOM	1764	NE	ARG	B	18	−47.724	−42.806	107.792	1.00	42.81		N
ATOM	1765	CZ	ARG	B	18	−47.249	−43.450	106.731	1.00	49.16		C
ATOM	1766	NH1	ARG	B	18	−45.993	−43.927	106.747	1.00	44.51		N1+
ATOM	1767	NH2	ARG	B	18	−48.021	−43.606	105.656	1.00	37.48		N
ATOM	1768	N	ALA	B	19	−45.104	−38.148	109.001	1.00	30.81		N
ATOM	1769	CA	ALA	B	19	−45.764	−36.880	108.699	1.00	27.46		C
ATOM	1770	C	ALA	B	19	−46.674	−37.020	107.488	1.00	27.67		C
ATOM	1771	O	ALA	B	19	−46.284	−37.594	106.466	1.00	29.51		O
ATOM	1772	CB	ALA	B	19	−44.745	−35.775	108.431	1.00	26.69		C
ATOM	1773	N	THR	B	20	−47.863	−36.437	107.576	1.00	23.65		N
ATOM	1774	CA	THR	B	20	−48.833	−36.478	106.489	1.00	28.01		C
ATOM	1775	C	THR	B	20	−49.374	−35.076	106.258	1.00	29.74		C
ATOM	1776	O	THR	B	20	−49.974	−34.477	107.155	1.00	31.62		O
ATOM	1777	CB	THR	B	20	−49.966	−37.477	106.791	1.00	31.91		C
ATOM	1778	OG1	THR	B	20	−49.516	−38.802	106.486	1.00	38.10		O
ATOM	1779	CG2	THR	B	20	−51.212	−37.192	105.973	1.00	31.11		C
ATOM	1780	N	LEU	B	21	−49.163	−34.561	105.054	1.00	28.91		N
ATOM	1781	CA	LEU	B	21	−49.541	−33.209	104.693	1.00	27.86		C
ATOM	1782	C	LEU	B	21	−50.689	−33.322	103.711	1.00	27.21		C
ATOM	1783	O	LEU	B	21	−50.742	−34.261	102.921	1.00	27.15		O
ATOM	1784	CB	LEU	B	21	−48.377	−32.459	104.031	1.00	24.41		C
ATOM	1785	CG	LEU	B	21	−46.975	−32.345	104.643	1.00	26.45		C
ATOM	1786	CD1	LEU	B	21	−46.405	−30.957	104.460	1.00	27.98		C
ATOM	1787	CD2	LEU	B	21	−46.871	−32.762	106.081	1.00	28.98		C
ATOM	1788	N	SER	B	22	−51.620	−32.390	103.764	1.00	27.44		N
ATOM	1789	CA	SER	B	22	−52.739	−32.439	102.843	1.00	27.56		C
ATOM	1790	C	SER	B	22	−52.718	−31.231	101.926	1.00	29.41		C
ATOM	1791	O	SER	B	22	−52.281	−30.148	102.321	1.00	23.55		O
ATOM	1792	CB	SER	B	22	−54.067	−32.506	103.571	1.00	22.71		C
ATOM	1793	OG	SER	B	22	−54.374	−33.869	103.733	1.00	40.86		O
ATOM	1794	N	CYS	B	23	−53.188	−31.445	100.693	1.00	24.46		N
ATOM	1795	CA	CYS	B	23	−53.456	−30.379	99.735	1.00	26.64		C
ATOM	1796	C	CYS	B	23	−54.824	−30.660	99.146	1.00	26.09		C
ATOM	1797	O	CYS	B	23	−55.034	−31.718	98.547	1.00	30.05		O
ATOM	1798	CB	CYS	B	23	−52.392	−30.330	98.623	1.00	29.42		C
ATOM	1799	SG	CYS	B	23	−52.509	−28.931	97.438	1.00	45.36		S
ATOM	1800	N	ARG	B	24	−55.756	−29.740	99.326	1.00	26.38		N
ATOM	1801	CA	ARG	B	24	−57.084	−29.874	98.762	1.00	25.14		C
ATOM	1802	C	ARG	B	24	−57.249	−28.870	97.633	1.00	27.66		C
ATOM	1803	O	ARG	B	24	−56.984	−27.677	97.815	1.00	27.74		O
ATOM	1804	CB	ARG	B	24	−58.151	−29.702	99.834	1.00	25.05		C
ATOM	1805	CG	ARG	B	24	−58.148	−30.888	100.781	1.00	39.63		C
ATOM	1806	CD	ARG	B	24	−58.919	−30.636	102.071	1.00	56.87		C
ATOM	1807	NE	ARG	B	24	−60.337	−30.971	101.921	1.00	70.81		N
ATOM	1808	CZ	ARG	B	24	−60.899	−32.091	102.373	1.00	75.66		C
ATOM	1809	NH1	ARG	B	24	−60.156	−32.994	103.017	1.00	74.34		N1+
ATOM	1810	NH2	ARG	B	24	−62.204	−32.303	102.187	1.00	69.31		N
ATOM	1811	N	ALA	B	25	−57.657	−29.371	96.465	1.00	25.97		N
ATOM	1812	CA	ALA	B	25	−57.809	−28.586	95.252	1.00	24.73		C
ATOM	1813	C	ALA	B	25	−59.271	−28.236	95.024	1.00	25.92		C
ATOM	1814	O	ALA	B	25	−60.147	−29.102	95.093	1.00	27.92		O
ATOM	1815	CB	ALA	B	25	−57.263	−29.344	94.042	1.00	25.78		C
ATOM	1816	N	SER	B	26	−59.524	−26.969	94.744	1.00	28.48		N
ATOM	1817	CA	SER	B	26	−60.840	−26.517	94.342	1.00	26.13		C
ATOM	1818	C	SER	B	26	−60.758	−25.481	93.190	1.00	29.42		C
ATOM	1819	O	SER	B	26	−60.242	−24.370	93.373	1.00	30.69		O
ATOM	1820	CB	SER	B	26	−61.562	−25.932	95.549	1.00	24.33		C
ATOM	1821	OG	SER	B	26	−62.823	−25.420	95.178	1.00	39.40		O
ATOM	1822	N	PRO	B	27	−61.248	−25.837	91.994	1.00	27.29		N
ATOM	1823	CA	PRO	B	27	−61.824	−27.118	91.541	1.00	25.37		C
ATOM	1824	C	PRO	B	27	−60.819	−28.258	91.496	1.00	27.72		C
ATOM	1825	O	PRO	B	27	−59.639	−28.025	91.702	1.00	28.26		O
ATOM	1826	CB	PRO	B	27	−62.331	−26.806	90.123	1.00	22.36		C
ATOM	1827	CG	PRO	B	27	−61.831	−25.420	89.788	1.00	21.74		C
ATOM	1828	CD	PRO	B	27	−61.584	−24.724	91.085	1.00	22.47		C
ATOM	1829	N	SER	B	28	−61.284	−29.468	91.201	1.00	29.06		N
ATOM	1830	CA	SER	B	28	−60.424	−30.643	91.235	1.00	29.98		C
ATOM	1831	C	SER	B	28	−59.291	−30.567	90.206	1.00	31.92		C
ATOM	1832	O	SER	B	28	−59.390	−29.898	89.174	1.00	33.40		O
ATOM	1833	CB	SER	B	28	−61.256	−31.892	90.993	1.00	30.66		C
ATOM	1834	OG	SER	B	28	−62.051	−32.132	92.124	1.00	36.68		O
ATOM	1835	N	VAL	B	29	−58.219	−31.314	90.488	1.00	29.10		N
ATOM	1836	CA	VAL	B	29	−57.081	−31.501	89.588	1.00	27.86		C
ATOM	1837	C	VAL	B	29	−57.110	−32.960	89.140	1.00	34.14		C
ATOM	1838	O	VAL	B	29	−56.339	−33.796	89.630	1.00	31.49		O
ATOM	1839	CB	VAL	B	29	−55.739	−31.126	90.270	1.00	26.93		C
ATOM	1840	CG1	VAL	B	29	−54.536	−31.343	89.352	1.00	31.84		C
ATOM	1841	CG2	VAL	B	29	−55.741	−29.679	90.699	1.00	27.83		C
ATOM	1842	N	ASN	B	30	−58.040	−33.287	88.234	1.00	37.48		N
ATOM	1843	CA	ASN	B	30	−58.225	−34.670	87.784	1.00	33.93		C
ATOM	1844	C	ASN	B	30	−57.128	−35.163	86.860	1.00	28.81		C
ATOM	1845	O	ASN	B	30	−57.130	−36.351	86.526	1.00	35.16		O
ATOM	1846	CB	ASN	B	30	−59.573	−34.847	87.088	1.00	30.66		C
ATOM	1847	CG	ASN	B	30	−60.750	−34.648	88.034	1.00	32.10		C
ATOM	1848	OD1	ASN	B	30	−60.735	−35.110	89.179	1.00	36.69		O
ATOM	1849	ND2	ASN	B	30	−61.763	−33.952	87.564	1.00	29.33		N
ATOM	1850	N	SER	B	31	−56.223	−34.293	86.406	1.00	30.18		N
ATOM	1851	CA	SER	B	31	−55.082	−34.759	85.625	1.00	28.46		C
ATOM	1852	C	SER	B	31	−54.004	−35.394	86.484	1.00	30.09		C
ATOM	1853	O	SER	B	31	−53.192	−36.163	85.956	1.00	25.87		O
ATOM	1854	CB	SER	B	31	−54.464	−33.608	84.839	1.00	28.04		C
ATOM	1855	OG	SER	B	31	−54.110	−32.544	85.699	1.00	28.97		O
ATOM	1856	N	GLY	B	32	−54.026	−35.129	87.797	1.00	30.79		N
ATOM	1857	CA	GLY	B	32	−52.930	−35.453	88.685	1.00	23.28		C
ATOM	1858	C	GLY	B	32	−51.708	−34.581	88.501	1.00	25.51		C
ATOM	1859	O	GLY	B	32	−50.636	−34.931	88.982	1.00	24.92		O
ATOM	1860	N	TYR	B	33	−51.838	−33.436	87.830	1.00	25.51		N
ATOM	1861	CA	TYR	B	33	−50.697	−32.549	87.607	1.00	22.85		C
ATOM	1862	C	TYR	B	33	−50.468	−31.718	88.875	1.00	28.41		C
ATOM	1863	O	TYR	B	33	−50.739	−30.514	88.938	1.00	24.46		O
ATOM	1864	CB	TYR	B	33	−50.934	−31.657	86.394	1.00	25.72		C
ATOM	1865	CG	TYR	B	33	−50.986	−32.351	85.031	1.00	27.40		C
ATOM	1866	CD1	TYR	B	33	−50.607	−33.684	84.869	1.00	25.12		C
ATOM	1867	CD2	TYR	B	33	−51.398	−31.651	83.901	1.00	25.37		C
ATOM	1868	CE1	TYR	B	33	−50.659	−34.306	83.618	1.00	27.61		C
ATOM	1869	CE2	TYR	B	33	−51.443	−32.256	82.647	1.00	28.75		C
ATOM	1870	CZ	TYR	B	33	−51.073	−33.582	82.505	1.00	31.43		C
ATOM	1871	OH	TYR	B	33	−51.108	−34.164	81.251	1.00	25.68		O
ATOM	1872	N	LEU	B	34	−49.964	−32.400	89.908	1.00	26.49		N
ATOM	1873	CA	LEU	B	34	−49.740	−31.801	91.217	1.00	25.62		C
ATOM	1874	C	LEU	B	34	−48.316	−32.075	91.697	1.00	25.75		C
ATOM	1875	O	LEU	B	34	−47.893	−33.228	91.789	1.00	27.99		O
ATOM	1876	CB	LEU	B	34	−50.742	−32.328	92.239	1.00	25.15		C
ATOM	1877	CG	LEU	B	34	−50.732	−31.388	93.436	1.00	22.33		C
ATOM	1878	CD1	LEU	B	34	−52.055	−30.748	93.532	1.00	24.71		C
ATOM	1879	CD2	LEU	B	34	−50.401	−32.127	94.682	1.00	22.19		C
ATOM	1880	N	ALA	B	35	−47.595	−31.021	92.035	1.00	26.54		N
ATOM	1881	CA	ALA	B	35	−46.221	−31.114	92.497	1.00	27.18		C
ATOM	1882	C	ALA	B	35	−46.154	−30.759	93.973	1.00	25.51		C
ATOM	1883	O	ALA	B	35	−47.050	−30.117	94.516	1.00	24.44		O
ATOM	1884	CB	ALA	B	35	−45.293	−30.186	91.706	1.00	20.44		C
ATOM	1885	N	TRP	B	36	−45.088	−31.214	94.621	1.00	23.22		N
ATOM	1886	CA	TRP	B	36	−44.790	−30.852	95.995	1.00	26.05		C
ATOM	1887	C	TRP	B	36	−43.368	−30.316	96.037	1.00	25.42		C
ATOM	1888	O	TRP	B	36	−42.462	−30.896	95.429	1.00	26.45		O
ATOM	1889	CB	TRP	B	36	−44.935	−32.050	96.966	1.00	23.50		C
ATOM	1890	CG	TRP	B	36	−46.328	−32.470	97.286	1.00	23.73		C
ATOM	1891	CD1	TRP	B	36	−47.071	−33.413	96.633	1.00	26.66		C
ATOM	1892	CD2	TRP	B	36	−47.144	−32.006	98.375	1.00	28.12		C
ATOM	1893	NE1	TRP	B	36	−48.304	−33.549	97.229	1.00	24.58		N
ATOM	1894	CE2	TRP	B	36	−48.374	−32.709	98.306	1.00	26.57		C
ATOM	1895	CE3	TRP	B	36	−46.951	−31.079	99.407	1.00	20.21		C
ATOM	1896	CZ2	TRP	B	36	−49.407	−32.506	99.222	1.00	22.88		C
ATOM	1897	CZ3	TRP	B	36	−47.970	−30.872	100.294	1.00	23.52		C
ATOM	1898	CH2	TRP	B	36	−49.190	−31.584	100.203	1.00	24.77		C
ATOM	1899	N	TYR	B	37	−43.173	−29.219	96.764	1.00	25.12		N
ATOM	1900	CA	TYR	B	37	−41.858	−28.628	96.947	1.00	23.85		C
ATOM	1901	C	TYR	B	37	−41.551	−28.525	98.427	1.00	27.32		C
ATOM	1902	O	TYR	B	37	−42.446	−28.279	99.247	1.00	28.76		O
ATOM	1903	CB	TYR	B	37	−41.764	−27.229	96.341	1.00	25.99		C
ATOM	1904	CG	TYR	B	37	−42.052	−27.217	94.879	1.00	25.68		C
ATOM	1905	CD2	TYR	B	37	−41.025	−27.346	93.944	1.00	27.12		C
ATOM	1906	CD1	TYR	B	37	−43.346	−27.106	94.426	1.00	20.71		C
ATOM	1907	CE2	TYR	B	37	−41.296	−27.349	92.584	1.00	23.06		C
ATOM	1908	CE1	TYR	B	37	−43.622	−27.112	93.088	1.00	25.67		C
ATOM	1909	CZ	TYR	B	37	−42.598	−27.241	92.170	1.00	22.19		C
ATOM	1910	OH	TYR	B	37	−42.911	−27.244	90.831	1.00	28.45		O
ATOM	1911	N	GLN	B	38	−40.267	−28.679	98.742	1.00	24.78		N
ATOM	1912	CA	GLN	B	38	−39.708	−28.428	100.061	1.00	26.12		C
ATOM	1913	C	GLN	B	38	−38.871	−27.147	100.017	1.00	23.99		C
ATOM	1914	O	GLN	B	38	−38.168	−26.890	99.034	1.00	22.68		O
ATOM	1915	CB	GLN	B	38	−38.852	−29.619	100.509	1.00	24.24		C
ATOM	1916	CG	GLN	B	38	−38.144	−29.399	101.826	1.00	22.10		C
ATOM	1917	CD	GLN	B	38	−37.108	−30.460	102.113	1.00	26.91		C
ATOM	1918	OE1	GLN	B	38	−36.023	−30.439	101.532	1.00	33.75		O
ATOM	1919	NE2	GLN	B	38	−37.418	−31.376	103.032	1.00	24.91		N
ATOM	1920	N	GLN	B	39	−38.944	−26.339	101.072	1.00	19.06		N
ATOM	1921	CA	GLN	B	39	−38.193	−25.085	101.113	1.00	24.00		C
ATOM	1922	C	GLN	B	39	−37.632	−24.846	102.498	1.00	23.43		C
ATOM	1923	O	GLN	B	39	−38.389	−24.722	103.462	1.00	21.25		O
ATOM	1924	CB	GLN	B	39	−39.043	−23.881	100.719	1.00	25.47		C
ATOM	1925	CG	GLN	B	39	−38.226	−22.610	100.620	1.00	25.34		C
ATOM	1926	CD	GLN	B	39	−39.027	−21.423	100.161	1.00	31.02		C
ATOM	1927	OE1	GLN	B	39	−40.183	−21.244	100.538	1.00	34.04		O
ATOM	1928	NE2	GLN	B	39	−38.418	−20.601	99.334	1.00	33.16		N
ATOM	1929	N	LYS	B	40	−36.319	−24.712	102.575	1.00	25.20		N
ATOM	1930	CA	LYS	B	40	−35.694	−24.322	103.822	1.00	25.84		C
ATOM	1931	C	LYS	B	40	−35.497	−22.813	103.870	1.00	27.20		C
ATOM	1932	O	LYS	B	40	−35.478	−22.145	102.827	1.00	26.37		O
ATOM	1933	CB	LYS	B	40	−34.382	−25.077	103.991	1.00	27.92		C
ATOM	1934	CG	LYS	B	40	−34.624	−26.487	104.544	1.00	30.32		C
ATOM	1935	CD	LYS	B	40	−33.459	−27.416	104.259	1.00	42.40		C
ATOM	1936	CE	LYS	B	40	−33.761	−28.834	104.704	1.00	39.36		C
ATOM	1937	NZ	LYS	B	40	−33.984	−28.911	106.185	1.00	42.39		N1+
ATOM	1938	N	PRO	B	41	−35.419	−22.231	105.072	1.00	28.86		N
ATOM	1939	CA	PRO	B	41	−35.467	−20.757	105.192	1.00	27.65		C
ATOM	1940	C	PRO	B	41	−34.345	−20.077	104.416	1.00	27.79		C
ATOM	1941	O	PRO	B	41	−33.168	−20.420	104.558	1.00	30.55		O
ATOM	1942	CB	PRO	B	41	−35.331	−20.523	106.701	1.00	25.62		C
ATOM	1943	CG	PRO	B	41	−35.861	−21.785	107.321	1.00	23.53		C
ATOM	1944	CD	PRO	B	41	−35.415	−22.885	106.393	1.00	22.03		C
ATOM	1945	N	GLY	B	42	−34.724	−19.113	103.577	1.00	30.24		N
ATOM	1946	CA	GLY	B	42	−33.743	−18.444	102.750	1.00	26.94		C
ATOM	1947	C	GLY	B	42	−33.131	−19.294	101.657	1.00	34.34		C
ATOM	1948	O	GLY	B	42	−32.033	−18.976	101.191	1.00	29.82		O
ATOM	1949	N	GLN	B	43	−33.790	−20.388	101.254	1.00	29.49		N
ATOM	1950	CA	GLN	B	43	−33.330	−21.236	100.164	1.00	29.08		C
ATOM	1951	C	GLN	B	43	−34.400	−21.299	99.086	1.00	26.57		C
ATOM	1952	O	GLN	B	43	−35.578	−21.019	99.329	1.00	28.43		O
ATOM	1953	CB	GLN	B	43	−32.994	−22.665	100.622	1.00	33.38		C
ATOM	1954	CG	GLN	B	43	−32.182	−22.796	101.894	1.00	31.30		C
ATOM	1955	CD	GLN	B	43	−30.769	−22.262	101.737	1.00	45.21		C
ATOM	1956	OE1	GLN	B	43	−30.173	−22.361	100.665	1.00	48.17		O
ATOM	1957	NE2	GLN	B	43	−30.215	−21.713	102.818	1.00	50.07		N
ATOM	1958	N	THR	B	44	−33.988	−21.698	97.895	1.00	28.06		N
ATOM	1959	CA	THR	B	44	−34.976	−21.828	96.832	1.00	32.50		C
ATOM	1960	C	THR	B	44	−35.755	−23.142	97.000	1.00	29.43		C
ATOM	1961	O	THR	B	44	−35.282	−24.077	97.652	1.00	28.21		O
ATOM	1962	CB	THR	B	44	−34.303	−21.769	95.453	1.00	28.68		C
ATOM	1963	OG1	THR	B	44	−33.844	−23.064	95.087	1.00	33.54		O
ATOM	1964	CG2	THR	B	44	−33.095	−20.847	95.473	1.00	35.23		C
ATOM	1965	N	PRO	B	45	−36.982	−23.217	96.495	1.00	29.94		N
ATOM	1966	CA	PRO	B	45	−37.745	−24.456	96.658	1.00	27.80		C
ATOM	1967	C	PRO	B	45	−37.021	−25.614	95.982	1.00	24.29		C
ATOM	1968	O	PRO	B	45	−36.256	−25.428	95.042	1.00	28.45		O
ATOM	1969	CB	PRO	B	45	−39.079	−24.140	95.967	1.00	26.59		C
ATOM	1970	CG	PRO	B	45	−39.175	−22.670	95.983	1.00	23.14		C
ATOM	1971	CD	PRO	B	45	−37.774	−22.177	95.813	1.00	27.43		C
ATOM	1972	N	ARG	B	46	−37.249	−26.817	96.485	1.00	24.84		N
ATOM	1973	CA	ARG	B	46	−36.741	−28.036	95.863	1.00	27.05		C
ATOM	1974	C	ARG	B	46	−37.920	−28.935	95.516	1.00	28.13		C
ATOM	1975	O	ARG	B	46	−38.743	−29.258	96.385	1.00	27.30		O
ATOM	1976	CB	ARG	B	46	−35.754	−28.763	96.782	1.00	27.57		C
ATOM	1977	CG	ARG	B	46	−35.323	−30.144	96.305	1.00	35.27		C
ATOM	1978	CD	ARG	B	46	−34.354	−30.799	97.302	1.00	42.68		C
ATOM	1979	NE	ARG	B	46	−33.035	−30.146	97.316	1.00	59.78		N
ATOM	1980	CZ	ARG	B	46	−32.623	−29.218	98.197	1.00	64.38		C
ATOM	1981	NH1	ARG	B	46	−33.408	−28.780	99.199	1.00	56.48		N1+
ATOM	1982	NH2	ARG	B	46	−31.399	−28.715	98.076	1.00	61.89		N
ATOM	1983	N	LEU	B	47	−38.007	−29.318	94.244	1.00	28.50		N
ATOM	1984	CA	LEU	B	47	−39.058	−30.216	93.781	1.00	25.28		C
ATOM	1985	C	LEU	B	47	−38.930	−31.576	94.455	1.00	25.95		C
ATOM	1986	O	LEU	B	47	−37.851	−32.175	94.457	1.00	30.65		O
ATOM	1987	CB	LEU	B	47	−38.970	−30.365	92.262	1.00	27.11		C
ATOM	1988	CG	LEU	B	47	−39.935	−31.368	91.643	1.00	27.81		C
ATOM	1989	CD1	LEU	B	47	−41.357	−30.870	91.856	1.00	21.28		C
ATOM	1990	CD2	LEU	B	47	−39.622	−31.533	90.175	1.00	24.15		C
ATOM	1991	N	LEU	B	48	−40.027	−32.055	95.040	1.00	22.73		N
ATOM	1992	CA	LEU	B	48	−40.056	−33.353	95.715	1.00	28.05		C
ATOM	1993	C	LEU	B	48	−40.844	−34.397	94.953	1.00	30.46		C
ATOM	1994	O	LEU	B	48	−40.406	−35.548	94.862	1.00	28.89		O
ATOM	1995	CB	LEU	B	48	−40.685	−33.237	97.112	1.00	29.74		C
ATOM	1996	CG	LEU	B	48	−40.032	−32.529	98.287	1.00	28.54		C
ATOM	1997	CD1	LEU	B	48	−40.954	−32.632	99.462	1.00	25.93		C
ATOM	1998	CD2	LEU	B	48	−38.712	−33.198	98.616	1.00	30.43		C
ATOM	1999	N	ILE	B	49	−42.012	−33.999	94.435	1.00	26.40		N
ATOM	2000	CA	ILE	B	49	−42.988	−34.879	93.804	1.00	26.75		C
ATOM	2001	C	ILE	B	49	−43.560	−34.161	92.594	1.00	24.70		C
ATOM	2002	O	ILE	B	49	−43.809	−32.958	92.648	1.00	22.99		O
ATOM	2003	CB	ILE	B	49	−44.129	−35.264	94.780	1.00	26.52		C
ATOM	2004	CG1	ILE	B	49	−43.583	−35.980	96.018	1.00	21.26		C
ATOM	2005	CG2	ILE	B	49	−45.215	−36.049	94.058	1.00	20.52		C
ATOM	2006	CD1	ILE	B	49	−43.212	−37.429	95.770	1.00	22.03		C
ATOM	2007	N	PHE	B	50	−43.749	−34.888	91.491	1.00	26.33		N
ATOM	2008	CA	PHE	B	50	−44.548	−34.395	90.375	1.00	26.42		C
ATOM	2009	C	PHE	B	50	−45.564	−35.460	89.959	1.00	30.44		C
ATOM	2010	O	PHE	B	50	−45.467	−36.634	90.342	1.00	27.91		O
ATOM	2011	CB	PHE	B	50	−43.678	−33.982	89.184	1.00	21.93		C
ATOM	2012	CG	PHE	B	50	−42.877	−35.114	88.610	1.00	30.11		C
ATOM	2013	CD1	PHE	B	50	−43.407	−35.919	87.609	1.00	27.24		C
ATOM	2014	CD2	PHE	B	50	−41.599	−35.383	89.079	1.00	28.83		C
ATOM	2015	CE1	PHE	B	50	−42.682	−36.965	87.085	1.00	34.14		C
ATOM	2016	CE2	PHE	B	50	−40.865	−36.430	88.547	1.00	34.66		C
ATOM	2017	CZ	PHE	B	50	−41.409	−37.230	87.553	1.00	31.45		C
ATOM	2018	N	GLY	B	51	−46.579	−35.022	89.216	1.00	29.06		N
ATOM	2019	CA	GLY	B	51	−47.640	−35.920	88.790	1.00	23.55		C
ATOM	2020	C	GLY	B	51	−48.357	−36.601	89.926	1.00	28.78		C
ATOM	2021	O	GLY	B	51	−48.771	−37.758	89.789	1.00	31.77		O
ATOM	2022	N	ALA	B	52	−48.497	−35.913	91.057	1.00	27.54		N
ATOM	2023	CA	ALA	B	52	−49.180	−36.389	92.253	1.00	27.65		C
ATOM	2024	C	ALA	B	52	−48.403	−37.468	92.995	1.00	27.89		C
ATOM	2025	O	ALA	B	52	−48.422	−37.465	94.231	1.00	25.68		O
ATOM	2026	CB	ALA	B	52	−50.589	−36.907	91.927	1.00	24.96		C
ATOM	2027	N	SER	B	53	−47.679	−38.358	92.289	1.00	24.53		N
ATOM	2028	CA	SER	B	53	−47.036	−39.468	93.002	1.00	27.35		C
ATOM	2029	C	SER	B	53	−45.606	−39.792	92.588	1.00	30.40		C
ATOM	2030	O	SER	B	53	−44.970	−40.616	93.257	1.00	31.18		O
ATOM	2031	CB	SER	B	53	−47.855	−40.745	92.844	1.00	27.15		C
ATOM	2032	OG	SER	B	53	−48.178	−40.933	91.485	1.00	33.66		O
ATOM	2033	N	SER	B	54	−45.082	−39.207	91.526	1.00	27.47		N
ATOM	2034	CA	SER	B	54	−43.758	−39.568	91.050	1.00	28.53		C
ATOM	2035	C	SER	B	54	−42.717	−38.787	91.833	1.00	28.97		C
ATOM	2036	O	SER	B	54	−42.754	−37.552	91.877	1.00	29.74		O
ATOM	2037	CB	SER	B	54	−43.621	−39.289	89.556	1.00	27.68		C
ATOM	2038	OG	SER	B	54	−44.449	−40.156	88.815	1.00	33.67		O
ATOM	2039	N	ARG	B	55	−41.795	−39.519	92.432	1.00	27.26		N
ATOM	2040	CA	ARG	B	55	−40.657	−38.955	93.138	1.00	32.14		C
ATOM	2041	C	ARG	B	55	−39.710	−38.275	92.152	1.00	30.42		C
ATOM	2042	O	ARG	B	55	−39.438	−38.817	91.084	1.00	34.35		O
ATOM	2043	CB	ARG	B	55	−39.955	−40.099	93.864	1.00	28.20		C
ATOM	2044	CG	ARG	B	55	−39.168	−39.786	95.061	1.00	33.52		C
ATOM	2045	CD	ARG	B	55	−38.583	−41.090	95.651	1.00	37.14		C
ATOM	2046	NE	ARG	B	55	−39.581	−41.791	96.442	1.00	41.03		N
ATOM	2047	CZ	ARG	B	55	−40.134	−42.948	96.118	1.00	41.47		C
ATOM	2048	NH1	ARG	B	55	−41.056	−43.474	96.923	1.00	39.94		N1+
ATOM	2049	NH2	ARG	B	55	−39.756	−43.579	95.009	1.00	39.66		N
ATOM	2050	N	ALA	B	56	−39.246	−37.068	92.483	1.00	32.10		N
ATOM	2051	CA	ALA	B	56	−38.216	−36.416	91.686	1.00	34.96		C
ATOM	2052	C	ALA	B	56	−36.843	−37.013	91.987	1.00	37.35		C
ATOM	2053	O	ALA	B	56	−36.647	−37.718	92.975	1.00	43.05		O
ATOM	2054	CB	ALA	B	56	−38.183	−34.911	91.952	1.00	30.18		C
ATOM	2055	N	THR	B	57	−35.892	−36.740	91.111	1.00	37.37		N
ATOM	2056	CA	THR	B	57	−34.521	−37.183	91.324	1.00	38.34		C
ATOM	2057	C	THR	B	57	−33.836	−36.270	92.313	1.00	39.91		C
ATOM	2058	O	THR	B	57	−34.179	−35.087	92.386	1.00	46.64		O
ATOM	2059	CB	THR	B	57	−33.716	−37.185	90.020	1.00	45.59		C
ATOM	2060	OG1	THR	B	57	−34.516	−36.612	88.969	1.00	40.75		O
ATOM	2061	CG2	THR	B	57	−33.271	−38.620	89.674	1.00	44.70		C
ATOM	2062	N	GLY	B	58	−32.937	−36.780	93.143	1.00	39.76		N
ATOM	2063	CA	GLY	B	58	−32.957	−38.118	93.653	1.00	35.82		C
ATOM	2064	C	GLY	B	58	−33.485	−37.854	95.061	1.00	40.59		C
ATOM	2065	O	GLY	B	58	−32.728	−37.724	96.021	1.00	37.19		O
ATOM	2066	N	ILE	B	59	−34.798	−37.704	95.160	1.00	33.85		N
ATOM	2067	CA	ILE	B	59	−35.455	−37.513	96.450	1.00	31.14		C
ATOM	2068	C	ILE	B	59	−35.518	−38.865	97.158	1.00	38.31		C
ATOM	2069	O	ILE	B	59	−35.890	−39.859	96.524	1.00	35.35		O
ATOM	2070	CB	ILE	B	59	−36.855	−36.904	96.264	1.00	29.49		C
ATOM	2071	CG1	ILE	B	59	−36.817	−35.375	96.109	1.00	29.46		C
ATOM	2072	CG2	ILE	B	59	−37.756	−37.240	97.420	1.00	30.78		C
ATOM	2073	CD1	ILE	B	59	−35.937	−34.826	95.062	1.00	37.31		C
ATOM	2074	N	PRO	B	60	−35.097	−38.960	98.459	1.00	38.88		N
ATOM	2075	CA	PRO	B	60	−35.157	−40.238	99.191	1.00	33.20		C
ATOM	2076	C	PRO	B	60	−36.530	−40.890	99.128	1.00	36.41		C
ATOM	2077	O	PRO	B	60	−37.527	−40.200	98.889	1.00	37.79		O
ATOM	2078	CB	PRO	B	60	−34.831	−39.817	100.629	1.00	34.92		C
ATOM	2079	CG	PRO	B	60	−34.076	−38.600	100.501	1.00	30.53		C
ATOM	2080	CD	PRO	B	60	−34.609	−37.876	99.320	1.00	31.01		C
ATOM	2081	N	ASP	B	61	−36.626	−42.202	99.320	1.00	33.86		N
ATOM	2082	CA	ASP	B	61	−37.968	−42.778	99.248	1.00	38.89		C
ATOM	2083	C	ASP	B	61	−38.762	−42.694	100.558	1.00	33.94		C
ATOM	2084	O	ASP	B	61	−39.868	−43.244	100.610	1.00	36.31		O
ATOM	2085	CB	ASP	B	61	−37.897	−44.220	98.751	1.00	43.25		C
ATOM	2086	CG	ASP	B	61	−36.955	−45.052	99.542	1.00	47.58		C
ATOM	2087	OD1	ASP	B	61	−36.741	−44.735	100.731	1.00	49.56		O
ATOM	2088	OD2	ASP	B	61	−36.427	−46.029	98.972	1.00	65.96		O1−
ATOM	2089	N	ARG	B	62	−38.222	−42.061	101.609	1.00	32.55		N
ATOM	2090	CA	ARG	B	62	−39.015	−41.532	102.717	1.00	32.36		C
ATOM	2091	C	ARG	B	62	−40.241	−40.805	102.198	1.00	29.63		C
ATOM	2092	O	ARG	B	62	−41.318	−40.850	102.794	1.00	30.70		O
ATOM	2093	CB	ARG	B	62	−38.243	−40.501	103.536	1.00	35.05		C
ATOM	2094	CG	ARG	B	62	−37.041	−40.958	104.180	1.00	36.82		C
ATOM	2095	CD	ARG	B	62	−36.754	−40.043	105.334	1.00	38.78		C
ATOM	2096	NE	ARG	B	62	−36.191	−38.739	105.001	1.00	39.12		N
ATOM	2097	CZ	ARG	B	62	−35.001	−38.571	104.422	1.00	39.01		C
ATOM	2098	NH1	ARG	B	62	−34.289	−39.630	104.056	1.00	36.63		N1+
ATOM	2099	NH2	ARG	B	62	−34.530	−37.352	104.195	1.00	33.11		N
ATOM	2100	N	PHE	B	63	−40.042	−40.074	101.115	1.00	31.12		N
ATOM	2101	CA	PHE	B	63	−41.075	−39.242	100.534	1.00	35.11		C
ATOM	2102	C	PHE	B	63	−41.916	−40.080	99.586	1.00	34.68		C
ATOM	2103	O	PHE	B	63	−41.373	−40.790	98.729	1.00	30.34		O
ATOM	2104	CB	PHE	B	63	−40.444	−38.054	99.803	1.00	27.94		C
ATOM	2105	CG	PHE	B	63	−39.701	−37.135	100.713	1.00	28.72		C
ATOM	2106	CD1	PHE	B	63	−38.408	−37.425	101.099	1.00	31.44		C
ATOM	2107	CD2	PHE	B	63	−40.308	−36.008	101.227	1.00	30.94		C
ATOM	2108	CE1	PHE	B	63	−37.731	−36.592	101.968	1.00	33.00		C
ATOM	2109	CE2	PHE	B	63	−39.630	−35.178	102.097	1.00	29.25		C
ATOM	2110	CZ	PHE	B	63	−38.344	−35.471	102.464	1.00	27.63		C
ATOM	2111	N	SER	B	64	−43.235	−40.023	99.775	1.00	30.03		N
ATOM	2112	CA	SER	B	64	−44.181	−40.581	98.819	1.00	30.73		C
ATOM	2113	C	SER	B	64	−45.432	−39.715	98.844	1.00	27.36		C
ATOM	2114	O	SER	B	64	−45.684	−38.974	99.796	1.00	25.57		O
ATOM	2115	CB	SER	B	64	−44.501	−42.064	99.109	1.00	28.95		C
ATOM	2116	OG	SER	B	64	−45.445	−42.217	100.156	1.00	29.24		O
ATOM	2117	N	ALA	B	65	−46.221	−39.806	97.784	1.00	26.92		N
ATOM	2118	CA	ALA	B	65	−47.407	−38.974	97.723	1.00	30.37		C
ATOM	2119	C	ALA	B	65	−48.448	−39.670	96.870	1.00	30.47		C
ATOM	2120	O	ALA	B	65	−48.134	−40.578	96.096	1.00	31.92		O
ATOM	2121	CB	ALA	B	65	−47.087	−37.583	97.157	1.00	26.67		C
ATOM	2122	N	SER	B	66	−49.692	−39.216	97.007	1.00	27.32		N
ATOM	2123	CA	SER	B	66	−50.792	−39.781	96.242	1.00	30.42		C
ATOM	2124	C	SER	B	66	−51.978	−38.825	96.278	1.00	27.86		C
ATOM	2125	O	SER	B	66	−51.955	−37.788	96.938	1.00	30.99		O
ATOM	2126	CB	SER	B	66	−51.165	−41.164	96.778	1.00	32.05		C
ATOM	2127	OG	SER	B	66	−51.732	−41.026	98.065	1.00	42.20		O
ATOM	2128	N	GLY	B	67	−53.025	−39.190	95.559	1.00	32.79		N
ATOM	2129	CA	GLY	B	67	−54.256	−38.435	95.552	1.00	28.74		C
ATOM	2130	C	GLY	B	67	−54.669	−38.125	94.138	1.00	34.13		C
ATOM	2131	O	GLY	B	67	−53.835	−38.175	93.223	1.00	38.32		O
ATOM	2132	N	SER	B	68	−55.943	−37.795	93.936	1.00	35.14		N
ATOM	2133	CA	SER	B	68	−56.352	−37.221	92.663	1.00	35.12		C
ATOM	2134	C	SER	B	68	−57.678	−36.522	92.863	1.00	35.78		C
ATOM	2135	O	SER	B	68	−58.409	−36.804	93.810	1.00	40.40		O
ATOM	2136	CB	SER	B	68	−56.473	−38.268	91.551	1.00	42.92		C
ATOM	2137	OG	SER	B	68	−56.634	−37.637	90.276	1.00	47.38		O
ATOM	2138	N	GLY	B	69	−57.990	−35.635	91.924	1.00	38.09		N
ATOM	2139	CA	GLY	B	69	−59.167	−34.812	91.999	1.00	27.17		C
ATOM	2140	C	GLY	B	69	−59.015	−33.747	93.048	1.00	30.94		C
ATOM	2141	O	GLY	B	69	−58.281	−32.775	92.867	1.00	32.99		O
ATOM	2142	N	ALA	B	70	−59.712	−33.901	94.161	1.00	36.50		N
ATOM	2143	CA	ALA	B	70	−59.738	−32.812	95.113	1.00	33.81		C
ATOM	2144	C	ALA	B	70	−58.726	−32.974	96.231	1.00	32.23		C
ATOM	2145	O	ALA	B	70	−58.401	−31.980	96.877	1.00	32.47		O
ATOM	2146	CB	ALA	B	70	−61.137	−32.661	95.704	1.00	27.91		C
ATOM	2147	N	ASP	B	71	−58.216	−34.184	96.471	1.00	28.53		N
ATOM	2148	CA	ASP	B	71	−57.431	−34.467	97.669	1.00	32.89		C
ATOM	2149	C	ASP	B	71	−56.068	−35.055	97.343	1.00	29.82		C
ATOM	2150	O	ASP	B	71	−55.966	−36.028	96.596	1.00	32.00		O
ATOM	2151	CB	ASP	B	71	−58.176	−35.394	98.631	1.00	29.01		C
ATOM	2152	CG	ASP	B	71	−59.067	−34.621	99.579	1.00	49.76		C
ATOM	2153	OD1	ASP	B	71	−58.492	−34.037	100.529	1.00	51.82		O
ATOM	2154	OD2	ASP	B	71	−60.313	−34.586	99.395	1.00	55.52		O1−
ATOM	2155	N	PHE	B	72	−55.023	−34.452	97.915	1.00	28.01		N
ATOM	2156	CA	PHE	B	72	−53.651	−34.911	97.756	1.00	26.76		C
ATOM	2157	C	PHE	B	72	−52.964	−34.963	99.110	1.00	24.59		C
ATOM	2158	O	PHE	B	72	−53.217	−34.129	99.987	1.00	27.45		O
ATOM	2159	CB	PHE	B	72	−52.889	−34.002	96.778	1.00	29.56		C
ATOM	2160	CG	PHE	B	72	−53.477	−34.000	95.391	1.00	29.36		C
ATOM	2161	CD1	PHE	B	72	−54.491	−33.128	95.058	1.00	29.76		C
ATOM	2162	CD2	PHE	B	72	−53.050	−34.917	94.441	1.00	28.24		C
ATOM	2163	CE1	PHE	B	72	−55.056	−33.152	93.790	1.00	33.06		C
ATOM	2164	CE2	PHE	B	72	−53.606	−34.935	93.163	1.00	29.21		C
ATOM	2165	CZ	PHE	B	72	−54.619	−34.058	92.846	1.00	27.62		C
ATOM	2166	N	THR	B	73	−52.117	−35.955	99.300	1.00	20.91		N
ATOM	2167	CA	THR	B	73	−51.335	−36.002	100.516	1.00	24.42		C
ATOM	2168	C	THR	B	73	−49.884	−36.323	100.180	1.00	25.69		C
ATOM	2169	O	THR	B	73	−49.583	−37.044	99.216	1.00	24.83		O
ATOM	2170	CB	THR	B	73	−51.917	−37.002	101.553	1.00	23.96		C
ATOM	2171	OG1	THR	B	73	−51.922	−38.307	101.005	1.00	31.75		O
ATOM	2172	CG2	THR	B	73	−53.357	−36.634	101.919	1.00	29.11		C
ATOM	2173	N	LEU	B	74	−48.989	−35.720	100.963	1.00	25.80		N
ATOM	2174	CA	LEU	B	74	−47.565	−36.023	100.955	1.00	26.02		C
ATOM	2175	C	LEU	B	74	−47.252	−36.738	102.262	1.00	25.39		C
ATOM	2176	O	LEU	B	74	−47.701	−36.303	103.322	1.00	25.96		O
ATOM	2177	CB	LEU	B	74	−46.730	−34.747	100.811	1.00	22.71		C
ATOM	2178	CG	LEU	B	74	−45.217	−34.943	100.997	1.00	27.97		C
ATOM	2179	CD1	LEU	B	74	−44.602	−35.660	99.806	1.00	23.58		C
ATOM	2180	CD2	LEU	B	74	−44.486	−33.635	101.264	1.00	25.42		C
ATOM	2181	N	THR	B	75	−46.551	−37.866	102.182	1.00	25.21		N
ATOM	2182	CA	THR	B	75	−46.187	−38.649	103.358	1.00	24.77		C
ATOM	2183	C	THR	B	75	−44.676	−38.773	103.458	1.00	29.94		C
ATOM	2184	O	THR	B	75	−44.012	−39.180	102.496	1.00	30.23		O
ATOM	2185	CB	THR	B	75	−46.830	−40.040	103.345	1.00	27.93		C
ATOM	2186	OG1	THR	B	75	−48.185	−39.936	103.785	1.00	33.93		O
ATOM	2187	CG2	THR	B	75	−46.105	−40.998	104.261	1.00	32.07		C
ATOM	2188	N	ILE	B	76	−44.145	−38.402	104.621	1.00	29.36		N
ATOM	2189	CA	ILE	B	76	−42.760	−38.649	105.003	1.00	29.13		C
ATOM	2190	C	ILE	B	76	−42.807	−39.727	106.074	1.00	29.72		C
ATOM	2191	O	ILE	B	76	−43.436	−39.537	107.122	1.00	30.62		O
ATOM	2192	CB	ILE	B	76	−42.070	−37.369	105.508	1.00	26.60		C
ATOM	2193	CG1	ILE	B	76	−42.336	−36.210	104.551	1.00	32.41		C
ATOM	2194	CG2	ILE	B	76	−40.581	−37.563	105.617	1.00	24.68		C
ATOM	2195	CD1	ILE	B	76	−41.949	−34.861	105.118	1.00	27.44		C
ATOM	2196	N	SER	B	77	−42.195	−40.878	105.798	1.00	31.29		N
ATOM	2197	CA	SER	B	77	−42.453	−42.041	106.645	1.00	34.52		C
ATOM	2198	C	SER	B	77	−41.647	−42.001	107.937	1.00	36.39		C
ATOM	2199	O	SER	B	77	−42.148	−42.404	108.994	1.00	42.84		O
ATOM	2200	CB	SER	B	77	−42.183	−43.327	105.871	1.00	28.00		C
ATOM	2201	OG	SER	B	77	−40.838	−43.394	105.441	1.00	30.78		O
ATOM	2202	N	ARG	B	78	−40.419	−41.502	107.873	1.00	29.86		N
ATOM	2203	CA	ARG	B	78	−39.567	−41.274	109.032	1.00	29.69		C
ATOM	2204	C	ARG	B	78	−38.973	−39.882	108.882	1.00	32.92		C
ATOM	2205	O	ARG	B	78	−38.317	−39.601	107.879	1.00	33.41		O
ATOM	2206	CB	ARG	B	78	−38.467	−42.342	109.133	1.00	39.68		C
ATOM	2207	CG	ARG	B	78	−37.255	−41.895	109.982	1.00	45.90		C
ATOM	2208	CD	ARG	B	78	−36.191	−42.997	110.245	1.00	50.49		C
ATOM	2209	NE	ARG	B	78	−35.401	−42.741	111.473	1.00	56.24		N
ATOM	2210	CZ	ARG	B	78	−35.796	−43.031	112.717	1.00	51.76		C
ATOM	2211	NH1	ARG	B	78	−35.013	−42.754	113.768	1.00	42.94		N1+
ATOM	2212	NH2	ARG	B	78	−36.989	−43.591	112.915	1.00	53.21		N
ATOM	2213	N	LEU	B	79	−39.284	−38.987	109.813	1.00	33.51		N
ATOM	2214	CA	LEU	B	79	−38.785	−37.612	109.757	1.00	30.48		C
ATOM	2215	C	LEU	B	79	−37.289	−37.545	110.092	1.00	31.79		C
ATOM	2216	O	LEU	B	79	−36.893	−37.791	111.233	1.00	34.10		O
ATOM	2217	CB	LEU	B	79	−39.590	−36.756	110.722	1.00	29.33		C
ATOM	2218	CG	LEU	B	79	−40.492	−35.683	110.136	1.00	29.23		C
ATOM	2219	CD1	LEU	B	79	−40.779	−35.916	108.706	1.00	23.33		C
ATOM	2220	CD2	LEU	B	79	−41.769	−35.681	110.920	1.00	27.74		C
ATOM	2221	N	GLU	B	80	−36.439	−37.169	109.109	1.00	32.68		N
ATOM	2222	CA	GLU	B	80	−35.028	−36.892	109.360	1.00	33.86		C
ATOM	2223	C	GLU	B	80	−34.836	−35.408	109.665	1.00	35.88		C
ATOM	2224	O	GLU	B	80	−35.701	−34.593	109.339	1.00	34.51		O
ATOM	2225	CB	GLU	B	80	−34.186	−37.294	108.144	1.00	36.87		C
ATOM	2226	CG	GLU	B	80	−34.116	−38.792	107.876	1.00	36.11		C
ATOM	2227	CD	GLU	B	80	−33.480	−39.579	109.018	1.00	45.93		C
ATOM	2228	OE1	GLU	B	80	−33.946	−40.719	109.264	1.00	47.66		O
ATOM	2229	OE2	GLU	B	80	−32.553	−39.050	109.696	1.00	47.84		O1−
ATOM	2230	N	PRO	B	81	−33.719	−35.014	110.302	1.00	38.88		N
ATOM	2231	CA	PRO	B	81	−33.544	−33.588	110.659	1.00	34.21		C
ATOM	2232	C	PRO	B	81	−33.719	−32.635	109.488	1.00	36.66		C
ATOM	2233	O	PRO	B	81	−34.340	−31.574	109.634	1.00	35.85		O
ATOM	2234	CB	PRO	B	81	−32.112	−33.540	111.209	1.00	41.16		C
ATOM	2235	CG	PRO	B	81	−31.881	−34.922	111.747	1.00	43.24		C
ATOM	2236	CD	PRO	B	81	−32.600	−35.843	110.790	1.00	43.50		C
ATOM	2237	N	GLU	B	82	−33.190	−32.994	108.325	1.00	33.34		N
ATOM	2238	CA	GLU	B	82	−33.310	−32.225	107.093	1.00	34.68		C
ATOM	2239	C	GLU	B	82	−34.704	−32.235	106.492	1.00	36.53		C
ATOM	2240	O	GLU	B	82	−34.861	−31.767	105.360	1.00	32.72		O
ATOM	2241	CB	GLU	B	82	−32.363	−32.799	106.059	1.00	37.11		C
ATOM	2242	CG	GLU	B	82	−32.783	−34.160	105.573	1.00	41.97		C
ATOM	2243	CD	GLU	B	82	−31.777	−35.240	105.930	1.00	51.14		C
ATOM	2244	OE1	GLU	B	82	−31.259	−35.252	107.093	1.00	45.81		O
ATOM	2245	OE2	GLU	B	82	−31.522	−36.080	105.032	1.00	60.52		O1−
ATOM	2246	N	ASP	B	83	−35.691	−32.835	107.151	1.00	36.25		N
ATOM	2247	CA	ASP	B	83	−37.045	−32.856	106.622	1.00	30.47		C
ATOM	2248	C	ASP	B	83	−37.924	−31.782	107.227	1.00	26.07		C
ATOM	2249	O	ASP	B	83	−39.029	−31.554	106.726	1.00	22.59		O
ATOM	2250	CB	ASP	B	83	−37.673	−34.235	106.815	1.00	28.20		C
ATOM	2251	CG	ASP	B	83	−36.966	−35.300	105.987	1.00	37.30		C
ATOM	2252	OD1	ASP	B	83	−36.200	−34.897	105.068	1.00	38.14		O
ATOM	2253	OD2	ASP	B	83	−37.177	−36.519	106.234	1.00	37.91		O1−
ATOM	2254	N	PHE	B	84	−37.420	−31.069	108.221	1.00	22.98		N
ATOM	2255	CA	PHE	B	84	−38.174	−30.025	108.897	1.00	27.33		C
ATOM	2256	C	PHE	B	84	−37.971	−28.727	108.122	1.00	28.99		C
ATOM	2257	O	PHE	B	84	−36.861	−28.182	108.083	1.00	25.03		O
ATOM	2258	CB	PHE	B	84	−37.721	−29.926	110.346	1.00	27.37		C
ATOM	2259	CG	PHE	B	84	−37.992	−31.172	111.114	1.00	29.16		C
ATOM	2260	CD2	PHE	B	84	−39.193	−31.337	111.794	1.00	27.59		C
ATOM	2261	CD1	PHE	B	84	−37.076	−32.213	111.100	1.00	25.70		C
ATOM	2262	CE2	PHE	B	84	−39.456	−32.507	112.497	1.00	31.00		C
ATOM	2263	CE1	PHE	B	84	−37.334	−33.386	111.793	1.00	31.57		C
ATOM	2264	CZ	PHE	B	84	−38.527	−33.529	112.505	1.00	32.40		C
ATOM	2265	N	ALA	B	85	−39.048	−28.257	107.494	1.00	26.46		N
ATOM	2266	CA	ALA	B	85	−39.022	−27.288	106.408	1.00	23.46		C
ATOM	2267	C	ALA	B	85	−40.457	−26.866	106.126	1.00	23.53		C
ATOM	2268	O	ALA	B	85	−41.404	−27.329	106.771	1.00	22.25		O
ATOM	2269	CB	ALA	B	85	−38.376	−27.893	105.154	1.00	21.86		C
ATOM	2270	N	VAL	B	86	−40.617	−26.039	105.105	1.00	23.47		N
ATOM	2271	CA	VAL	B	86	−41.936	−25.680	104.600	1.00	23.19		C
ATOM	2272	C	VAL	B	86	−42.201	−26.477	103.330	1.00	22.81		C
ATOM	2273	O	VAL	B	86	−41.314	−26.672	102.500	1.00	22.61		O
ATOM	2274	CB	VAL	B	86	−42.053	−24.162	104.366	1.00	25.35		C
ATOM	2275	CG1	VAL	B	86	−43.330	−23.837	103.664	1.00	26.56		C
ATOM	2276	CG2	VAL	B	86	−42.014	−23.424	105.700	1.00	19.36		C
ATOM	2277	N	TYR	B	87	−43.417	−26.967	103.188	1.00	23.96		N
ATOM	2278	CA	TYR	B	87	−43.798	−27.738	102.021	1.00	25.43		C
ATOM	2279	C	TYR	B	87	−44.915	−27.002	101.304	1.00	27.51		C
ATOM	2280	O	TYR	B	87	−45.806	−26.452	101.949	1.00	24.76		O
ATOM	2281	CB	TYR	B	87	−44.216	−29.157	102.418	1.00	22.13		C
ATOM	2282	CG	TYR	B	87	−43.036	−29.940	102.943	1.00	26.73		C
ATOM	2283	CD1	TYR	B	87	−42.575	−29.754	104.253	1.00	22.18		C
ATOM	2284	CD2	TYR	B	87	−42.355	−30.833	102.129	1.00	22.28		C
ATOM	2285	CE1	TYR	B	87	−41.484	−30.435	104.729	1.00	21.84		C
ATOM	2286	CE2	TYR	B	87	−41.256	−31.533	102.612	1.00	25.81		C
ATOM	2287	CZ	TYR	B	87	−40.816	−31.334	103.906	1.00	22.45		C
ATOM	2288	OH	TYR	B	87	−39.716	−32.037	104.374	1.00	18.88		O
ATOM	2289	N	PHE	B	88	−44.823	−26.949	99.973	1.00	25.00		N
ATOM	2290	CA	PHE	B	88	−45.780	−26.258	99.124	1.00	26.03		C
ATOM	2291	C	PHE	B	88	−46.299	−27.240	98.077	1.00	30.78		C
ATOM	2292	O	PHE	B	88	−45.519	−28.026	97.519	1.00	30.24		O
ATOM	2293	CB	PHE	B	88	−45.131	−25.063	98.406	1.00	27.78		C
ATOM	2294	CG	PHE	B	88	−44.809	−23.887	99.307	1.00	31.23		C
ATOM	2295	CD1	PHE	B	88	−45.802	−23.008	99.730	1.00	30.25		C
ATOM	2296	CD2	PHE	B	88	−43.494	−23.634	99.690	1.00	30.31		C
ATOM	2297	CE1	PHE	B	88	−45.493	−21.904	100.539	1.00	30.57		C
ATOM	2298	CE2	PHE	B	88	−43.185	−22.549	100.489	1.00	34.11		C
ATOM	2299	CZ	PHE	B	88	−44.197	−21.678	100.917	1.00	34.33		C
ATOM	2300	N	CYS	B	89	−47.603	−27.210	97.808	1.00	25.66		N
ATOM	2301	CA	CYS	B	89	−48.130	−27.930	96.660	1.00	24.07		C
ATOM	2302	C	CYS	B	89	−48.355	−26.953	95.513	1.00	23.52		C
ATOM	2303	O	CYS	B	89	−48.402	−25.739	95.708	1.00	21.13		O
ATOM	2304	CB	CYS	B	89	−49.416	−28.709	96.998	1.00	21.36		C
ATOM	2305	SG	CYS	B	89	−50.748	−27.800	97.719	1.00	30.20		S
ATOM	2306	N	GLN	B	90	−48.451	−27.502	94.302	1.00	22.98		N
ATOM	2307	CA	GLN	B	90	−48.547	−26.702	93.085	1.00	23.61		C
ATOM	2308	C	GLN	B	90	−49.265	−27.514	92.017	1.00	24.59		C
ATOM	2309	O	GLN	B	90	−48.979	−28.703	91.859	1.00	24.95		O
ATOM	2310	CB	GLN	B	90	−47.153	−26.272	92.588	1.00	23.03		C
ATOM	2311	CG	GLN	B	90	−47.199	−25.382	91.346	1.00	24.92		C
ATOM	2312	CD	GLN	B	90	−46.481	−25.971	90.137	1.00	26.13		C
ATOM	2313	OE1	GLN	B	90	−45.402	−26.556	90.261	1.00	32.43		O
ATOM	2314	NE2	GLN	B	90	−47.093	−25.847	88.969	1.00	23.23		N
ATOM	2315	N	GLN	B	91	−50.221	−26.897	91.319	1.00	22.59		N
ATOM	2316	CA	GLN	B	91	−50.911	−27.567	90.224	1.00	24.25		C
ATOM	2317	C	GLN	B	91	−50.510	−26.926	88.899	1.00	25.92		C
ATOM	2318	O	GLN	B	91	−50.206	−25.731	88.830	1.00	24.83		O
ATOM	2319	CB	GLN	B	91	−52.449	−27.564	90.405	1.00	19.74		C
ATOM	2320	CG	GLN	B	91	−53.125	−26.219	90.299	1.00	21.60		C
ATOM	2321	CD	GLN	B	91	−53.417	−25.811	88.871	1.00	24.32		C
ATOM	2322	OE1	GLN	B	91	−53.515	−26.657	87.975	1.00	23.50		O
ATOM	2323	NE2	GLN	B	91	−53.561	−24.499	88.648	1.00	23.44		N
ATOM	2324	N	TYR	B	92	−50.462	−27.737	87.850	1.00	24.33		N
ATOM	2325	CA	TYR	B	92	−50.099	−27.241	86.524	1.00	26.73		C
ATOM	2326	C	TYR	B	92	−51.027	−27.842	85.493	1.00	27.55		C
ATOM	2327	O	TYR	B	92	−50.626	−28.137	84.362	1.00	29.60		O
ATOM	2328	CB	TYR	B	92	−48.610	−27.501	86.194	1.00	23.03		C
ATOM	2329	CG	TYR	B	92	−48.133	−28.903	86.494	1.00	22.43		C
ATOM	2330	CD1	TYR	B	92	−47.776	−29.257	87.789	1.00	22.77		C
ATOM	2331	CD2	TYR	B	92	−48.036	−29.874	85.496	1.00	22.32		C
ATOM	2332	CE1	TYR	B	92	−47.349	−30.533	88.095	1.00	22.69		C
ATOM	2333	CE2	TYR	B	92	−47.589	−31.154	85.788	1.00	21.88		C
ATOM	2334	CZ	TYR	B	92	−47.254	−31.478	87.096	1.00	23.71		C
ATOM	2335	OH	TYR	B	92	−46.820	−32.729	87.444	1.00	20.44		O
ATOM	2336	N	GLU	B	93	−52.289	−28.031	85.880	1.00	27.99		N
ATOM	2337	CA	GLU	B	93	−53.312	−28.512	84.958	1.00	30.82		C
ATOM	2338	C	GLU	B	93	−53.999	−27.364	84.244	1.00	31.11		C
ATOM	2339	O	GLU	B	93	−54.182	−27.424	83.026	1.00	30.30		O
ATOM	2340	CB	GLU	B	93	−54.360	−29.364	85.691	1.00	30.98		C
ATOM	2341	CG	GLU	B	93	−55.690	−29.496	84.939	1.00	25.68		C
ATOM	2342	CD	GLU	B	93	−56.678	−30.425	85.629	1.00	33.12		C
ATOM	2343	OE1	GLU	B	93	−56.247	−31.498	86.123	1.00	31.54		O
ATOM	2344	OE2	GLU	B	93	−57.889	−30.090	85.680	1.00	32.74		O1−
ATOM	2345	N	SER	B	94	−54.366	−26.310	84.970	1.00	30.35		N
ATOM	2346	CA	SER	B	94	−55.097	−25.199	84.378	1.00	32.23		C
ATOM	2347	C	SER	B	94	−54.388	−23.888	84.703	1.00	28.38		C
ATOM	2348	O	SER	B	94	−54.044	−23.617	85.861	1.00	23.42		O
ATOM	2349	CB	SER	B	94	−56.556	−25.171	84.862	1.00	32.62		C
ATOM	2350	OG	SER	B	94	−57.144	−23.891	84.656	1.00	44.26		O
ATOM	2351	N	SER	B	95	−54.180	−23.077	83.678	1.00	29.26		N
ATOM	2352	CA	SER	B	95	−53.498	−21.814	83.854	1.00	28.94		C
ATOM	2353	C	SER	B	95	−54.464	−20.862	84.524	1.00	28.67		C
ATOM	2354	O	SER	B	95	−55.645	−20.897	84.219	1.00	29.79		O
ATOM	2355	CB	SER	B	95	−53.015	−21.271	82.514	1.00	23.10		C
ATOM	2356	OG	SER	B	95	−52.370	−20.022	82.690	1.00	38.38		O
ATOM	2357	N	PRO	B	96	−53.976	−20.029	85.458	1.00	27.09		N
ATOM	2358	CA	PRO	B	96	−52.599	−19.892	85.956	1.00	26.26		C
ATOM	2359	C	PRO	B	96	−52.131	−21.034	86.857	1.00	27.92		C
ATOM	2360	O	PRO	B	96	−52.933	−21.550	87.627	1.00	31.29		O
ATOM	2361	CB	PRO	B	96	−52.658	−18.601	86.768	1.00	25.28		C
ATOM	2362	CG	PRO	B	96	−54.047	−18.557	87.258	1.00	27.55		C
ATOM	2363	CD	PRO	B	96	−54.892	−19.111	86.148	1.00	23.84		C
ATOM	2364	N	TRP	B	97	−50.858	−21.419	86.786	1.00	26.30		N
ATOM	2365	CA	TRP	B	97	−50.330	−22.305	87.811	1.00	26.57		C
ATOM	2366	C	TRP	B	97	−50.524	−21.661	89.178	1.00	25.80		C
ATOM	2367	O	TRP	B	97	−50.307	−20.460	89.358	1.00	25.76		O
ATOM	2368	CB	TRP	B	97	−48.847	−22.617	87.594	1.00	25.63		C
ATOM	2369	CG	TRP	B	97	−48.411	−23.337	86.309	1.00	28.94		C
ATOM	2370	CD1	TRP	B	97	−47.124	−23.541	85.926	1.00	29.48		C
ATOM	2371	CD2	TRP	B	97	−49.229	−23.928	85.264	1.00	29.78		C
ATOM	2372	NE1	TRP	B	97	−47.073	−24.216	84.733	1.00	32.61		N
ATOM	2373	CE2	TRP	B	97	−48.344	−24.459	84.296	1.00	28.86		C
ATOM	2374	CE3	TRP	B	97	−50.608	−24.072	85.061	1.00	29.91		C
ATOM	2375	CZ2	TRP	B	97	−48.789	−25.116	83.134	1.00	31.43		C
ATOM	2376	CZ3	TRP	B	97	−51.054	−24.724	83.902	1.00	28.75		C
ATOM	2377	CH2	TRP	B	97	−50.140	−25.232	82.951	1.00	31.01		C
ATOM	2378	N	THR	B	98	−50.931	−22.460	90.148	1.00	21.99		N
ATOM	2379	CA	THR	B	98	−51.167	−21.932	91.472	1.00	23.81		C
ATOM	2380	C	THR	B	98	−50.474	−22.819	92.488	1.00	23.94		C
ATOM	2381	O	THR	B	98	−50.148	−23.973	92.215	1.00	25.95		O
ATOM	2382	CB	THR	B	98	−52.674	−21.787	91.782	1.00	26.18		C
ATOM	2383	OG1	THR	B	98	−53.374	−23.006	91.498	1.00	23.15		O
ATOM	2384	CG2	THR	B	98	−53.270	−20.618	90.969	1.00	24.44		C
ATOM	2385	N	PHE	B	99	−50.184	−22.209	93.633	1.00	28.63		N
ATOM	2386	CA	PHE	B	99	−49.511	−22.803	94.776	1.00	26.82		C
ATOM	2387	C	PHE	B	99	−50.436	−22.773	95.988	1.00	29.46		C
ATOM	2388	O	PHE	B	99	−51.311	−21.912	96.089	1.00	31.15		O
ATOM	2389	CB	PHE	B	99	−48.236	−22.020	95.121	1.00	27.58		C
ATOM	2390	CG	PHE	B	99	−47.123	−22.166	94.115	1.00	26.17		C
ATOM	2391	CD1	PHE	B	99	−46.212	−23.210	94.213	1.00	21.23		C
ATOM	2392	CD2	PHE	B	99	−46.970	−21.236	93.096	1.00	26.56		C
ATOM	2393	CE1	PHE	B	99	−45.179	−23.346	93.313	1.00	23.45		C
ATOM	2394	CE2	PHE	B	99	−45.935	−21.362	92.177	1.00	28.21		C
ATOM	2395	CZ	PHE	B	99	−45.028	−22.420	92.291	1.00	25.30		C
ATOM	2396	N	GLY	B	100	−50.252	−23.722	96.909	1.00	29.01		N
ATOM	2397	CA	GLY	B	100	−50.849	−23.604	98.224	1.00	26.65		C
ATOM	2398	C	GLY	B	100	−50.062	−22.660	99.136	1.00	32.15		C
ATOM	2399	O	GLY	B	100	−48.953	−22.224	98.831	1.00	30.70		O
ATOM	2400	N	GLN	B	101	−50.651	−22.339	100.291	1.00	32.09		N
ATOM	2401	CA	GLN	B	101	−49.953	−21.455	101.219	1.00	27.63		C
ATOM	2402	C	GLN	B	101	−48.788	−22.134	101.926	1.00	31.28		C
ATOM	2403	O	GLN	B	101	−47.993	−21.430	102.555	1.00	31.67		O
ATOM	2404	CB	GLN	B	101	−50.888	−20.871	102.296	1.00	31.00		C
ATOM	2405	CG	GLN	B	101	−52.371	−21.297	102.285	1.00	41.04		C
ATOM	2406	CD	GLN	B	101	−52.581	−22.771	102.623	1.00	41.89		C
ATOM	2407	OE1	GLN	B	101	−52.927	−23.567	101.736	1.00	36.09		O
ATOM	2408	NE2	GLN	B	101	−52.365	−23.147	103.900	1.00	37.62		N
ATOM	2409	N	GLY	B	102	−48.665	−23.453	101.858	1.00	26.43		N
ATOM	2410	CA	GLY	B	102	−47.548	−24.085	102.535	1.00	24.50		C
ATOM	2411	C	GLY	B	102	−47.895	−24.678	103.898	1.00	27.19		C
ATOM	2412	O	GLY	B	102	−48.800	−24.215	104.600	1.00	27.42		O
ATOM	2413	N	THR	B	103	−47.158	−25.724	104.283	1.00	24.40		N
ATOM	2414	CA	THR	B	103	−47.207	−26.276	105.634	1.00	27.22		C
ATOM	2415	C	THR	B	103	−45.806	−26.259	106.239	1.00	25.76		C
ATOM	2416	O	THR	B	103	−44.857	−26.746	105.621	1.00	27.96		O
ATOM	2417	CB	THR	B	103	−47.752	−27.718	105.647	1.00	28.05		C
ATOM	2418	OG1	THR	B	103	−49.120	−27.729	105.232	1.00	31.71		O
ATOM	2419	CG2	THR	B	103	−47.654	−28.348	107.061	1.00	25.08		C
ATOM	2420	N	LYS	B	104	−45.673	−25.709	107.442	1.00	22.08		N
ATOM	2421	CA	LYS	B	104	−44.409	−25.758	108.159	1.00	26.19		C
ATOM	2422	C	LYS	B	104	−44.360	−27.021	109.014	1.00	27.07		C
ATOM	2423	O	LYS	B	104	−45.205	−27.212	109.889	1.00	28.44		O
ATOM	2424	CB	LYS	B	104	−44.212	−24.523	109.032	1.00	25.21		C
ATOM	2425	CG	LYS	B	104	−42.846	−24.510	109.709	1.00	26.78		C
ATOM	2426	CD	LYS	B	104	−42.677	−23.365	110.699	1.00	30.43		C
ATOM	2427	CE	LYS	B	104	−41.301	−23.463	111.391	1.00	45.22		C
ATOM	2428	NZ	LYS	B	104	−40.967	−22.316	112.301	1.00	44.27		N1+
ATOM	2429	N	VAL	B	105	−43.366	−27.869	108.779	1.00	25.76		N
ATOM	2430	CA	VAL	B	105	−43.119	−29.033	109.624	1.00	29.32		C
ATOM	2431	C	VAL	B	105	−42.005	−28.664	110.597	1.00	27.51		C
ATOM	2432	O	VAL	B	105	−40.841	−28.516	110.211	1.00	25.98		O
ATOM	2433	CB	VAL	B	105	−42.757	−30.283	108.813	1.00	24.39		C
ATOM	2434	CG1	VAL	B	105	−42.488	−31.445	109.776	1.00	26.12		C
ATOM	2435	CG2	VAL	B	105	−43.868	−30.636	107.890	1.00	21.86		C
ATOM	2436	N	GLU	B	106	−42.367	−28.533	111.863	1.00	31.16		N
ATOM	2437	CA	GLU	B	106	−41.473	−28.092	112.919	1.00	28.93		C
ATOM	2438	C	GLU	B	106	−41.144	−29.242	113.875	1.00	33.11		C
ATOM	2439	O	GLU	B	106	−41.922	−30.197	114.030	1.00	30.26		O
ATOM	2440	CB	GLU	B	106	−42.130	−26.943	113.669	1.00	31.52		C
ATOM	2441	CG	GLU	B	106	−41.324	−26.435	114.830	1.00	41.69		C
ATOM	2442	CD	GLU	B	106	−42.170	−26.121	116.028	1.00	37.31		C
ATOM	2443	OE1	GLU	B	106	−42.903	−27.027	116.485	1.00	37.32		O
ATOM	2444	OE2	GLU	B	106	−42.102	−24.963	116.492	1.00	39.39		O1−
ATOM	2445	N	ILE	B	107	−39.971	−29.149	114.495	1.00	26.80		N
ATOM	2446	CA	ILE	B	107	−39.486	−30.168	115.421	1.00	28.39		C
ATOM	2447	C	ILE	B	107	−40.205	−30.038	116.755	1.00	32.03		C
ATOM	2448	O	ILE	B	107	−40.118	−29.003	117.420	1.00	27.69		O
ATOM	2449	CB	ILE	B	107	−37.974	−30.050	115.622	1.00	26.88		C
ATOM	2450	CG1	ILE	B	107	−37.240	−30.423	114.344	1.00	27.26		C
ATOM	2451	CG2	ILE	B	107	−37.552	−30.898	116.793	1.00	26.83		C
ATOM	2452	CD1	ILE	B	107	−35.799	−30.043	114.347	1.00	30.15		C
ATOM	2453	N	LYS	B	108	−40.866	−31.106	117.182	1.00	31.78		N
ATOM	2454	CA	LYS	B	108	−41.455	−31.110	118.512	1.00	32.40		C
ATOM	2455	C	LYS	B	108	−40.382	−31.497	119.529	1.00	32.97		C
ATOM	2456	O	LYS	B	108	−39.654	−32.475	119.336	1.00	33.78		O
ATOM	2457	CB	LYS	B	108	−42.649	−32.069	118.567	1.00	34.38		C
ATOM	2458	CG	LYS	B	108	−43.460	−32.006	119.864	1.00	35.60		C
ATOM	2459	CD	LYS	B	108	−44.379	−33.223	120.000	1.00	34.87		C
ATOM	2460	CE	LYS	B	108	−45.671	−32.857	120.690	1.00	39.16		C
ATOM	2461	NZ	LYS	B	108	−45.560	−31.457	121.228	1.00	41.36		N1+
ATOM	2462	N	ARG	B	109	−40.270	−30.720	120.604	1.00	30.43		N
ATOM	2463	CA	ARG	B	109	−39.298	−30.996	121.651	1.00	27.95		C
ATOM	2464	C	ARG	B	109	−39.942	−30.659	122.985	1.00	29.25		C
ATOM	2465	O	ARG	B	109	−41.117	−30.284	123.040	1.00	33.46		O
ATOM	2466	CB	ARG	B	109	−37.993	−30.224	121.445	1.00	27.54		C
ATOM	2467	CG	ARG	B	109	−38.128	−28.705	121.378	1.00	29.91		C
ATOM	2468	CD	ARG	B	109	−36.873	−28.023	121.928	1.00	26.11		C
ATOM	2469	NE	ARG	B	109	−36.853	−28.173	123.386	1.00	32.71		N
ATOM	2470	CZ	ARG	B	109	−35.751	−28.189	124.126	1.00	27.84		C
ATOM	2471	NH1	ARG	B	109	−35.827	−28.351	125.449	1.00	24.67		N1+
ATOM	2472	NH2	ARG	B	109	−34.577	−28.039	123.536	1.00	23.42		N
ATOM	2473	N	THR	B	110	−39.191	−30.838	124.073	1.00	27.37		N
ATOM	2474	CA	THR	B	110	−39.762	−30.554	125.385	1.00	28.62		C
ATOM	2475	C	THR	B	110	−39.775	−29.056	125.631	1.00	29.53		C
ATOM	2476	O	THR	B	110	−38.878	−28.311	125.203	1.00	26.75		O
ATOM	2477	CB	THR	B	110	−39.006	−31.227	126.546	1.00	27.19		C
ATOM	2478	OG1	THR	B	110	−37.641	−30.803	126.570	1.00	31.87		O
ATOM	2479	CG2	THR	B	110	−39.052	−32.727	126.445	1.00	25.84		C
ATOM	2480	N	VAL	B	111	−40.796	−28.630	126.367	1.00	31.89		N
ATOM	2481	CA	VAL	B	111	−40.905	−27.236	126.752	1.00	33.07		C
ATOM	2482	C	VAL	B	111	−39.618	−26.751	127.407	1.00	31.48		C
ATOM	2483	O	VAL	B	111	−38.982	−27.463	128.195	1.00	31.62		O
ATOM	2484	CB	VAL	B	111	−42.112	−27.056	127.683	1.00	30.76		C
ATOM	2485	CG1	VAL	B	111	−42.176	−25.612	128.149	1.00	27.34		C
ATOM	2486	CG2	VAL	B	111	−43.381	−27.478	126.949	1.00	24.38		C
ATOM	2487	N	ALA	B	112	−39.223	−25.532	127.044	1.00	29.57		N
ATOM	2488	CA	ALA	B	112	−38.047	−24.863	127.582	1.00	25.09		C
ATOM	2489	C	ALA	B	112	−38.425	−23.405	127.788	1.00	30.16		C
ATOM	2490	O	ALA	B	112	−38.831	−22.734	126.835	1.00	27.80		O
ATOM	2491	CB	ALA	B	112	−36.844	−24.984	126.639	1.00	23.34		C
ATOM	2492	N	ALA	B	113	−38.318	−22.928	129.029	1.00	32.01		N
ATOM	2493	CA	ALA	B	113	−38.663	−21.549	129.326	1.00	28.03		C
ATOM	2494	C	ALA	B	113	−37.579	−20.640	128.768	1.00	29.40		C
ATOM	2495	O	ALA	B	113	−36.412	−21.035	128.710	1.00	31.93		O
ATOM	2496	CB	ALA	B	113	−38.799	−21.325	130.830	1.00	23.97		C
ATOM	2497	N	PRO	B	114	−37.934	−19.422	128.353	1.00	27.52		N
ATOM	2498	CA	PRO	B	114	−36.911	−18.489	127.860	1.00	27.42		C
ATOM	2499	C	PRO	B	114	−36.095	−17.920	129.004	1.00	27.03		C
ATOM	2500	O	PRO	B	114	−36.590	−17.719	130.108	1.00	29.23		O
ATOM	2501	CB	PRO	B	114	−37.731	−17.386	127.186	1.00	27.64		C
ATOM	2502	CG	PRO	B	114	−39.012	−17.376	127.998	1.00	27.54		C
ATOM	2503	CD	PRO	B	114	−39.274	−18.806	128.403	1.00	24.48		C
ATOM	2504	N	SER	B	115	−34.835	−17.635	128.730	1.00	27.91		N
ATOM	2505	CA	SER	B	115	−34.092	−16.739	129.592	1.00	25.63		C
ATOM	2506	C	SER	B	115	−34.236	−15.331	129.028	1.00	25.72		C
ATOM	2507	O	SER	B	115	−34.238	−15.130	127.814	1.00	27.20		O
ATOM	2508	CB	SER	B	115	−32.628	−17.157	129.726	1.00	24.15		C
ATOM	2509	OG	SER	B	115	−32.139	−17.720	128.535	1.00	40.34		O
ATOM	2510	N	VAL	B	116	−34.430	−14.371	129.922	1.00	26.54		N
ATOM	2511	CA	VAL	B	116	−34.857	−13.023	129.579	1.00	28.89		C
ATOM	2512	C	VAL	B	116	−33.762	−12.037	129.979	1.00	26.93		C
ATOM	2513	O	VAL	B	116	−33.243	−12.093	131.094	1.00	31.62		O
ATOM	2514	CB	VAL	B	116	−36.203	−12.695	130.259	1.00	28.35		C
ATOM	2515	CG1	VAL	B	116	−36.709	−11.313	129.860	1.00	28.35		C
ATOM	2516	CG2	VAL	B	116	−37.212	−13.740	129.882	1.00	18.89		C
ATOM	2517	N	PHE	B	117	−33.406	−11.151	129.063	1.00	25.01		N
ATOM	2518	CA	PHE	B	117	−32.424	−10.118	129.311	1.00	25.46		C
ATOM	2519	C	PHE	B	117	−32.963	−8.826	128.726	1.00	28.62		C
ATOM	2520	O	PHE	B	117	−33.533	−8.832	127.632	1.00	31.30		O
ATOM	2521	CB	PHE	B	117	−31.081	−10.413	128.650	1.00	25.62		C
ATOM	2522	CG	PHE	B	117	−30.536	−11.799	128.892	1.00	29.84		C
ATOM	2523	CD1	PHE	B	117	−30.935	−12.876	128.093	1.00	24.22		C
ATOM	2524	CD2	PHE	B	117	−29.542	−12.015	129.835	1.00	31.65		C
ATOM	2525	CE1	PHE	B	117	−30.405	−14.136	128.283	1.00	22.90		C
ATOM	2526	CE2	PHE	B	117	−28.998	−13.290	130.013	1.00	29.63		C
ATOM	2527	CZ	PHE	B	117	−29.430	−14.339	129.234	1.00	24.06		C
ATOM	2528	N	ILE	B	118	−32.755	−7.717	129.428	1.00	28.33		N
ATOM	2529	CA	ILE	B	118	−33.211	−6.409	128.973	1.00	27.52		C
ATOM	2530	C	ILE	B	118	−31.997	−5.501	128.878	1.00	27.02		C
ATOM	2531	O	ILE	B	118	−31.130	−5.541	129.750	1.00	28.87		O
ATOM	2532	CB	ILE	B	118	−34.280	−5.811	129.911	1.00	29.46		C
ATOM	2533	CG1	ILE	B	118	−34.774	−4.480	129.347	1.00	30.76		C
ATOM	2534	CG2	ILE	B	118	−33.752	−5.639	131.343	1.00	25.68		C
ATOM	2535	CD1	ILE	B	118	−35.736	−3.775	130.229	1.00	29.17		C
ATOM	2536	N	PHE	B	119	−31.925	−4.700	127.811	1.00	28.09		N
ATOM	2537	CA	PHE	B	119	−30.765	−3.875	127.503	1.00	24.90		C
ATOM	2538	C	PHE	B	119	−31.149	−2.406	127.478	1.00	29.17		C
ATOM	2539	O	PHE	B	119	−32.037	−2.018	126.706	1.00	31.62		O
ATOM	2540	CB	PHE	B	119	−30.163	−4.224	126.148	1.00	26.03		C
ATOM	2541	CG	PHE	B	119	−29.643	−5.603	126.045	1.00	29.01		C
ATOM	2542	CD1	PHE	B	119	−28.383	−5.913	126.505	1.00	26.67		C
ATOM	2543	CD2	PHE	B	119	−30.400	−6.594	125.430	1.00	30.15		C
ATOM	2544	CE1	PHE	B	119	−27.897	−7.200	126.403	1.00	29.34		C
ATOM	2545	CE2	PHE	B	119	−29.927	−7.882	125.314	1.00	25.71		C
ATOM	2546	CZ	PHE	B	119	−28.670	−8.191	125.806	1.00	29.15		C
ATOM	2547	N	PRO	B	120	−30.468	−1.550	128.231	1.00	34.18		N
ATOM	2548	CA	PRO	B	120	−30.747	−0.106	128.152	1.00	34.68		C
ATOM	2549	C	PRO	B	120	−30.251	0.460	126.834	1.00	34.50		C
ATOM	2550	O	PRO	B	120	−29.378	−0.140	126.188	1.00	36.34		O
ATOM	2551	CB	PRO	B	120	−29.963	0.474	129.339	1.00	33.20		C
ATOM	2552	CG	PRO	B	120	−29.568	−0.746	130.190	1.00	37.48		C
ATOM	2553	CD	PRO	B	120	−29.417	−1.862	129.212	1.00	32.46		C
ATOM	2554	N	PRO	B	121	−30.761	1.616	126.402	1.00	35.15		N
ATOM	2555	CA	PRO	B	121	−30.200	2.248	125.203	1.00	34.06		C
ATOM	2556	C	PRO	B	121	−28.766	2.697	125.452	1.00	32.75		C
ATOM	2557	O	PRO	B	121	−28.410	3.117	126.551	1.00	34.53		O
ATOM	2558	CB	PRO	B	121	−31.138	3.436	124.958	1.00	30.93		C
ATOM	2559	CG	PRO	B	121	−31.733	3.718	126.279	1.00	29.12		C
ATOM	2560	CD	PRO	B	121	−31.870	2.404	126.965	1.00	30.02		C
ATOM	2561	N	SER	B	122	−27.930	2.583	124.431	1.00	35.60		N
ATOM	2562	CA	SER	B	122	−26.558	3.043	124.576	1.00	40.70		C
ATOM	2563	C	SER	B	122	−26.517	4.570	124.585	1.00	42.19		C
ATOM	2564	O	SER	B	122	−27.311	5.239	123.913	1.00	40.94		O
ATOM	2565	CB	SER	B	122	−25.677	2.503	123.437	1.00	38.69		C
ATOM	2566	OG	SER	B	122	−25.921	3.200	122.223	1.00	33.97		O
ATOM	2567	N	ASP	B	123	−25.550	5.120	125.328	1.00	41.84		N
ATOM	2568	CA	ASP	B	123	−25.391	6.569	125.357	1.00	44.12		C
ATOM	2569	C	ASP	B	123	−25.119	7.126	123.965	1.00	48.91		C
ATOM	2570	O	ASP	B	123	−25.453	8.285	123.682	1.00	47.81		O
ATOM	2571	CB	ASP	B	123	−24.267	6.968	126.311	1.00	47.34		C
ATOM	2572	CG	ASP	B	123	−24.693	6.950	127.779	1.00	59.18		C
ATOM	2573	OD1	ASP	B	123	−25.864	7.272	128.086	1.00	59.74		O
ATOM	2574	OD2	ASP	B	123	−23.839	6.640	128.638	1.00	65.74		O1−
ATOM	2575	N	GLU	B	124	−24.542	6.312	123.079	1.00	44.91		N
ATOM	2576	CA	GLU	B	124	−24.273	6.776	121.722	1.00	48.45		C
ATOM	2577	C	GLU	B	124	−25.559	7.001	120.919	1.00	48.55		C
ATOM	2578	O	GLU	B	124	−25.649	7.962	120.145	1.00	48.61		O
ATOM	2579	CB	GLU	B	124	−23.360	5.788	121.014	1.00	46.13		C
ATOM	2580	CG	GLU	B	124	−22.949	6.279	119.661	1.00	52.72		C
ATOM	2581	CD	GLU	B	124	−22.264	5.209	118.846	1.00	59.55		C
ATOM	2582	OE1	GLU	B	124	−22.167	5.408	117.608	1.00	50.04		O
ATOM	2583	OE2	GLU	B	124	−21.850	4.175	119.443	1.00	55.47		O1−
ATOM	2584	N	GLN	B	125	−26.574	6.143	121.093	1.00	46.17		N
ATOM	2585	CA	GLN	B	125	−27.839	6.369	120.391	1.00	41.17		C
ATOM	2586	C	GLN	B	125	−28.632	7.506	121.018	1.00	44.73		C
ATOM	2587	O	GLN	B	125	−29.391	8.187	120.315	1.00	41.05		O
ATOM	2588	CB	GLN	B	125	−28.687	5.095	120.366	1.00	36.73		C
ATOM	2589	CG	GLN	B	125	−30.012	5.222	119.593	1.00	33.48		C
ATOM	2590	CD	GLN	B	125	−31.023	4.118	119.918	1.00	37.11		C
ATOM	2591	OE1	GLN	B	125	−30.936	3.430	120.947	1.00	35.61		O
ATOM	2592	NE2	GLN	B	125	−31.976	3.925	119.016	1.00	41.82		N
ATOM	2593	N	LEU	B	126	−28.493	7.704	122.337	1.00	43.68		N
ATOM	2594	CA	LEU	B	126	−29.168	8.813	123.006	1.00	45.10		C
ATOM	2595	C	LEU	B	126	−28.719	10.152	122.434	1.00	49.62		C
ATOM	2596	O	LEU	B	126	−29.526	11.085	122.313	1.00	49.20		O
ATOM	2597	CB	LEU	B	126	−28.906	8.751	124.510	1.00	46.51		C
ATOM	2598	CG	LEU	B	126	−29.691	7.699	125.300	1.00	44.00		C
ATOM	2599	CD1	LEU	B	126	−29.263	7.692	126.754	1.00	37.07		C
ATOM	2600	CD2	LEU	B	126	−31.208	7.898	125.167	1.00	36.79		C
ATOM	2601	N	LYS	B	127	−27.428	10.263	122.083	1.00	47.40		N
ATOM	2602	CA	LYS	B	127	−26.902	11.463	121.438	1.00	44.91		C
ATOM	2603	C	LYS	B	127	−27.707	11.875	120.208	1.00	50.97		C
ATOM	2604	O	LYS	B	127	−27.782	13.065	119.883	1.00	56.06		O
ATOM	2605	CB	LYS	B	127	−25.441	11.244	121.060	1.00	53.95		C
ATOM	2606	CG	LYS	B	127	−24.474	11.931	122.009	1.00	65.16		C
ATOM	2607	CD	LYS	B	127	−24.039	11.038	123.160	1.00	60.17		C
ATOM	2608	CE	LYS	B	127	−22.846	10.198	122.738	1.00	65.63		C
ATOM	2609	NZ	LYS	B	127	−21.833	11.021	122.005	1.00	65.70		N1+
ATOM	2610	N	SER	B	128	−28.302	10.918	119.506	1.00	48.42		N
ATOM	2611	CA	SER	B	128	−29.026	11.194	118.274	1.00	44.86		C
ATOM	2612	C	SER	B	128	−30.527	11.393	118.485	1.00	48.97		C
ATOM	2613	O	SER	B	128	−31.271	11.432	117.498	1.00	56.04		O
ATOM	2614	CB	SER	B	128	−28.814	10.057	117.266	1.00	51.64		C
ATOM	2615	OG	SER	B	128	−29.460	8.856	117.686	1.00	48.78		O
ATOM	2616	N	GLY	B	129	−30.999	11.500	119.728	1.00	42.11		N
ATOM	2617	CA	GLY	B	129	−32.383	11.859	119.953	1.00	39.56		C
ATOM	2618	C	GLY	B	129	−33.356	10.703	120.071	1.00	47.15		C
ATOM	2619	O	GLY	B	129	−34.553	10.945	120.312	1.00	45.83		O
ATOM	2620	N	THR	B	130	−32.894	9.459	119.903	1.00	44.00		N
ATOM	2621	CA	THR	B	130	−33.745	8.278	119.983	1.00	37.83		C
ATOM	2622	C	THR	B	130	−33.231	7.272	121.008	1.00	36.90		C
ATOM	2623	O	THR	B	130	−32.023	7.117	121.190	1.00	41.23		O
ATOM	2624	CB	THR	B	130	−33.871	7.637	118.606	1.00	40.93		C
ATOM	2625	OG1	THR	B	130	−34.572	8.543	117.740	1.00	34.84		O
ATOM	2626	CG2	THR	B	130	−34.617	6.297	118.679	1.00	44.09		C
ATOM	2627	N	ALA	B	131	−34.155	6.598	121.686	1.00	35.77		N
ATOM	2628	CA	ALA	B	131	−33.841	5.535	122.636	1.00	35.93		C
ATOM	2629	C	ALA	B	131	−34.469	4.216	122.186	1.00	35.42		C
ATOM	2630	O	ALA	B	131	−35.693	4.128	121.999	1.00	37.68		O
ATOM	2631	CB	ALA	B	131	−34.346	5.896	124.039	1.00	33.77		C
ATOM	2632	N	SER	B	132	−33.645	3.183	122.055	1.00	29.61		N
ATOM	2633	CA	SER	B	132	−34.127	1.837	121.791	1.00	29.37		C
ATOM	2634	C	SER	B	132	−33.845	0.960	122.999	1.00	24.73		C
ATOM	2635	O	SER	B	132	−32.689	0.774	123.367	1.00	30.61		O
ATOM	2636	CB	SER	B	132	−33.466	1.265	120.545	1.00	28.99		C
ATOM	2637	OG	SER	B	132	−33.838	2.013	119.420	1.00	32.09		O
ATOM	2638	N	VAL	B	133	−34.890	0.411	123.599	1.00	29.26		N
ATOM	2639	CA	VAL	B	133	−34.753	−0.593	124.654	1.00	30.39		C
ATOM	2640	C	VAL	B	133	−35.021	−1.960	124.044	1.00	28.40		C
ATOM	2641	O	VAL	B	133	−35.963	−2.123	123.264	1.00	30.58		O
ATOM	2642	CB	VAL	B	133	−35.717	−0.303	125.816	1.00	29.07		C
ATOM	2643	CG1	VAL	B	133	−35.309	−1.095	127.049	1.00	27.89		C
ATOM	2644	CG2	VAL	B	133	−35.751	1.186	126.090	1.00	26.20		C
ATOM	2645	N	VAL	B	134	−34.203	−2.948	124.392	1.00	26.36		N
ATOM	2646	CA	VAL	B	134	−34.262	−4.261	123.762	1.00	28.94		C
ATOM	2647	C	VAL	B	134	−34.505	−5.315	124.830	1.00	29.71		C
ATOM	2648	O	VAL	B	134	−33.851	−5.305	125.880	1.00	30.17		O
ATOM	2649	CB	VAL	B	134	−32.973	−4.576	122.980	1.00	30.23		C
ATOM	2650	CG1	VAL	B	134	−33.115	−5.912	122.281	1.00	22.43		C
ATOM	2651	CG2	VAL	B	134	−32.648	−3.460	121.991	1.00	24.76		C
ATOM	2652	N	CYS	B	135	−35.438	−6.226	124.560	1.00	27.09		N
ATOM	2653	CA	CYS	B	135	−35.688	−7.373	125.423	1.00	30.29		C
ATOM	2654	C	CYS	B	135	−35.351	−8.641	124.645	1.00	30.83		C
ATOM	2655	O	CYS	B	135	−35.841	−8.828	123.528	1.00	31.86		O
ATOM	2656	CB	CYS	B	135	−37.149	−7.402	125.895	1.00	28.77		C
ATOM	2657	SG	CYS	B	135	−37.549	−8.569	127.279	1.00	36.90		S
ATOM	2658	N	LEU	B	136	−34.537	−9.514	125.236	1.00	28.65		N
ATOM	2659	CA	LEU	B	136	−34.113	−10.767	124.610	1.00	26.89		C
ATOM	2660	C	LEU	B	136	−34.712	−11.963	125.340	1.00	27.49		C
ATOM	2661	O	LEU	B	136	−34.462	−12.158	126.536	1.00	26.81		O
ATOM	2662	CB	LEU	B	136	−32.587	−10.874	124.591	1.00	23.26		C
ATOM	2663	CG	LEU	B	136	−32.021	−12.242	124.215	1.00	26.55		C
ATOM	2664	CD1	LEU	B	136	−32.394	−12.677	122.784	1.00	29.37		C
ATOM	2665	CD2	LEU	B	136	−30.539	−12.206	124.383	1.00	26.86		C
ATOM	2666	N	LEU	B	137	−35.471	−12.776	124.612	1.00	27.17		N
ATOM	2667	CA	LEU	B	137	−36.003	−14.046	125.109	1.00	24.46		C
ATOM	2668	C	LEU	B	137	−35.244	−15.151	124.412	1.00	25.24		C
ATOM	2669	O	LEU	B	137	−35.476	−15.416	123.232	1.00	27.19		O
ATOM	2670	CB	LEU	B	137	−37.498	−14.197	124.847	1.00	24.41		C
ATOM	2671	CG	LEU	B	137	−38.513	−13.411	125.671	1.00	26.56		C
ATOM	2672	CD1	LEU	B	137	−38.301	−11.899	125.512	1.00	22.36		C
ATOM	2673	CD2	LEU	B	137	−39.922	−13.845	125.275	1.00	24.34		C
ATOM	2674	N	ASN	B	138	−34.374	−15.820	125.147	1.00	27.07		N
ATOM	2675	CA	ASN	B	138	−33.403	−16.731	124.575	1.00	27.89		C
ATOM	2676	C	ASN	B	138	−33.800	−18.186	124.822	1.00	28.77		C
ATOM	2677	O	ASN	B	138	−34.161	−18.546	125.945	1.00	33.61		O
ATOM	2678	CB	ASN	B	138	−32.033	−16.411	125.163	1.00	31.08		C
ATOM	2679	CG	ASN	B	138	−30.904	−16.806	124.256	1.00	37.01		C
ATOM	2680	OD1	ASN	B	138	−30.870	−16.438	123.076	1.00	34.03		O
ATOM	2681	ND2	ASN	B	138	−29.933	−17.509	124.815	1.00	40.66		N
ATOM	2682	N	ASN	B	139	−33.800	−18.987	123.747	1.00	26.63		N
ATOM	2683	CA	ASN	B	139	−33.861	−20.463	123.722	1.00	26.50		C
ATOM	2684	C	ASN	B	139	−35.075	−21.037	124.462	1.00	25.84		C
ATOM	2685	O	ASN	B	139	−34.958	−21.778	125.436	1.00	30.08		O
ATOM	2686	CB	ASN	B	139	−32.559	−21.104	124.220	1.00	27.61		C
ATOM	2687	CG	ASN	B	139	−31.415	−20.897	123.232	1.00	35.63		C
ATOM	2688	OD1	ASN	B	139	−31.150	−19.770	122.822	1.00	31.84		O
ATOM	2689	ND2	ASN	B	139	−30.785	−21.990	122.787	1.00	33.37		N
ATOM	2690	N	PHE	B	140	−36.249	−20.756	123.903	1.00	27.05		N
ATOM	2691	CA	PHE	B	140	−37.494	−21.275	124.449	1.00	28.39		C
ATOM	2692	C	PHE	B	140	−38.206	−22.147	123.413	1.00	30.25		C
ATOM	2693	O	PHE	B	140	−37.990	−22.032	122.203	1.00	30.54		O
ATOM	2694	CB	PHE	B	140	−38.430	−20.144	124.905	1.00	25.56		C
ATOM	2695	CG	PHE	B	140	−38.791	−19.192	123.813	1.00	27.91		C
ATOM	2696	CD1	PHE	B	140	−37.989	−18.086	123.541	1.00	25.72		C
ATOM	2697	CD2	PHE	B	140	−39.922	−19.410	123.030	1.00	27.50		C
ATOM	2698	CE1	PHE	B	140	−38.309	−17.202	122.515	1.00	24.13		C
ATOM	2699	CE2	PHE	B	140	−40.257	−18.524	122.002	1.00	29.76		C
ATOM	2700	CZ	PHE	B	140	−39.438	−17.415	121.744	1.00	27.82		C
ATOM	2701	N	TYR	B	141	−39.054	−23.030	123.914	1.00	27.15		N
ATOM	2702	CA	TYR	B	141	−39.947	−23.833	123.101	1.00	27.13		C
ATOM	2703	C	TYR	B	141	−41.183	−24.086	123.982	1.00	29.40		C
ATOM	2704	O	TYR	B	141	−41.048	−24.404	125.162	1.00	28.49		O
ATOM	2705	CB	TYR	B	141	−39.278	−25.150	122.634	1.00	27.47		C
ATOM	2706	CG	TYR	B	141	−40.171	−25.919	121.693	1.00	28.08		C
ATOM	2707	CD1	TYR	B	141	−41.133	−26.780	122.196	1.00	30.33		C
ATOM	2708	CD2	TYR	B	141	−40.098	−25.746	120.308	1.00	24.75		C
ATOM	2709	CE1	TYR	B	141	−42.002	−27.456	121.359	1.00	30.51		C
ATOM	2710	CE2	TYR	B	141	−40.969	−26.402	119.464	1.00	25.25		C
ATOM	2711	CZ	TYR	B	141	−41.930	−27.270	120.002	1.00	30.79		C
ATOM	2712	OH	TYR	B	141	−42.841	−27.974	119.229	1.00	28.57		O
ATOM	2713	N	PRO	B	142	−42.394	−23.975	123.414	1.00	29.92		N
ATOM	2714	CA	PRO	B	142	−42.663	−23.735	121.996	1.00	28.29		C
ATOM	2715	C	PRO	B	142	−42.638	−22.263	121.586	1.00	29.24		C
ATOM	2716	O	PRO	B	142	−42.345	−21.399	122.404	1.00	30.25		O
ATOM	2717	CB	PRO	B	142	−44.067	−24.327	121.825	1.00	28.67		C
ATOM	2718	CG	PRO	B	142	−44.726	−24.029	123.121	1.00	25.40		C
ATOM	2719	CD	PRO	B	142	−43.635	−24.261	124.160	1.00	27.51		C
ATOM	2720	N	ARG	B	143	−43.042	−22.022	120.332	1.00	33.09		N
ATOM	2721	CA	ARG	B	143	−42.828	−20.754	119.634	1.00	32.76		C
ATOM	2722	C	ARG	B	143	−43.567	−19.587	120.289	1.00	33.19		C
ATOM	2723	O	ARG	B	143	−43.061	−18.461	120.295	1.00	34.09		O
ATOM	2724	CB	ARG	B	143	−43.256	−20.953	118.174	1.00	30.54		C
ATOM	2725	CG	ARG	B	143	−43.343	−19.750	117.269	1.00	30.54		C
ATOM	2726	CD	ARG	B	143	−42.071	−19.508	116.495	1.00	35.91		C
ATOM	2727	NE	ARG	B	143	−42.253	−18.751	115.239	1.00	36.61		N
ATOM	2728	CZ	ARG	B	143	−42.878	−17.569	115.145	1.00	37.84		C
ATOM	2729	NH1	ARG	B	143	−43.464	−17.009	116.203	1.00	40.08		N1+
ATOM	2730	NH2	ARG	B	143	−42.943	−16.947	113.987	1.00	35.58		N
ATOM	2731	N	GLU	B	144	−44.743	−19.837	120.856	1.00	31.25		N
ATOM	2732	CA	GLU	B	144	−45.607	−18.768	121.346	1.00	35.56		C
ATOM	2733	C	GLU	B	144	−45.024	−18.121	122.602	1.00	34.95		C
ATOM	2734	O	GLU	B	144	−44.602	−18.808	123.537	1.00	34.88		O
ATOM	2735	CB	GLU	B	144	−47.021	−19.299	121.646	1.00	30.65		C
ATOM	2736	CG	GLU	B	144	−47.821	−19.817	120.448	1.00	34.84		C
ATOM	2737	CD	GLU	B	144	−47.385	−21.206	119.951	1.00	44.49		C
ATOM	2738	OE1	GLU	B	144	−47.117	−22.107	120.783	1.00	41.20		O
ATOM	2739	OE2	GLU	B	144	−47.333	−21.404	118.716	1.00	47.18		O1−
ATOM	2740	N	ALA	B	145	−45.002	−16.795	122.623	1.00	29.26		N
ATOM	2741	CA	ALA	B	145	−44.486	−16.077	123.774	1.00	34.47		C
ATOM	2742	C	ALA	B	145	−45.102	−14.691	123.756	1.00	33.83		C
ATOM	2743	O	ALA	B	145	−45.457	−14.194	122.684	1.00	35.59		O
ATOM	2744	CB	ALA	B	145	−42.952	−16.007	123.737	1.00	31.26		C
ATOM	2745	N	LYS	B	146	−45.250	−14.077	124.937	1.00	26.49		N
ATOM	2746	CA	LYS	B	146	−45.754	−12.707	125.026	1.00	28.76		C
ATOM	2747	C	LYS	B	146	−44.766	−11.790	125.756	1.00	32.11		C
ATOM	2748	O	LYS	B	146	−44.336	−12.085	126.880	1.00	25.51		O
ATOM	2749	CB	LYS	B	146	−47.130	−12.683	125.687	1.00	34.49		C
ATOM	2750	CG	LYS	B	146	−47.879	−11.354	125.547	1.00	44.62		C
ATOM	2751	CD	LYS	B	146	−49.339	−11.502	126.002	1.00	51.17		C
ATOM	2752	CE	LYS	B	146	−50.157	−10.231	125.771	1.00	55.61		C
ATOM	2753	NZ	LYS	B	146	−51.627	−10.552	125.678	1.00	51.90		N1+
ATOM	2754	N	VAL	B	147	−44.417	−10.672	125.113	1.00	32.22		N
ATOM	2755	CA	VAL	B	147	−43.616	−9.609	125.712	1.00	28.21		C
ATOM	2756	C	VAL	B	147	−44.534	−8.434	126.015	1.00	34.36		C
ATOM	2757	O	VAL	B	147	−45.332	−8.029	125.165	1.00	33.36		O
ATOM	2758	CB	VAL	B	147	−42.464	−9.160	124.794	1.00	27.98		C
ATOM	2759	CG1	VAL	B	147	−41.768	−7.931	125.372	1.00	29.12		C
ATOM	2760	CG2	VAL	B	147	−41.472	−10.275	124.560	1.00	32.19		C
ATOM	2761	N	GLN	B	148	−44.444	−7.904	127.230	1.00	35.67		N
ATOM	2762	CA	GLN	B	148	−45.128	−6.673	127.593	1.00	36.29		C
ATOM	2763	C	GLN	B	148	−44.100	−5.665	128.073	1.00	33.05		C
ATOM	2764	O	GLN	B	148	−43.303	−5.968	128.966	1.00	29.76		O
ATOM	2765	CB	GLN	B	148	−46.192	−6.913	128.676	1.00	36.98		C
ATOM	2766	CG	GLN	B	148	−47.614	−6.800	128.154	1.00	47.87		C
ATOM	2767	CD	GLN	B	148	−48.651	−7.188	129.192	1.00	64.59		C
ATOM	2768	OE1	GLN	B	148	−48.420	−7.050	130.398	1.00	64.90		O
ATOM	2769	NE2	GLN	B	148	−49.806	−7.674	128.728	1.00	58.09		N
ATOM	2770	N	TRP	B	149	−44.099	−4.485	127.465	1.00	34.92		N
ATOM	2771	CA	TRP	B	149	−43.234	−3.400	127.918	1.00	35.07		C
ATOM	2772	C	TRP	B	149	−43.941	−2.522	128.952	1.00	31.98		C
ATOM	2773	O	TRP	B	149	−45.105	−2.154	128.778	1.00	33.16		O
ATOM	2774	CB	TRP	B	149	−42.797	−2.549	126.730	1.00	28.25		C
ATOM	2775	CG	TRP	B	149	−41.704	−3.158	125.876	1.00	31.59		C
ATOM	2776	CD1	TRP	B	149	−41.851	−3.717	124.640	1.00	28.61		C
ATOM	2777	CD2	TRP	B	149	−40.305	−3.236	126.186	1.00	28.06		C
ATOM	2778	NE1	TRP	B	149	−40.640	−4.134	124.164	1.00	31.98		N
ATOM	2779	CE2	TRP	B	149	−39.671	−3.852	125.091	1.00	31.31		C
ATOM	2780	CE3	TRP	B	149	−39.529	−2.842	127.280	1.00	32.39		C
ATOM	2781	CZ2	TRP	B	149	−38.289	−4.080	125.048	1.00	29.16		C
ATOM	2782	CZ3	TRP	B	149	−38.159	−3.066	127.242	1.00	36.30		C
ATOM	2783	CH2	TRP	B	149	−37.550	−3.676	126.125	1.00	32.50		C
ATOM	2784	N	LYS	B	150	−43.228	−2.174	130.023	1.00	34.33		N
ATOM	2785	CA	LYS	B	150	−43.736	−1.240	131.030	1.00	35.21		C
ATOM	2786	C	LYS	B	150	−42.711	−0.143	131.257	1.00	36.04		C
ATOM	2787	O	LYS	B	150	−41.534	−0.433	131.489	1.00	40.23		O
ATOM	2788	CB	LYS	B	150	−44.050	−1.918	132.374	1.00	29.19		C
ATOM	2789	CG	LYS	B	150	−45.326	−2.755	132.421	1.00	32.86		C
ATOM	2790	CD	LYS	B	150	−45.296	−3.677	133.643	1.00	42.43		C
ATOM	2791	CE	LYS	B	150	−46.327	−4.800	133.536	1.00	54.13		C
ATOM	2792	NZ	LYS	B	150	−46.598	−5.502	134.839	1.00	48.84		N1+
ATOM	2793	N	VAL	B	151	−43.158	1.107	131.189	1.00	34.12		N
ATOM	2794	CA	VAL	B	151	−42.355	2.270	131.559	1.00	34.61		C
ATOM	2795	C	VAL	B	151	−43.003	2.921	132.784	1.00	36.08		C
ATOM	2796	O	VAL	B	151	−44.118	3.448	132.699	1.00	35.70		O
ATOM	2797	CB	VAL	B	151	−42.241	3.255	130.392	1.00	31.07		C
ATOM	2798	CG1	VAL	B	151	−41.307	4.377	130.732	1.00	31.60		C
ATOM	2799	CG2	VAL	B	151	−41.752	2.528	129.173	1.00	37.80		C
ATOM	2800	N	ASP	B	152	−42.299	2.902	133.921	1.00	39.23		N
ATOM	2801	CA	ASP	B	152	−42.854	3.340	135.217	1.00	38.88		C
ATOM	2802	C	ASP	B	152	−44.243	2.743	135.428	1.00	37.74		C
ATOM	2803	O	ASP	B	152	−45.194	3.412	135.836	1.00	35.76		O
ATOM	2804	CB	ASP	B	152	−42.848	4.863	135.343	1.00	36.31		C
ATOM	2805	CG	ASP	B	152	−41.451	5.404	135.628	1.00	44.31		C
ATOM	2806	OD1	ASP	B	152	−40.688	4.719	136.357	1.00	39.45		O
ATOM	2807	OD2	ASP	B	152	−41.093	6.479	135.094	1.00	46.68		O1−
ATOM	2808	N	ASN	B	153	−44.333	1.457	135.097	1.00	38.94		N
ATOM	2809	CA	ASN	B	153	−45.491	0.579	135.212	1.00	39.28		C
ATOM	2810	C	ASN	B	153	−46.660	0.990	134.321	1.00	37.08		C
ATOM	2811	O	ASN	B	153	−47.783	0.508	134.502	1.00	39.74		O
ATOM	2812	CB	ASN	B	153	−45.933	0.433	136.666	1.00	37.94		C
ATOM	2813	CG	ASN	B	153	−46.502	−0.927	136.937	1.00	41.53		C
ATOM	2814	OD1	ASN	B	153	−47.693	−1.071	137.197	1.00	48.49		O
ATOM	2815	ND2	ASN	B	153	−45.658	−1.953	136.827	1.00	47.40		N
ATOM	2816	N	ALA	B	154	−46.418	1.824	133.322	1.00	27.73		N
ATOM	2817	CA	ALA	B	154	−47.403	2.060	132.281	1.00	31.59		C
ATOM	2818	C	ALA	B	154	−47.152	1.064	131.145	1.00	35.73		C
ATOM	2819	O	ALA	B	154	−46.034	1.006	130.611	1.00	34.76		O
ATOM	2820	CB	ALA	B	154	−47.314	3.503	131.785	1.00	30.19		C
ATOM	2821	N	LEU	B	155	−48.168	0.246	130.817	1.00	31.02		N
ATOM	2822	CA	LEU	B	155	−48.092	−0.680	129.680	1.00	29.47		C
ATOM	2823	C	LEU	B	155	−47.940	0.045	128.364	1.00	29.26		C
ATOM	2824	O	LEU	B	155	−48.816	0.809	127.967	1.00	32.19		O
ATOM	2825	CB	LEU	B	155	−49.321	−1.578	129.581	1.00	26.14		C
ATOM	2826	CG	LEU	B	155	−49.137	−2.963	130.188	1.00	41.59		C
ATOM	2827	CD1	LEU	B	155	−49.358	−2.997	131.716	1.00	37.40		C
ATOM	2828	CD2	LEU	B	155	−49.966	−3.985	129.430	1.00	49.03		C
ATOM	2829	N	GLN	B	156	−46.891	−0.293	127.632	1.00	32.37		N
ATOM	2830	CA	GLN	B	156	−46.687	0.225	126.289	1.00	31.54		C
ATOM	2831	C	GLN	B	156	−47.433	−0.647	125.293	1.00	27.02		C
ATOM	2832	O	GLN	B	156	−47.493	−1.864	125.444	1.00	36.94		O
ATOM	2833	CB	GLN	B	156	−45.193	0.270	125.966	1.00	31.74		C
ATOM	2834	CG	GLN	B	156	−44.395	0.948	127.069	1.00	31.12		C
ATOM	2835	CD	GLN	B	156	−44.877	2.358	127.299	1.00	33.29		C
ATOM	2836	OE1	GLN	B	156	−44.789	3.213	126.412	1.00	33.92		O
ATOM	2837	NE2	GLN	B	156	−45.445	2.599	128.470	1.00	34.06		N
ATOM	2838	N	SER	B	157	−48.069	−0.017	124.322	1.00	25.15		N
ATOM	2839	CA	SER	B	157	−48.818	−0.745	123.309	1.00	24.13		C
ATOM	2840	C	SER	B	157	−48.684	0.008	121.998	1.00	28.91		C
ATOM	2841	O	SER	B	157	−49.132	1.153	121.903	1.00	33.39		O
ATOM	2842	CB	SER	B	157	−50.284	−0.869	123.724	1.00	27.59		C
ATOM	2843	OG	SER	B	157	−51.056	−1.511	122.738	1.00	34.07		O
ATOM	2844	N	GLY	B	158	−48.052	−0.597	121.005	1.00	23.39		N
ATOM	2845	CA	GLY	B	158	−47.959	0.017	119.698	1.00	22.69		C
ATOM	2846	C	GLY	B	158	−46.630	0.665	119.370	1.00	26.97		C
ATOM	2847	O	GLY	B	158	−46.467	1.166	118.256	1.00	30.74		O
ATOM	2848	N	ASN	B	159	−45.695	0.721	120.312	1.00	26.14		N
ATOM	2849	CA	ASN	B	159	−44.412	1.373	120.086	1.00	25.51		C
ATOM	2850	C	ASN	B	159	−43.236	0.401	120.206	1.00	30.63		C
ATOM	2851	O	ASN	B	159	−42.149	0.779	120.660	1.00	25.81		O
ATOM	2852	CB	ASN	B	159	−44.236	2.542	121.043	1.00	22.42		C
ATOM	2853	CG	ASN	B	159	−44.537	2.165	122.463	1.00	29.01		C
ATOM	2854	OD1	ASN	B	159	−44.940	1.021	122.757	1.00	30.10		O
ATOM	2855	ND2	ASN	B	159	−44.335	3.114	123.370	1.00	32.61		N
ATOM	2856	N	SER	B	160	−43.439	−0.859	119.819	1.00	27.65		N
ATOM	2857	CA	SER	B	160	−42.360	−1.827	119.814	1.00	29.05		C
ATOM	2858	C	SER	B	160	−42.510	−2.753	118.615	1.00	28.89		C
ATOM	2859	O	SER	B	160	−43.602	−2.939	118.089	1.00	29.48		O
ATOM	2860	CB	SER	B	160	−42.328	−2.626	121.112	1.00	26.29		C
ATOM	2861	OG	SER	B	160	−43.447	−3.475	121.181	1.00	31.67		O
ATOM	2862	N	GLN	B	161	−41.400	−3.357	118.197	1.00	28.03		N
ATOM	2863	CA	GLN	B	161	−41.425	−4.362	117.147	1.00	26.96		C
ATOM	2864	C	GLN	B	161	−40.634	−5.596	117.581	1.00	31.51		C
ATOM	2865	O	GLN	B	161	−39.759	−5.537	118.451	1.00	30.01		O
ATOM	2866	CB	GLN	B	161	−40.871	−3.794	115.850	1.00	27.24		C
ATOM	2867	CG	GLN	B	161	−41.747	−2.764	115.183	1.00	27.43		C
ATOM	2868	CD	GLN	B	161	−41.064	−2.142	113.976	1.00	35.97		C
ATOM	2869	OE1	GLN	B	161	−40.203	−1.267	114.121	1.00	35.92		O
ATOM	2870	NE2	GLN	B	161	−41.418	−2.607	112.782	1.00	30.28		N
ATOM	2871	N	GLU	B	162	−40.938	−6.720	116.938	1.00	31.79		N
ATOM	2872	CA	GLU	B	162	−40.438	−8.034	117.331	1.00	29.63		C
ATOM	2873	C	GLU	B	162	−40.040	−8.837	116.104	1.00	30.95		C
ATOM	2874	O	GLU	B	162	−40.654	−8.718	115.042	1.00	26.14		O
ATOM	2875	CB	GLU	B	162	−41.503	−8.877	117.989	1.00	23.86		C
ATOM	2876	CG	GLU	B	162	−41.567	−8.969	119.420	1.00	34.85		C
ATOM	2877	CD	GLU	B	162	−42.807	−9.765	119.781	1.00	41.65		C
ATOM	2878	OE1	GLU	B	162	−43.430	−10.284	118.835	1.00	38.04		O
ATOM	2879	OE2	GLU	B	162	−43.177	−9.858	120.973	1.00	45.93		O1−
ATOM	2880	N	SER	B	163	−39.057	−9.712	116.280	1.00	31.61		N
ATOM	2881	CA	SER	B	163	−38.794	−10.763	115.312	1.00	25.04		C
ATOM	2882	C	SER	B	163	−38.348	−11.995	116.088	1.00	28.10		C
ATOM	2883	O	SER	B	163	−37.857	−11.890	117.218	1.00	25.85		O
ATOM	2884	CB	SER	B	163	−37.781	−10.326	114.254	1.00	26.93		C
ATOM	2885	OG	SER	B	163	−36.461	−10.447	114.714	1.00	29.93		O
ATOM	2886	N	VAL	B	164	−38.587	−13.169	115.504	1.00	29.93		N
ATOM	2887	CA	VAL	B	164	−38.200	−14.441	116.104	1.00	26.45		C
ATOM	2888	C	VAL	B	164	−37.323	−15.214	115.130	1.00	23.48		C
ATOM	2889	O	VAL	B	164	−37.520	−15.156	113.918	1.00	28.17		O
ATOM	2890	CB	VAL	B	164	−39.430	−15.281	116.521	1.00	30.77		C
ATOM	2891	CG1	VAL	B	164	−40.375	−14.468	117.392	1.00	26.66		C
ATOM	2892	CG2	VAL	B	164	−40.156	−15.786	115.308	1.00	40.64		C
ATOM	2893	N	THR	B	165	−36.328	−15.908	115.663	1.00	28.51		N
ATOM	2894	CA	THR	B	165	−35.442	−16.716	114.848	1.00	27.61		C
ATOM	2895	C	THR	B	165	−36.154	−17.967	114.344	1.00	29.58		C
ATOM	2896	O	THR	B	165	−37.279	−18.300	114.751	1.00	28.80		O
ATOM	2897	CB	THR	B	165	−34.195	−17.113	115.641	1.00	28.32		C
ATOM	2898	OG1	THR	B	165	−34.575	−17.596	116.939	1.00	33.79		O
ATOM	2899	CG2	THR	B	165	−33.275	−15.942	115.795	1.00	25.22		C
ATOM	2900	N	GLU	B	166	−35.489	−18.634	113.402	1.00	28.57		N
ATOM	2901	CA	GLU	B	166	−35.851	−19.992	113.026	1.00	29.18		C
ATOM	2902	C	GLU	B	166	−35.474	−20.953	114.149	1.00	25.81		C
ATOM	2903	O	GLU	B	166	−34.705	−20.622	115.046	1.00	28.21		O
ATOM	2904	CB	GLU	B	166	−35.158	−20.398	111.722	1.00	25.69		C
ATOM	2905	CG	GLU	B	166	−35.615	−19.673	110.472	1.00	23.14		C
ATOM	2906	CD	GLU	B	166	−37.112	−19.776	110.263	1.00	35.69		C
ATOM	2907	OE1	GLU	B	166	−37.691	−20.801	110.689	1.00	45.01		O
ATOM	2908	OE2	GLU	B	166	−37.715	−18.853	109.661	1.00	37.00		O1−
ATOM	2909	N	GLN	B	167	−36.061	−22.138	114.120	1.00	29.35		N
ATOM	2910	CA	GLN	B	167	−35.749	−23.146	115.126	1.00	27.70		C
ATOM	2911	C	GLN	B	167	−34.250	−23.426	115.143	1.00	26.23		C
ATOM	2912	O	GLN	B	167	−33.622	−23.530	114.093	1.00	25.94		O
ATOM	2913	CB	GLN	B	167	−36.538	−24.406	114.823	1.00	25.14		C
ATOM	2914	CG	GLN	B	167	−36.995	−25.171	116.012	1.00	27.67		C
ATOM	2915	CD	GLN	B	167	−38.037	−26.211	115.661	1.00	25.13		C
ATOM	2916	OE1	GLN	B	167	−38.324	−26.473	114.489	1.00	27.17		O
ATOM	2917	NE2	GLN	B	167	−38.591	−26.819	116.672	1.00	23.92		N
ATOM	2918	N	ASP	B	168	−33.660	−23.496	116.338	1.00	30.80		N
ATOM	2919	CA	ASP	B	168	−32.202	−23.493	116.448	1.00	28.93		C
ATOM	2920	C	ASP	B	168	−31.602	−24.806	115.962	1.00	31.78		C
ATOM	2921	O	ASP	B	168	−31.981	−25.882	116.433	1.00	30.59		O
ATOM	2922	CB	ASP	B	168	−31.771	−23.268	117.895	1.00	31.58		C
ATOM	2923	CG	ASP	B	168	−30.269	−23.104	118.028	1.00	34.74		C
ATOM	2924	OD1	ASP	B	168	−29.610	−24.086	118.410	1.00	36.21		O1−
ATOM	2925	OD2	ASP	B	168	−29.737	−22.026	117.677	1.00	38.15		O
ATOM	2926	N	SER	B	169	−30.583	−24.714	115.101	1.00	37.85		N
ATOM	2927	CA	SER	B	169	−30.001	−25.906	114.488	1.00	32.86		C
ATOM	2928	C	SER	B	169	−29.342	−26.845	115.487	1.00	33.78		C
ATOM	2929	O	SER	B	169	−29.068	−27.992	115.126	1.00	37.40		O
ATOM	2930	CB	SER	B	169	−28.999	−25.515	113.412	1.00	35.71		C
ATOM	2931	OG	SER	B	169	−27.919	−24.817	113.973	1.00	45.05		O
ATOM	2932	N	LYS	B	170	−29.105	−26.415	116.725	1.00	35.30		N
ATOM	2933	CA	LYS	B	170	−28.484	−27.260	117.742	1.00	32.69		C
ATOM	2934	C	LYS	B	170	−29.445	−27.779	118.816	1.00	33.51		C
ATOM	2935	O	LYS	B	170	−29.365	−28.957	119.161	1.00	33.92		O
ATOM	2936	CB	LYS	B	170	−27.311	−26.510	118.389	1.00	32.22		C
ATOM	2937	CG	LYS	B	170	−26.523	−27.313	119.398	1.00	35.45		C
ATOM	2938	CD	LYS	B	170	−25.696	−26.399	120.284	1.00	39.33		C
ATOM	2939	CE	LYS	B	170	−24.687	−27.150	121.125	1.00	41.85		C
ATOM	2940	NZ	LYS	B	170	−23.466	−26.291	121.260	1.00	49.14		N1+
ATOM	2941	N	ASP	B	171	−30.386	−26.985	119.360	1.00	29.53		N
ATOM	2942	CA	ASP	B	171	−31.298	−27.535	120.366	1.00	24.54		C
ATOM	2943	C	ASP	B	171	−32.772	−27.335	120.036	1.00	25.46		C
ATOM	2944	O	ASP	B	171	−33.615	−27.519	120.926	1.00	22.30		O
ATOM	2945	CB	ASP	B	171	−31.001	−27.011	121.795	1.00	25.26		C
ATOM	2946	CG	ASP	B	171	−31.151	−25.471	121.965	1.00	35.81		C
ATOM	2947	OD1	ASP	B	171	−31.871	−24.789	121.205	1.00	38.80		O
ATOM	2948	OD2	ASP	B	171	−30.555	−24.925	122.927	1.00	42.26		O1−
ATOM	2949	N	SER	B	172	−33.096	−26.958	118.791	1.00	24.40		N
ATOM	2950	CA	SER	B	172	−34.458	−26.783	118.271	1.00	22.81		C
ATOM	2951	C	SER	B	172	−35.296	−25.735	119.023	1.00	29.46		C
ATOM	2952	O	SER	B	172	−36.540	−25.777	118.980	1.00	30.46		O
ATOM	2953	CB	SER	B	172	−35.204	−28.122	118.240	1.00	27.26		C
ATOM	2954	OG	SER	B	172	−34.476	−29.076	117.480	1.00	29.50		O
ATOM	2955	N	THR	B	173	−34.685	−24.758	119.688	1.00	26.53		N
ATOM	2956	CA	THR	B	173	−35.479	−23.750	120.371	1.00	30.13		C
ATOM	2957	C	THR	B	173	−35.667	−22.512	119.487	1.00	28.94		C
ATOM	2958	O	THR	B	173	−35.137	−22.397	118.377	1.00	28.80		O
ATOM	2959	CB	THR	B	173	−34.869	−23.380	121.742	1.00	29.06		C
ATOM	2960	OG1	THR	B	173	−33.536	−22.886	121.592	1.00	27.56		O
ATOM	2961	CG2	THR	B	173	−34.849	−24.577	122.671	1.00	23.15		C
ATOM	2962	N	TYR	B	174	−36.479	−21.598	119.989	1.00	27.86		N
ATOM	2963	CA	TYR	B	174	−36.710	−20.306	119.375	1.00	27.59		C
ATOM	2964	C	TYR	B	174	−36.103	−19.210	120.245	1.00	28.01		C
ATOM	2965	O	TYR	B	174	−35.906	−19.388	121.452	1.00	28.60		O
ATOM	2966	CB	TYR	B	174	−38.210	−20.069	119.181	1.00	27.30		C
ATOM	2967	CG	TYR	B	174	−38.818	−20.983	118.147	1.00	30.86		C
ATOM	2968	CD1	TYR	B	174	−38.743	−20.672	116.791	1.00	26.78		C
ATOM	2969	CD2	TYR	B	174	−39.452	−22.171	118.521	1.00	31.18		C
ATOM	2970	CE1	TYR	B	174	−39.283	−21.496	115.842	1.00	27.76		C
ATOM	2971	CE2	TYR	B	174	−39.994	−23.016	117.567	1.00	30.49		C
ATOM	2972	CZ	TYR	B	174	−39.906	−22.666	116.224	1.00	31.46		C
ATOM	2973	OH	TYR	B	174	−40.448	−23.480	115.262	1.00	32.46		O
ATOM	2974	N	SER	B	175	−35.773	−18.087	119.621	1.00	26.84		N
ATOM	2975	CA	SER	B	175	−35.396	−16.886	120.355	1.00	28.52		C
ATOM	2976	C	SER	B	175	−36.172	−15.696	119.814	1.00	28.84		C
ATOM	2977	O	SER	B	175	−36.595	−15.687	118.656	1.00	24.93		O
ATOM	2978	CB	SER	B	175	−33.904	−16.608	120.274	1.00	31.06		C
ATOM	2979	OG	SER	B	175	−33.199	−17.479	121.133	1.00	35.19		O
ATOM	2980	N	LEU	B	176	−36.367	−14.694	120.671	1.00	29.11		N
ATOM	2981	CA	LEU	B	176	−37.165	−13.529	120.323	1.00	27.58		C
ATOM	2982	C	LEU	B	176	−36.445	−12.262	120.739	1.00	24.37		C
ATOM	2983	O	LEU	B	176	−35.796	−12.218	121.779	1.00	27.04		O
ATOM	2984	CB	LEU	B	176	−38.553	−13.589	120.973	1.00	29.13		C
ATOM	2985	CG	LEU	B	176	−39.558	−12.517	120.560	1.00	30.07		C
ATOM	2986	CD1	LEU	B	176	−40.920	−13.129	120.631	1.00	30.39		C
ATOM	2987	CD2	LEU	B	176	−39.485	−11.303	121.483	1.00	24.93		C
ATOM	2988	N	SER	B	177	−36.556	−11.235	119.905	1.00	29.33		N
ATOM	2989	CA	SER	B	177	−35.972	−9.932	120.178	1.00	26.82		C
ATOM	2990	C	SER	B	177	−37.041	−8.863	119.992	1.00	27.17		C
ATOM	2991	O	SER	B	177	−37.669	−8.809	118.934	1.00	25.25		O
ATOM	2992	CB	SER	B	177	−34.782	−9.694	119.255	1.00	26.28		C
ATOM	2993	OG	SER	B	177	−34.307	−8.377	119.379	1.00	27.89		O
ATOM	2994	N	SER	B	178	−37.232	−8.006	121.013	1.00	25.92		N
ATOM	2995	CA	SER	B	178	−38.255	−6.966	121.020	1.00	23.84		C
ATOM	2996	C	SER	B	178	−37.624	−5.603	121.261	1.00	27.80		C
ATOM	2997	O	SER	B	178	−36.822	−5.443	122.189	1.00	29.43		O
ATOM	2998	CB	SER	B	178	−39.308	−7.226	122.096	1.00	28.27		C
ATOM	2999	OG	SER	B	178	−40.307	−6.215	122.090	1.00	26.54		O
ATOM	3000	N	THR	B	179	−38.007	−4.617	120.444	1.00	26.02		N
ATOM	3001	CA	THR	B	179	−37.450	−3.266	120.535	1.00	30.99		C
ATOM	3002	C	THR	B	179	−38.536	−2.247	120.809	1.00	25.23		C
ATOM	3003	O	THR	B	179	−39.357	−1.967	119.938	1.00	24.43		O
ATOM	3004	CB	THR	B	179	−36.714	−2.839	119.274	1.00	31.29		C
ATOM	3005	OG1	THR	B	179	−35.681	−3.781	118.962	1.00	35.76		O
ATOM	3006	CG2	THR	B	179	−36.121	−1.472	119.512	1.00	23.65		C
ATOM	3007	N	LEU	B	180	−38.489	−1.662	121.997	1.00	26.49		N
ATOM	3008	CA	LEU	B	180	−39.263	−0.482	122.349	1.00	28.48		C
ATOM	3009	C	LEU	B	180	−38.502	0.769	121.939	1.00	24.67		C
ATOM	3010	O	LEU	B	180	−37.356	0.949	122.350	1.00	26.90		O
ATOM	3011	CB	LEU	B	180	−39.510	−0.482	123.855	1.00	30.84		C
ATOM	3012	CG	LEU	B	180	−40.291	0.643	124.498	1.00	34.83		C
ATOM	3013	CD1	LEU	B	180	−41.724	0.580	123.976	1.00	34.95		C
ATOM	3014	CD2	LEU	B	180	−40.215	0.471	126.015	1.00	31.30		C
ATOM	3015	N	THR	B	181	−39.142	1.642	121.161	1.00	25.09		N
ATOM	3016	CA	THR	B	181	−38.529	2.892	120.712	1.00	34.09		C
ATOM	3017	C	THR	B	181	−39.245	4.090	121.341	1.00	40.80		C
ATOM	3018	O	THR	B	181	−40.484	4.142	121.354	1.00	36.26		O
ATOM	3019	CB	THR	B	181	−38.548	3.005	119.181	1.00	33.92		C
ATOM	3020	OG1	THR	B	181	−37.870	1.881	118.610	1.00	36.57		O
ATOM	3021	CG2	THR	B	181	−37.793	4.230	118.744	1.00	36.41		C
ATOM	3022	N	LEU	B	182	−38.452	5.031	121.882	1.00	36.61		N
ATOM	3023	CA	LEU	B	182	−38.910	6.286	122.483	1.00	33.83		C
ATOM	3024	C	LEU	B	182	−38.034	7.434	121.997	1.00	37.62		C
ATOM	3025	O	LEU	B	182	−36.923	7.235	121.506	1.00	36.88		O
ATOM	3026	CB	LEU	B	182	−38.837	6.287	124.017	1.00	39.93		C
ATOM	3027	CG	LEU	B	182	−39.550	5.271	124.901	1.00	43.75		C
ATOM	3028	CD1	LEU	B	182	−39.188	5.503	126.364	1.00	42.80		C
ATOM	3029	CD2	LEU	B	182	−41.051	5.401	124.698	1.00	48.91		C
ATOM	3030	N	SER	B	183	−38.515	8.653	122.183	1.00	40.17		N
ATOM	3031	CA	SER	B	183	−37.616	9.784	122.023	1.00	39.39		C
ATOM	3032	C	SER	B	183	−36.639	9.844	123.195	1.00	39.08		C
ATOM	3033	O	SER	B	183	−36.882	9.278	124.259	1.00	39.26		O
ATOM	3034	CB	SER	B	183	−38.401	11.088	121.963	1.00	38.95		C
ATOM	3035	OG	SER	B	183	−39.031	11.322	123.210	1.00	35.92		O
ATOM	3036	N	LYS	B	184	−35.510	10.530	122.986	1.00	42.26		N
ATOM	3037	CA	LYS	B	184	−34.617	10.803	124.109	1.00	40.17		C
ATOM	3038	C	LYS	B	184	−35.348	11.566	125.208	1.00	41.28		C
ATOM	3039	O	LYS	B	184	−35.138	11.310	126.401	1.00	38.53		O
ATOM	3040	CB	LYS	B	184	−33.405	11.605	123.646	1.00	42.87		C
ATOM	3041	CG	LYS	B	184	−32.462	11.986	124.806	1.00	52.77		C
ATOM	3042	CD	LYS	B	184	−31.228	12.771	124.339	1.00	51.17		C
ATOM	3043	CE	LYS	B	184	−30.325	13.153	125.500	1.00	56.17		C
ATOM	3044	NZ	LYS	B	184	−30.191	14.632	125.670	1.00	63.96		N1+
ATOM	3045	N	ALA	B	185	−36.219	12.500	124.816	1.00	39.51		N
ATOM	3046	CA	ALA	B	185	−36.995	13.275	125.780	1.00	38.41		C
ATOM	3047	C	ALA	B	185	−37.914	12.389	126.613	1.00	39.82		C
ATOM	3048	O	ALA	B	185	−37.897	12.456	127.844	1.00	44.20		O
ATOM	3049	CB	ALA	B	185	−37.806	14.346	125.057	1.00	33.82		C
ATOM	3050	N	ASP	B	186	−38.764	11.591	125.959	1.00	42.91		N
ATOM	3051	CA	ASP	B	186	−39.646	10.690	126.697	1.00	37.37		C
ATOM	3052	C	ASP	B	186	−38.844	9.750	127.573	1.00	37.99		C
ATOM	3053	O	ASP	B	186	−39.192	9.506	128.736	1.00	37.79		O
ATOM	3054	CB	ASP	B	186	−40.512	9.876	125.739	1.00	42.26		C
ATOM	3055	CG	ASP	B	186	−41.589	10.703	125.065	1.00	48.82		C
ATOM	3056	OD1	ASP	B	186	−42.264	11.496	125.752	1.00	49.68		O
ATOM	3057	OD2	ASP	B	186	−41.778	10.531	123.839	1.00	61.13		O1−
ATOM	3058	N	TYR	B	187	−37.781	9.181	127.006	1.00	41.31		N
ATOM	3059	CA	TYR	B	187	−36.932	8.262	127.745	1.00	37.24		C
ATOM	3060	C	TYR	B	187	−36.398	8.907	129.016	1.00	35.05		C
ATOM	3061	O	TYR	B	187	−36.349	8.272	130.075	1.00	36.76		O
ATOM	3062	CB	TYR	B	187	−35.786	7.785	126.852	1.00	37.33		C
ATOM	3063	CG	TYR	B	187	−34.823	6.915	127.604	1.00	37.18		C
ATOM	3064	CD1	TYR	B	187	−35.223	5.663	128.068	1.00	34.09		C
ATOM	3065	CD2	TYR	B	187	−33.539	7.359	127.900	1.00	27.91		C
ATOM	3066	CE1	TYR	B	187	−34.363	4.870	128.780	1.00	33.76		C
ATOM	3067	CE2	TYR	B	187	−32.678	6.577	128.618	1.00	30.33		C
ATOM	3068	CZ	TYR	B	187	−33.090	5.328	129.058	1.00	31.48		C
ATOM	3069	OH	TYR	B	187	−32.233	4.528	129.785	1.00	31.99		O
ATOM	3070	N	GLU	B	188	−35.991	10.166	128.935	1.00	39.77		N
ATOM	3071	CA	GLU	B	188	−35.344	10.782	130.083	1.00	44.77		C
ATOM	3072	C	GLU	B	188	−36.325	11.334	131.097	1.00	40.36		C
ATOM	3073	O	GLU	B	188	−35.879	11.832	132.131	1.00	41.81		O
ATOM	3074	CB	GLU	B	188	−34.358	11.849	129.625	1.00	39.20		C
ATOM	3075	CG	GLU	B	188	−32.978	11.224	129.620	1.00	45.15		C
ATOM	3076	CD	GLU	B	188	−31.974	11.914	128.723	1.00	56.05		C
ATOM	3077	OE1	GLU	B	188	−32.317	12.924	128.049	1.00	48.75		O
ATOM	3078	OE2	GLU	B	188	−30.831	11.394	128.688	1.00	59.27		O1−
ATOM	3079	N	LYS	B	189	−37.630	11.197	130.852	1.00	37.43		N
ATOM	3080	CA	LYS	B	189	−38.687	11.560	131.788	1.00	38.07		C
ATOM	3081	C	LYS	B	189	−39.236	10.363	132.579	1.00	40.62		C
ATOM	3082	O	LYS	B	189	−40.315	10.465	133.167	1.00	46.60		O
ATOM	3083	CB	LYS	B	189	−39.813	12.270	131.030	1.00	37.89		C
ATOM	3084	CG	LYS	B	189	−39.327	13.568	130.380	1.00	51.23		C
ATOM	3085	CD	LYS	B	189	−40.333	14.215	129.404	1.00	62.14		C
ATOM	3086	CE	LYS	B	189	−39.717	15.470	128.720	1.00	60.71		C
ATOM	3087	NZ	LYS	B	189	−40.587	16.123	127.684	1.00	51.31		N1+
ATOM	3088	N	HIS	B	190	−38.541	9.223	132.588	1.00	41.83		N
ATOM	3089	CA	HIS	B	190	−39.025	8.026	133.271	1.00	35.94		C
ATOM	3090	C	HIS	B	190	−37.865	7.259	133.879	1.00	35.72		C
ATOM	3091	O	HIS	B	190	−36.701	7.484	133.543	1.00	36.41		O
ATOM	3092	CB	HIS	B	190	−39.810	7.120	132.337	1.00	37.87		C
ATOM	3093	CG	HIS	B	190	−41.069	7.745	131.840	1.00	37.33		C
ATOM	3094	ND1	HIS	B	190	−41.173	8.323	130.596	1.00	40.44		N
ATOM	3095	CD2	HIS	B	190	−42.264	7.926	132.442	1.00	37.28		C
ATOM	3096	CE1	HIS	B	190	−42.386	8.813	130.442	1.00	36.52		C
ATOM	3097	NE2	HIS	B	190	−43.068	8.583	131.548	1.00	42.61		N
ATOM	3098	N	LYS	B	191	−38.188	6.365	134.806	1.00	32.95		N
ATOM	3099	CA	LYS	B	191	−37.139	5.707	135.580	1.00	44.01		C
ATOM	3100	C	LYS	B	191	−37.065	4.204	135.352	1.00	37.37		C
ATOM	3101	O	LYS	B	191	−35.988	3.687	135.032	1.00	37.81		O
ATOM	3102	CB	LYS	B	191	−37.316	6.017	137.084	1.00	41.79		C
ATOM	3103	CG	LYS	B	191	−36.346	5.312	138.042	1.00	43.26		C
ATOM	3104	CD	LYS	B	191	−36.731	5.623	139.511	1.00	54.07		C
ATOM	3105	CE	LYS	B	191	−35.668	5.177	140.515	1.00	56.60		C
ATOM	3106	NZ	LYS	B	191	−36.031	5.546	141.905	1.00	51.73		N1+
ATOM	3107	N	VAL	B	192	−38.164	3.482	135.530	1.00	31.57		N
ATOM	3108	CA	VAL	B	192	−38.156	2.027	135.503	1.00	34.89		C
ATOM	3109	C	VAL	B	192	−38.596	1.564	134.126	1.00	35.04		C
ATOM	3110	O	VAL	B	192	−39.687	1.918	133.661	1.00	35.31		O
ATOM	3111	CB	VAL	B	192	−39.054	1.439	136.599	1.00	34.98		C
ATOM	3112	CG1	VAL	B	192	−39.122	−0.073	136.464	1.00	30.15		C
ATOM	3113	CG2	VAL	B	192	−38.522	1.842	137.965	1.00	36.73		C
ATOM	3114	N	TYR	B	193	−37.737	0.785	133.473	1.00	36.15		N
ATOM	3115	CA	TYR	B	193	−38.019	0.172	132.181	1.00	35.85		C
ATOM	3116	C	TYR	B	193	−38.078	−1.327	132.381	1.00	29.50		C
ATOM	3117	O	TYR	B	193	−37.178	−1.898	132.995	1.00	31.86		O
ATOM	3118	CB	TYR	B	193	−36.958	0.576	131.150	1.00	28.31		C
ATOM	3119	CG	TYR	B	193	−37.137	2.020	130.781	1.00	32.21		C
ATOM	3120	CD1	TYR	B	193	−36.656	3.034	131.613	1.00	34.12		C
ATOM	3121	CD2	TYR	B	193	−37.831	2.384	129.628	1.00	32.20		C
ATOM	3122	CE1	TYR	B	193	−36.859	4.366	131.313	1.00	31.90		C
ATOM	3123	CE2	TYR	B	193	−38.023	3.724	129.299	1.00	38.14		C
ATOM	3124	CZ	TYR	B	193	−37.536	4.707	130.163	1.00	37.14		C
ATOM	3125	OH	TYR	B	193	−37.717	6.025	129.872	1.00	39.52		O
ATOM	3126	N	ALA	B	194	−39.149	−1.954	131.908	1.00	28.74		N
ATOM	3127	CA	ALA	B	194	−39.300	−3.384	132.148	1.00	34.71		C
ATOM	3128	C	ALA	B	194	−39.970	−4.081	130.963	1.00	33.72		C
ATOM	3129	O	ALA	B	194	−40.748	−3.479	130.211	1.00	34.66		O
ATOM	3130	CB	ALA	B	194	−40.083	−3.634	133.442	1.00	29.91		C
ATOM	3131	N	CYS	B	195	−39.623	−5.349	130.776	1.00	32.36		N
ATOM	3132	CA	CYS	B	195	−40.382	−6.251	129.919	1.00	37.46		C
ATOM	3133	C	CYS	B	195	−40.814	−7.461	130.732	1.00	40.08		C
ATOM	3134	O	CYS	B	195	−40.045	−8.000	131.544	1.00	39.11		O
ATOM	3135	CB	CYS	B	195	−39.615	−6.703	128.639	1.00	33.36		C
ATOM	3136	SG	CYS	B	195	−37.984	−7.394	128.903	1.00	49.70		S
ATOM	3137	N	GLU	B	196	−42.077	−7.822	130.550	1.00	36.65		N
ATOM	3138	CA	GLU	B	196	−42.702	−8.939	131.228	1.00	37.99		C
ATOM	3139	C	GLU	B	196	−42.961	−10.009	130.181	1.00	33.89		C
ATOM	3140	O	GLU	B	196	−43.502	−9.711	129.111	1.00	30.27		O
ATOM	3141	CB	GLU	B	196	−43.986	−8.481	131.926	1.00	37.34		C
ATOM	3142	CG	GLU	B	196	−44.748	−9.548	132.707	1.00	42.18		C
ATOM	3143	CD	GLU	B	196	−46.068	−9.008	133.278	1.00	51.19		C
ATOM	3144	OE1	GLU	B	196	−46.538	−7.957	132.796	1.00	55.09		O
ATOM	3145	OE2	GLU	B	196	−46.618	−9.605	134.234	1.00	54.09		O1−
ATOM	3146	N	VAL	B	197	−42.549	−11.236	130.491	1.00	33.59		N
ATOM	3147	CA	VAL	B	197	−42.499	−12.350	129.550	1.00	28.73		C
ATOM	3148	C	VAL	B	197	−43.396	−13.467	130.057	1.00	31.19		C
ATOM	3149	O	VAL	B	197	−43.137	−14.053	131.117	1.00	32.63		O
ATOM	3150	CB	VAL	B	197	−41.057	−12.851	129.355	1.00	29.79		C
ATOM	3151	CG1	VAL	B	197	−41.040	−14.182	128.614	1.00	27.12		C
ATOM	3152	CG2	VAL	B	197	−40.238	−11.808	128.589	1.00	28.85		C
ATOM	3153	N	THR	B	198	−44.436	−13.778	129.293	1.00	32.91		N
ATOM	3154	CA	THR	B	198	−45.297	−14.926	129.549	1.00	29.91		C
ATOM	3155	C	THR	B	198	−45.009	−16.037	128.547	1.00	32.14		C
ATOM	3156	O	THR	B	198	−45.017	−15.808	127.328	1.00	29.74		O
ATOM	3157	CB	THR	B	198	−46.763	−14.516	129.502	1.00	29.14		C
ATOM	3158	OG1	THR	B	198	−46.977	−13.539	130.518	1.00	36.91		O
ATOM	3159	CG2	THR	B	198	−47.664	−15.701	129.771	1.00	31.29		C
ATOM	3160	N	HIS	B	199	−44.758	−17.237	129.066	1.00	29.27		N
ATOM	3161	CA	HIS	B	199	−44.464	−18.393	128.233	1.00	32.48		C
ATOM	3162	C	HIS	B	199	−44.929	−19.638	128.964	1.00	34.28		C
ATOM	3163	O	HIS	B	199	−44.998	−19.645	130.194	1.00	35.68		O
ATOM	3164	CB	HIS	B	199	−42.975	−18.520	127.932	1.00	28.76		C
ATOM	3165	CG	HIS	B	199	−42.659	−19.599	126.950	1.00	31.19		C
ATOM	3166	ND1	HIS	B	199	−42.284	−20.867	127.331	1.00	29.79		N
ATOM	3167	CD2	HIS	B	199	−42.657	−19.594	125.595	1.00	31.07		C
ATOM	3168	CE1	HIS	B	199	−42.066	−21.596	126.252	1.00	29.75		C
ATOM	3169	NE2	HIS	B	199	−42.280	−20.845	125.185	1.00	26.47		N
ATOM	3170	N	GLN	B	200	−45.239	−20.693	128.204	1.00	28.40		N
ATOM	3171	CA	GLN	B	200	−45.833	−21.862	128.839	1.00	28.53		C
ATOM	3172	C	GLN	B	200	−44.841	−22.620	129.706	1.00	34.07		C
ATOM	3173	O	GLN	B	200	−45.270	−23.425	130.535	1.00	36.20		O
ATOM	3174	CB	GLN	B	200	−46.471	−22.791	127.805	1.00	34.90		C
ATOM	3175	CG	GLN	B	200	−45.638	−23.987	127.362	1.00	36.70		C
ATOM	3176	CD	GLN	B	200	−46.492	−25.092	126.712	1.00	43.78		C
ATOM	3177	OE1	GLN	B	200	−46.443	−26.257	127.124	1.00	43.09		O
ATOM	3178	NE2	GLN	B	200	−47.268	−24.723	125.692	1.00	41.04		N
ATOM	3179	N	GLY	B	201	−43.538	−22.378	129.558	1.00	35.51		N
ATOM	3180	CA	GLY	B	201	−42.576	−22.968	130.464	1.00	29.44		C
ATOM	3181	C	GLY	B	201	−42.338	−22.163	131.720	1.00	33.22		C
ATOM	3182	O	GLY	B	201	−41.524	−22.553	132.563	1.00	33.63		O
ATOM	3183	N	LEU	B	202	−43.062	−21.058	131.884	1.00	32.15		N
ATOM	3184	CA	LEU	B	202	−42.986	−20.209	133.061	1.00	36.14		C
ATOM	3185	C	LEU	B	202	−44.298	−20.336	133.808	1.00	37.68		C
ATOM	3186	O	LEU	B	202	−45.352	−20.003	133.256	1.00	37.45		O
ATOM	3187	CB	LEU	B	202	−42.765	−18.743	132.669	1.00	36.59		C
ATOM	3188	CG	LEU	B	202	−41.529	−18.334	131.867	1.00	27.10		C
ATOM	3189	CD1	LEU	B	202	−41.560	−16.866	131.516	1.00	29.06		C
ATOM	3190	CD2	LEU	B	202	−40.313	−18.626	132.669	1.00	31.65		C
ATOM	3191	N	SER	B	203	−44.227	−20.741	135.082	1.00	42.21		N
ATOM	3192	CA	SER	B	203	−45.444	−20.866	135.880	1.00	41.93		C
ATOM	3193	C	SER	B	203	−46.098	−19.513	136.127	1.00	42.43		C
ATOM	3194	O	SER	B	203	−47.312	−19.458	136.334	1.00	41.82		O
ATOM	3195	CB	SER	B	203	−45.145	−21.561	137.214	1.00	44.30		C
ATOM	3196	OG	SER	B	203	−44.114	−20.886	137.919	1.00	57.08		O
ATOM	3197	N	SER	B	204	−45.333	−18.425	136.065	1.00	41.83		N
ATOM	3198	CA	SER	B	204	−45.886	−17.077	136.094	1.00	43.80		C
ATOM	3199	C	SER	B	204	−44.928	−16.136	135.369	1.00	41.32		C
ATOM	3200	O	SER	B	204	−43.777	−16.501	135.094	1.00	39.18		O
ATOM	3201	CB	SER	B	204	−46.175	−16.616	137.537	1.00	37.72		C
ATOM	3202	OG	SER	B	204	−45.011	−16.540	138.333	1.00	37.17		O
ATOM	3203	N	PRO	B	205	−45.400	−14.953	134.971	1.00	34.11		N
ATOM	3204	CA	PRO	B	205	−44.574	−14.046	134.171	1.00	33.10		C
ATOM	3205	C	PRO	B	205	−43.256	−13.665	134.836	1.00	39.09		C
ATOM	3206	O	PRO	B	205	−43.148	−13.550	136.053	1.00	45.40		O
ATOM	3207	CB	PRO	B	205	−45.475	−12.821	133.999	1.00	37.31		C
ATOM	3208	CG	PRO	B	205	−46.835	−13.372	134.001	1.00	39.03		C
ATOM	3209	CD	PRO	B	205	−46.817	−14.553	134.944	1.00	38.32		C
ATOM	3210	N	VAL	B	206	−42.232	−13.502	134.016	1.00	34.71		N
ATOM	3211	CA	VAL	B	206	−40.922	−13.075	134.467	1.00	35.91		C
ATOM	3212	C	VAL	B	206	−40.692	−11.645	133.984	1.00	38.85		C
ATOM	3213	O	VAL	B	206	−40.938	−11.328	132.811	1.00	36.12		O
ATOM	3214	CB	VAL	B	206	−39.836	−14.036	133.951	1.00	34.83		C
ATOM	3215	CG1	VAL	B	206	−38.475	−13.474	134.183	1.00	32.65		C
ATOM	3216	CG2	VAL	B	206	−39.970	−15.355	134.650	1.00	35.57		C
ATOM	3217	N	THR	B	207	−40.236	−10.774	134.883	1.00	38.08		N
ATOM	3218	CA	THR	B	207	−39.870	−9.416	134.504	1.00	40.84		C
ATOM	3219	C	THR	B	207	−38.378	−9.204	134.736	1.00	39.54		C
ATOM	3220	O	THR	B	207	−37.836	−9.618	135.761	1.00	42.64		O
ATOM	3221	CB	THR	B	207	−40.678	−8.361	135.276	1.00	37.84		C
ATOM	3222	OG1	THR	B	207	−42.077	−8.538	135.017	1.00	43.59		O
ATOM	3223	CG2	THR	B	207	−40.291	−6.972	134.837	1.00	32.49		C
ATOM	3224	N	LYS	B	208	−37.715	−8.590	133.762	1.00	38.06		N
ATOM	3225	CA	LYS	B	208	−36.376	−8.048	133.928	1.00	36.13		C
ATOM	3226	C	LYS	B	208	−36.503	−6.553	133.717	1.00	30.77		C
ATOM	3227	O	LYS	B	208	−37.237	−6.108	132.840	1.00	34.40		O
ATOM	3228	CB	LYS	B	208	−35.349	−8.617	132.922	1.00	32.55		C
ATOM	3229	CG	LYS	B	208	−35.155	−10.137	132.891	1.00	33.52		C
ATOM	3230	CD	LYS	B	208	−34.907	−10.808	134.236	1.00	35.71		C
ATOM	3231	CE	LYS	B	208	−34.562	−12.283	133.994	1.00	39.12		C
ATOM	3232	NZ	LYS	B	208	−34.393	−13.134	135.206	1.00	41.39		N1+
ATOM	3233	N	SER	B	209	−35.841	−5.768	134.543	1.00	37.37		N
ATOM	3234	CA	SER	B	209	−36.013	−4.330	134.455	1.00	33.94		C
ATOM	3235	C	SER	B	209	−34.700	−3.653	134.776	1.00	29.43		C
ATOM	3236	O	SER	B	209	−33.780	−4.271	135.305	1.00	31.80		O
ATOM	3237	CB	SER	B	209	−37.096	−3.848	135.420	1.00	33.21		C
ATOM	3238	OG	SER	B	209	−36.754	−4.262	136.724	1.00	35.51		O
ATOM	3239	N	PHE	B	210	−34.653	−2.351	134.517	1.00	34.31		N
ATOM	3240	CA	PHE	B	210	−33.559	−1.507	134.978	1.00	37.85		C
ATOM	3241	C	PHE	B	210	−34.108	−0.121	135.302	1.00	39.37		C
ATOM	3242	O	PHE	B	210	−35.098	0.319	134.705	1.00	33.58		O
ATOM	3243	CB	PHE	B	210	−32.434	−1.395	133.935	1.00	26.33		C
ATOM	3244	CG	PHE	B	210	−32.827	−0.647	132.698	1.00	33.39		C
ATOM	3245	CD1	PHE	B	210	−32.688	0.736	132.632	1.00	31.43		C
ATOM	3246	CD2	PHE	B	210	−33.342	−1.321	131.597	1.00	32.75		C
ATOM	3247	CE1	PHE	B	210	−33.052	1.438	131.490	1.00	35.66		C
ATOM	3248	CE2	PHE	B	210	−33.702	−0.630	130.436	1.00	33.47		C
ATOM	3249	CZ	PHE	B	210	−33.559	0.752	130.380	1.00	34.55		C
ATOM	3250	N	ASN	B	211	−33.475	0.547	136.284	1.00	42.75		N
ATOM	3251	CA	ASN	B	211	−33.738	1.955	136.583	1.00	38.70		C
ATOM	3252	C	ASN	B	211	−32.818	2.832	135.752	1.00	43.04		C
ATOM	3253	O	ASN	B	211	−31.602	2.610	135.717	1.00	39.58		O
ATOM	3254	CB	ASN	B	211	−33.515	2.295	138.054	1.00	48.54		C
ATOM	3255	CG	ASN	B	211	−34.216	1.354	138.988	1.00	51.99		C
ATOM	3256	OD1	ASN	B	211	−35.237	0.765	138.642	1.00	48.81		O
ATOM	3257	ND2	ASN	B	211	−33.672	1.208	140.193	1.00	53.46		N
ATOM	3258	N	ARG	B	212	−33.396	3.826	135.088	1.00	42.30		N
ATOM	3259	CA	ARG	B	212	−32.585	4.725	134.279	1.00	44.00		C
ATOM	3260	C	ARG	B	212	−31.547	5.416	135.166	1.00	53.42		C
ATOM	3261	O	ARG	B	212	−31.838	5.807	136.304	1.00	49.38		O
ATOM	3262	CB	ARG	B	212	−33.478	5.748	133.579	1.00	35.08		C
ATOM	3263	CG	ARG	B	212	−32.768	6.567	132.543	1.00	35.57		C
ATOM	3264	CD	ARG	B	212	−33.745	7.458	131.855	1.00	39.63		C
ATOM	3265	NE	ARG	B	212	−34.383	8.298	132.850	1.00	48.56		N
ATOM	3266	CZ	ARG	B	212	−33.927	9.489	133.210	1.00	47.89		C
ATOM	3267	NH1	ARG	B	212	−32.853	9.988	132.617	1.00	49.63		N1+
ATOM	3268	NH2	ARG	B	212	−34.554	10.182	134.150	1.00	49.80		N
ATOM	3269	N	GLY	B	213	−30.313	5.513	134.660	1.00	57.27		N
ATOM	3270	CA	GLY	B	213	−29.233	6.174	135.372	1.00	56.62		C
ATOM	3271	C	GLY	B	213	−28.594	5.389	136.502	1.00	64.15		C
ATOM	3272	O	GLY	B	213	−27.852	5.979	137.297	1.00	72.50		O
ATOM	3273	N	GLU	B	214	−28.872	4.093	136.624	1.00	62.54		N
ATOM	3274	CA	GLU	B	214	−28.300	3.285	137.703	1.00	62.11		C
ATOM	3275	C	GLU	B	214	−27.713	1.996	137.157	1.00	59.03		C
ATOM	3276	O	GLU	B	214	−26.518	1.940	136.863	1.00	63.86		O
ATOM	3277	CB	GLU	B	214	−29.353	3.001	138.781	1.00	51.33		C
ATOM	3278	CG	GLU	B	214	−29.912	4.302	139.342	1.00	61.22		C
ATOM	3279	CD	GLU	B	214	−31.228	4.170	140.105	1.00	66.11		C
ATOM	3280	OE1	GLU	B	214	−31.496	3.123	140.751	1.00	61.27		O
ATOM	3281	OE2	GLU	B	214	−32.004	5.152	140.044	1.00	64.67		O1−
TER
ATOM	3282	N	GLN	C	1	−37.672	−36.358	87.095	1.00	48.43		N
ATOM	3283	CA	GLN	C	1	−37.796	−35.842	85.733	1.00	53.92		C
ATOM	3284	C	GLN	C	1	−36.907	−36.762	84.921	1.00	48.53		C
ATOM	3285	O	GLN	C	1	−37.375	−37.531	84.085	1.00	49.71		O
ATOM	3286	CB	GLN	C	1	−37.335	−34.383	85.628	1.00	47.24		C
ATOM	3287	CG	GLN	C	1	−37.925	−33.494	86.693	1.00	41.90		C
ATOM	3288	CD	GLN	C	1	−37.270	−33.771	88.072	1.00	54.37		C
ATOM	3289	OE1	GLN	C	1	−37.245	−34.914	88.549	1.00	44.69		O
ATOM	3290	NE2	GLN	C	1	−36.710	−32.731	88.690	1.00	59.79		N
ATOM	3291	N	VAL	C	2	−35.614	−36.686	85.222	1.00	51.69		N
ATOM	3292	CA	VAL	C	2	−34.607	−37.545	84.617	1.00	47.55		C
ATOM	3293	C	VAL	C	2	−34.423	−38.731	85.545	1.00	47.63		C
ATOM	3294	O	VAL	C	2	−33.898	−38.581	86.647	1.00	46.25		O
ATOM	3295	CB	VAL	C	2	−33.299	−36.782	84.412	1.00	42.21		C
ATOM	3296	CG1	VAL	C	2	−32.374	−37.549	83.497	1.00	38.77		C
ATOM	3297	CG2	VAL	C	2	−33.625	−35.409	83.861	1.00	38.63		C
ATOM	3298	N	GLN	C	3	−34.870	−39.908	85.122	1.00	44.76		N
ATOM	3299	CA	GLN	C	3	−34.623	−41.114	85.894	1.00	46.20		C
ATOM	3300	C	GLN	C	3	−33.571	−41.955	85.194	1.00	38.10		C
ATOM	3301	O	GLN	C	3	−33.475	−41.955	83.965	1.00	39.47		O
ATOM	3302	CB	GLN	C	3	−35.902	−41.931	86.152	1.00	46.17		C
ATOM	3303	CG	GLN	C	3	−36.857	−42.057	84.981	1.00	54.72		C
ATOM	3304	CD	GLN	C	3	−37.939	−40.974	84.954	1.00	59.64		C
ATOM	3305	OE1	GLN	C	3	−38.022	−40.180	83.996	1.00	55.09		O
ATOM	3306	NE2	GLN	C	3	−38.794	−40.952	85.996	1.00	49.26		N
ATOM	3307	N	LEU	C	4	−32.728	−42.584	85.993	1.00	36.10		N
ATOM	3308	CA	LEU	C	4	−31.834	−43.639	85.548	1.00	36.24		C
ATOM	3309	C	LEU	C	4	−32.349	−44.892	86.234	1.00	38.70		C
ATOM	3310	O	LEU	C	4	−32.006	−45.155	87.383	1.00	41.03		O
ATOM	3311	CB	LEU	C	4	−30.377	−43.351	85.916	1.00	31.18		C
ATOM	3312	CG	LEU	C	4	−29.695	−42.051	85.479	1.00	32.11		C
ATOM	3313	CD1	LEU	C	4	−28.199	−42.201	85.552	1.00	34.48		C
ATOM	3314	CD2	LEU	C	4	−30.085	−41.672	84.084	1.00	36.90		C
ATOM	3315	N	GLN	C	5	−33.149	−45.677	85.525	1.00	44.15		N
ATOM	3316	CA	GLN	C	5	−33.773	−46.856	86.108	1.00	45.12		C
ATOM	3317	C	GLN	C	5	−32.880	−48.063	85.887	1.00	41.78		C
ATOM	3318	O	GLN	C	5	−32.475	−48.340	84.755	1.00	41.54		O
ATOM	3319	CB	GLN	C	5	−35.152	−47.084	85.489	1.00	49.54		C
ATOM	3320	CG	GLN	C	5	−35.943	−48.256	86.071	1.00	56.47		C
ATOM	3321	CD	GLN	C	5	−37.440	−48.116	85.797	1.00	74.65		C
ATOM	3322	OE1	GLN	C	5	−37.935	−47.009	85.533	1.00	74.08		O
ATOM	3323	NE2	GLN	C	5	−38.166	−49.236	85.850	1.00	70.76		N
ATOM	3324	N	GLN	C	6	−32.592	−48.786	86.963	1.00	36.00		N
ATOM	3325	CA	GLN	C	6	−31.668	−49.905	86.917	1.00	37.25		C
ATOM	3326	C	GLN	C	6	−32.432	−51.207	87.049	1.00	40.30		C
ATOM	3327	O	GLN	C	6	−33.416	−51.281	87.787	1.00	48.42		O
ATOM	3328	CB	GLN	C	6	−30.617	−49.841	88.032	1.00	37.59		C
ATOM	3329	CG	GLN	C	6	−29.875	−48.541	88.142	1.00	40.04		C
ATOM	3330	CD	GLN	C	6	−28.646	−48.621	89.041	1.00	38.65		C
ATOM	3331	OE1	GLN	C	6	−28.173	−47.599	89.535	1.00	36.68		O
ATOM	3332	NE2	GLN	C	6	−28.111	−49.834	89.239	1.00	31.43		N
ATOM	3333	N	TRP	C	7	−31.969	−52.228	86.334	1.00	36.46		N
ATOM	3334	CA	TRP	C	7	−32.424	−53.585	86.573	1.00	39.72		C
ATOM	3335	C	TRP	C	7	−31.284	−54.527	86.258	1.00	37.13		C
ATOM	3336	O	TRP	C	7	−30.252	−54.125	85.709	1.00	36.52		O
ATOM	3337	CB	TRP	C	7	−33.669	−53.937	85.756	1.00	36.24		C
ATOM	3338	CG	TRP	C	7	−33.515	−53.880	84.294	1.00	38.80		C
ATOM	3339	CD1	TRP	C	7	−33.103	−54.893	83.464	1.00	37.72		C
ATOM	3340	CD2	TRP	C	7	−33.812	−52.760	83.446	1.00	41.40		C
ATOM	3341	NE1	TRP	C	7	−33.111	−54.462	82.153	1.00	39.38		N
ATOM	3342	CE2	TRP	C	7	−33.544	−53.159	82.113	1.00	39.28		C
ATOM	3343	CE3	TRP	C	7	−34.270	−51.460	83.683	1.00	41.24		C
ATOM	3344	CZ2	TRP	C	7	−33.713	−52.298	81.022	1.00	37.17		C
ATOM	3345	CZ3	TRP	C	7	−34.443	−50.603	82.589	1.00	42.48		C
ATOM	3346	CH2	TRP	C	7	−34.164	−51.032	81.278	1.00	38.07		C
ATOM	3347	N	GLY	C	8	−31.479	−55.779	86.640	1.00	30.53		N
ATOM	3348	CA	GLY	C	8	−30.480	−56.819	86.491	1.00	29.00		C
ATOM	3349	C	GLY	C	8	−30.542	−57.704	87.715	1.00	28.80		C
ATOM	3350	O	GLY	C	8	−30.936	−57.284	88.802	1.00	35.52		O
ATOM	3351	N	ALA	C	9	−30.175	−58.964	87.536	1.00	31.95		N
ATOM	3352	CA	ALA	C	9	−30.163	−59.902	88.650	1.00	36.64		C
ATOM	3353	C	ALA	C	9	−29.108	−59.490	89.672	1.00	40.72		C
ATOM	3354	O	ALA	C	9	−27.936	−59.312	89.329	1.00	44.07		O
ATOM	3355	CB	ALA	C	9	−29.893	−61.324	88.152	1.00	32.88		C
ATOM	3356	N	GLY	C	10	−29.528	−59.350	90.927	1.00	40.53		N
ATOM	3357	CA	GLY	C	10	−28.651	−58.938	92.001	1.00	34.92		C
ATOM	3358	C	GLY	C	10	−28.135	−60.045	92.894	1.00	32.59		C
ATOM	3359	O	GLY	C	10	−27.259	−59.787	93.722	1.00	37.26		O
ATOM	3360	N	LEU	C	11	−28.643	−61.269	92.760	1.00	33.32		N
ATOM	3361	CA	LEU	C	11	−28.155	−62.401	93.550	1.00	35.63		C
ATOM	3362	C	LEU	C	11	−27.388	−63.330	92.625	1.00	37.18		C
ATOM	3363	O	LEU	C	11	−27.945	−63.832	91.641	1.00	40.37		O
ATOM	3364	CB	LEU	C	11	−29.292	−63.162	94.238	1.00	33.21		C
ATOM	3365	CG	LEU	C	11	−29.045	−63.745	95.639	1.00	35.68		C
ATOM	3366	CD1	LEU	C	11	−29.828	−65.026	95.836	1.00	37.14		C
ATOM	3367	CD2	LEU	C	11	−27.589	−63.991	95.974	1.00	34.37		C
ATOM	3368	N	LEU	C	12	−26.125	−63.573	92.957	1.00	33.96		N
ATOM	3369	CA	LEU	C	12	−25.238	−64.365	92.126	1.00	37.97		C
ATOM	3370	C	LEU	C	12	−24.363	−65.240	93.002	1.00	35.65		C
ATOM	3371	O	LEU	C	12	−24.068	−64.894	94.147	1.00	36.30		O
ATOM	3372	CB	LEU	C	12	−24.331	−63.494	91.246	1.00	34.37		C
ATOM	3373	CG	LEU	C	12	−24.960	−62.530	90.262	1.00	37.66		C
ATOM	3374	CD1	LEU	C	12	−23.856	−61.733	89.638	1.00	43.23		C
ATOM	3375	CD2	LEU	C	12	−25.713	−63.294	89.190	1.00	44.30		C
ATOM	3376	N	LYS	C	13	−23.932	−66.390	92.428	1.00	36.66		N
ATOM	3377	CA	LYS	C	13	−22.957	−67.321	92.963	1.00	38.43		C
ATOM	3378	C	LYS	C	13	−21.606	−67.082	92.306	1.00	39.27		C
ATOM	3379	O	LYS	C	13	−21.543	−66.620	91.160	1.00	39.31		O
ATOM	3380	CB	LYS	C	13	−23.391	−68.766	92.715	1.00	36.21		C
ATOM	3381	CG	LYS	C	13	−24.872	−68.896	92.517	1.00	42.22		C
ATOM	3382	CD	LYS	C	13	−25.398	−70.074	93.270	1.00	45.83		C
ATOM	3383	CE	LYS	C	13	−25.107	−69.921	94.743	1.00	45.08		C
ATOM	3384	NZ	LYS	C	13	−25.676	−71.073	95.499	1.00	49.42		N1+
ATOM	3385	N	PRO	C	14	−20.517	−67.383	93.016	1.00	33.06		N
ATOM	3386	CA	PRO	C	14	−19.180	−67.135	92.464	1.00	31.17		C
ATOM	3387	C	PRO	C	14	−19.019	−67.705	91.063	1.00	35.18		C
ATOM	3388	O	PRO	C	14	−19.621	−68.717	90.712	1.00	37.79		O
ATOM	3389	CB	PRO	C	14	−18.258	−67.830	93.463	1.00	24.90		C
ATOM	3390	CG	PRO	C	14	−19.016	−67.795	94.737	1.00	29.59		C
ATOM	3391	CD	PRO	C	14	−20.461	−67.876	94.405	1.00	27.79		C
ATOM	3392	N	SER	C	15	−18.235	−66.995	90.251	1.00	38.99		N
ATOM	3393	CA	SER	C	15	−17.811	−67.278	88.882	1.00	33.18		C
ATOM	3394	C	SER	C	15	−18.911	−66.976	87.855	1.00	35.06		C
ATOM	3395	O	SER	C	15	−18.601	−66.892	86.661	1.00	34.68		O
ATOM	3396	CB	SER	C	15	−17.276	−68.717	88.689	1.00	35.00		C
ATOM	3397	OG	SER	C	15	−18.279	−69.665	88.363	1.00	36.60		O
ATOM	3398	N	GLU	C	16	−20.172	−66.781	88.266	1.00	33.98		N
ATOM	3399	CA	GLU	C	16	−21.187	−66.305	87.322	1.00	35.39		C
ATOM	3400	C	GLU	C	16	−20.811	−64.890	86.852	1.00	35.84		C
ATOM	3401	O	GLU	C	16	−19.841	−64.279	87.324	1.00	35.76		O
ATOM	3402	CB	GLU	C	16	−22.590	−66.308	87.953	1.00	33.60		C
ATOM	3403	CG	GLU	C	16	−22.982	−67.595	88.701	1.00	38.40		C
ATOM	3404	CD	GLU	C	16	−24.487	−67.720	89.061	1.00	49.48		C
ATOM	3405	OE1	GLU	C	16	−25.199	−66.698	89.225	1.00	50.75		O
ATOM	3406	OE2	GLU	C	16	−24.950	−68.866	89.261	1.00	51.03		O1−
ATOM	3407	N	THR	C	17	−21.570	−64.359	85.905	1.00	32.01		N
ATOM	3408	CA	THR	C	17	−21.301	−63.010	85.451	1.00	32.01		C
ATOM	3409	C	THR	C	17	−22.463	−62.094	85.818	1.00	39.55		C
ATOM	3410	O	THR	C	17	−23.637	−62.460	85.685	1.00	36.43		O
ATOM	3411	CB	THR	C	17	−20.978	−62.950	83.939	1.00	34.07		C
ATOM	3412	OG1	THR	C	17	−21.956	−62.180	83.230	1.00	39.64		O
ATOM	3413	CG2	THR	C	17	−20.841	−64.327	83.325	1.00	35.94		C
ATOM	3414	N	LEU	C	18	−22.109	−60.901	86.295	1.00	37.34		N
ATOM	3415	CA	LEU	C	18	−23.065	−59.889	86.703	1.00	30.52		C
ATOM	3416	C	LEU	C	18	−23.481	−59.095	85.476	1.00	34.01		C
ATOM	3417	O	LEU	C	18	−22.639	−58.717	84.651	1.00	35.55		O
ATOM	3418	CB	LEU	C	18	−22.437	−59.006	87.782	1.00	29.47		C
ATOM	3419	CG	LEU	C	18	−22.993	−57.708	88.384	1.00	35.82		C
ATOM	3420	CD1	LEU	C	18	−22.732	−56.524	87.491	1.00	32.88		C
ATOM	3421	CD2	LEU	C	18	−24.488	−57.846	88.679	1.00	31.62		C
ATOM	3422	N	SER	C	19	−24.783	−58.870	85.340	1.00	31.00		N
ATOM	3423	CA	SER	C	19	−25.301	−58.146	84.187	1.00	36.91		C
ATOM	3424	C	SER	C	19	−26.378	−57.173	84.657	1.00	32.12		C
ATOM	3425	O	SER	C	19	−27.371	−57.593	85.262	1.00	30.22		O
ATOM	3426	CB	SER	C	19	−25.835	−59.143	83.141	1.00	33.82		C
ATOM	3427	OG	SER	C	19	−26.265	−58.506	81.963	1.00	42.48		O
ATOM	3428	N	LEU	C	20	−26.175	−55.877	84.364	1.00	30.42		N
ATOM	3429	CA	LEU	C	20	−27.041	−54.785	84.804	1.00	30.56		C
ATOM	3430	C	LEU	C	20	−27.300	−53.840	83.643	1.00	29.54		C
ATOM	3431	O	LEU	C	20	−26.430	−53.618	82.801	1.00	31.80		O
ATOM	3432	CB	LEU	C	20	−26.416	−53.973	85.970	1.00	25.88		C
ATOM	3433	CG	LEU	C	20	−26.042	−54.745	87.243	1.00	27.95		C
ATOM	3434	CD1	LEU	C	20	−25.312	−53.866	88.232	1.00	25.17		C
ATOM	3435	CD2	LEU	C	20	−27.288	−55.391	87.897	1.00	28.86		C
ATOM	3436	N	THR	C	21	−28.479	−53.236	83.636	1.00	29.19		N
ATOM	3437	CA	THR	C	21	−28.844	−52.262	82.616	1.00	32.34		C
ATOM	3438	C	THR	C	21	−29.444	−51.043	83.297	1.00	33.93		C
ATOM	3439	O	THR	C	21	−30.059	−51.155	84.360	1.00	41.09		O
ATOM	3440	CB	THR	C	21	−29.833	−52.839	81.576	1.00	32.67		C
ATOM	3441	OG1	THR	C	21	−29.282	−54.034	81.016	1.00	29.98		O
ATOM	3442	CG2	THR	C	21	−30.116	−51.832	80.457	1.00	28.76		C
ATOM	3443	N	CYS	C	22	−29.221	−49.880	82.686	1.00	28.26		N
ATOM	3444	CA	CYS	C	22	−29.766	−48.596	83.090	1.00	26.22		C
ATOM	3445	C	CYS	C	22	−30.582	−48.024	81.939	1.00	35.11		C
ATOM	3446	O	CYS	C	22	−30.119	−48.022	80.794	1.00	35.88		O
ATOM	3447	CB	CYS	C	22	−28.601	−47.671	83.441	1.00	34.45		C
ATOM	3448	SG	CYS	C	22	−28.863	−46.199	84.443	1.00	53.91		S
ATOM	3449	N	ALA	C	23	−31.786	−47.526	82.223	1.00	41.07		N
ATOM	3450	CA	ALA	C	23	−32.593	−46.849	81.211	1.00	32.31		C
ATOM	3451	C	ALA	C	23	−32.715	−45.377	81.565	1.00	38.18		C
ATOM	3452	O	ALA	C	23	−33.077	−45.034	82.693	1.00	40.40		O
ATOM	3453	CB	ALA	C	23	−33.971	−47.489	81.072	1.00	31.29		C
ATOM	3454	N	VAL	C	24	−32.419	−44.515	80.601	1.00	37.14		N
ATOM	3455	CA	VAL	C	24	−32.433	−43.067	80.777	1.00	34.17		C
ATOM	3456	C	VAL	C	24	−33.726	−42.531	80.183	1.00	39.79		C
ATOM	3457	O	VAL	C	24	−34.063	−42.841	79.033	1.00	44.85		O
ATOM	3458	CB	VAL	C	24	−31.202	−42.429	80.111	1.00	35.68		C
ATOM	3459	CG1	VAL	C	24	−31.194	−40.927	80.274	1.00	33.16		C
ATOM	3460	CG2	VAL	C	24	−29.937	−43.034	80.689	1.00	35.47		C
ATOM	3461	N	SER	C	25	−34.433	−41.694	80.936	1.00	40.19		N
ATOM	3462	CA	SER	C	25	−35.722	−41.217	80.453	1.00	37.50		C
ATOM	3463	C	SER	C	25	−35.843	−39.707	80.355	1.00	46.83		C
ATOM	3464	O	SER	C	25	−36.323	−39.206	79.339	1.00	56.63		O
ATOM	3465	CB	SER	C	25	−36.842	−41.735	81.372	1.00	39.57		C
ATOM	3466	OG	SER	C	25	−36.448	−42.914	82.077	1.00	44.46		O
ATOM	3467	N	GLY	C	26	−35.362	−38.958	81.342	1.00	46.38		N
ATOM	3468	CA	GLY	C	26	−35.703	−37.542	81.413	1.00	45.90		C
ATOM	3469	C	GLY	C	26	−35.175	−36.666	80.290	1.00	45.91		C
ATOM	3470	O	GLY	C	26	−35.926	−35.873	79.720	1.00	50.30		O
ATOM	3471	N	GLY	C	27	−33.881	−36.752	79.983	1.00	41.90		N
ATOM	3472	CA	GLY	C	27	−33.299	−35.764	79.082	1.00	33.59		C
ATOM	3473	C	GLY	C	27	−32.626	−36.313	77.847	1.00	35.39		C
ATOM	3474	O	GLY	C	27	−33.065	−37.324	77.298	1.00	41.91		O
ATOM	3475	N	SER	C	28	−31.574	−35.646	77.382	1.00	41.18		N
ATOM	3476	CA	SER	C	28	−30.856	−36.113	76.204	1.00	38.29		C
ATOM	3477	C	SER	C	28	−29.975	−37.312	76.538	1.00	36.07		C
ATOM	3478	O	SER	C	28	−29.631	−37.575	77.693	1.00	37.41		O
ATOM	3479	CB	SER	C	28	−29.983	−35.007	75.609	1.00	38.36		C
ATOM	3480	OG	SER	C	28	−30.761	−33.920	75.126	1.00	40.67		O
ATOM	3481	N	PHE	C	29	−29.605	−38.042	75.494	1.00	36.30		N
ATOM	3482	CA	PHE	C	29	−28.717	−39.178	75.630	1.00	36.41		C
ATOM	3483	C	PHE	C	29	−27.350	−38.932	75.015	1.00	41.79		C
ATOM	3484	O	PHE	C	29	−26.408	−39.669	75.329	1.00	42.57		O
ATOM	3485	CB	PHE	C	29	−29.357	−40.414	74.999	1.00	29.89		C
ATOM	3486	CG	PHE	C	29	−28.843	−41.712	75.541	1.00	31.96		C
ATOM	3487	CD1	PHE	C	29	−28.786	−41.939	76.912	1.00	37.24		C
ATOM	3488	CD2	PHE	C	29	−28.466	−42.735	74.682	1.00	32.71		C
ATOM	3489	CE1	PHE	C	29	−28.325	−43.161	77.428	1.00	31.78		C
ATOM	3490	CE2	PHE	C	29	−28.010	−43.953	75.182	1.00	32.65		C
ATOM	3491	CZ	PHE	C	29	−27.946	−44.167	76.558	1.00	31.78		C
ATOM	3492	N	ARG	C	30	−27.207	−37.893	74.190	1.00	36.62		N
ATOM	3493	CA	ARG	C	30	−26.097	−37.790	73.261	1.00	40.24		C
ATOM	3494	C	ARG	C	30	−24.969	−36.896	73.757	1.00	41.65		C
ATOM	3495	O	ARG	C	30	−23.861	−36.972	73.223	1.00	37.36		O
ATOM	3496	CB	ARG	C	30	−26.601	−37.249	71.922	1.00	37.58		C
ATOM	3497	CG	ARG	C	30	−27.046	−35.805	72.068	1.00	51.10		C
ATOM	3498	CD	ARG	C	30	−27.335	−35.130	70.748	1.00	52.17		C
ATOM	3499	NE	ARG	C	30	−28.733	−35.284	70.381	1.00	58.44		N
ATOM	3500	CZ	ARG	C	30	−29.297	−34.695	69.334	1.00	65.83		C
ATOM	3501	NH1	ARG	C	30	−30.583	−34.897	69.073	1.00	66.12		N1+
ATOM	3502	NH2	ARG	C	30	−28.575	−33.907	68.548	1.00	74.46		N
ATOM	3503	N	TYR	C	31	−25.210	−36.062	74.758	1.00	44.38		N
ATOM	3504	CA	TYR	C	31	−24.179	−35.148	75.227	1.00	38.68		C
ATOM	3505	C	TYR	C	31	−23.376	−35.702	76.382	1.00	38.31		C
ATOM	3506	O	TYR	C	31	−22.476	−35.022	76.876	1.00	37.88		O
ATOM	3507	CB	TYR	C	31	−24.791	−33.816	75.660	1.00	39.97		C
ATOM	3508	CG	TYR	C	31	−25.693	−33.157	74.646	1.00	38.66		C
ATOM	3509	CD1	TYR	C	31	−25.199	−32.718	73.428	1.00	39.15		C
ATOM	3510	CD2	TYR	C	31	−27.032	−32.967	74.913	1.00	40.52		C
ATOM	3511	CE1	TYR	C	31	−26.008	−32.113	72.518	1.00	41.25		C
ATOM	3512	CE2	TYR	C	31	−27.852	−32.352	74.011	1.00	45.11		C
ATOM	3513	CZ	TYR	C	31	−27.342	−31.928	72.814	1.00	48.11		C
ATOM	3514	OH	TYR	C	31	−28.178	−31.317	71.914	1.00	50.76		O
ATOM	3515	N	TYR	C	32	−23.699	−36.894	76.851	1.00	41.37		N
ATOM	3516	CA	TYR	C	32	−23.187	−37.357	78.121	1.00	33.57		C
ATOM	3517	C	TYR	C	32	−22.357	−38.615	77.953	1.00	35.33		C
ATOM	3518	O	TYR	C	32	−22.466	−39.346	76.967	1.00	39.05		O
ATOM	3519	CB	TYR	C	32	−24.325	−37.630	79.090	1.00	34.60		C
ATOM	3520	CG	TYR	C	32	−25.238	−36.454	79.258	1.00	38.37		C
ATOM	3521	CD1	TYR	C	32	−24.873	−35.386	80.057	1.00	38.78		C
ATOM	3522	CD2	TYR	C	32	−26.472	−36.408	78.610	1.00	37.80		C
ATOM	3523	CE1	TYR	C	32	−25.711	−34.288	80.207	1.00	42.05		C
ATOM	3524	CE2	TYR	C	32	−27.310	−35.329	78.749	1.00	41.43		C
ATOM	3525	CZ	TYR	C	32	−26.927	−34.266	79.551	1.00	45.45		C
ATOM	3526	OH	TYR	C	32	−27.758	−33.180	79.704	1.00	53.26		O
ATOM	3527	N	TYR	C	33	−21.511	−38.840	78.942	1.00	36.12		N
ATOM	3528	CA	TYR	C	33	−20.902	−40.133	79.185	1.00	33.30		C
ATOM	3529	C	TYR	C	33	−21.731	−40.841	80.236	1.00	29.90		C
ATOM	3530	O	TYR	C	33	−22.282	−40.201	81.135	1.00	34.09		O
ATOM	3531	CB	TYR	C	33	−19.453	−39.988	79.655	1.00	32.91		C
ATOM	3532	CG	TYR	C	33	−18.490	−39.876	78.500	1.00	32.64		C
ATOM	3533	CD1	TYR	C	33	−18.235	−38.637	77.891	1.00	29.43		C
ATOM	3534	CD2	TYR	C	33	−17.843	−41.004	78.005	1.00	32.78		C
ATOM	3535	CE1	TYR	C	33	−17.352	−38.526	76.834	1.00	31.81		C
ATOM	3536	CE2	TYR	C	33	−16.947	−40.905	76.954	1.00	37.66		C
ATOM	3537	CZ	TYR	C	33	−16.714	−39.671	76.363	1.00	36.45		C
ATOM	3538	OH	TYR	C	33	−15.840	−39.599	75.307	1.00	33.16		O
ATOM	3539	N	TRP	C	34	−21.845	−42.154	80.099	1.00	31.46		N
ATOM	3540	CA	TRP	C	34	−22.687	−42.974	80.957	1.00	28.61		C
ATOM	3541	C	TRP	C	34	−21.790	−43.981	81.658	1.00	31.34		C
ATOM	3542	O	TRP	C	34	−20.997	−44.666	80.994	1.00	26.44		O
ATOM	3543	CB	TRP	C	34	−23.790	−43.628	80.118	1.00	25.06		C
ATOM	3544	CG	TRP	C	34	−24.610	−42.557	79.485	1.00	31.01		C
ATOM	3545	CD1	TRP	C	34	−24.506	−42.091	78.205	1.00	32.39		C
ATOM	3546	CD2	TRP	C	34	−25.632	−41.770	80.113	1.00	33.17		C
ATOM	3547	NE1	TRP	C	34	−25.403	−41.072	77.993	1.00	33.65		N
ATOM	3548	CE2	TRP	C	34	−26.108	−40.853	79.145	1.00	34.22		C
ATOM	3549	CE3	TRP	C	34	−26.205	−41.761	81.389	1.00	28.29		C
ATOM	3550	CZ2	TRP	C	34	−27.131	−39.940	79.416	1.00	33.64		C
ATOM	3551	CZ3	TRP	C	34	−27.211	−40.834	81.659	1.00	30.29		C
ATOM	3552	CH2	TRP	C	34	−27.660	−39.944	80.682	1.00	29.13		C
ATOM	3553	N	SER	C	35	−21.903	−44.049	82.998	1.00	28.84		N
ATOM	3554	CA	SER	C	35	−20.898	−44.663	83.856	1.00	26.34		C
ATOM	3555	C	SER	C	35	−21.495	−45.683	84.815	1.00	25.62		C
ATOM	3556	O	SER	C	35	−22.691	−45.688	85.096	1.00	28.59		O
ATOM	3557	CB	SER	C	35	−20.153	−43.603	84.674	1.00	25.36		C
ATOM	3558	OG	SER	C	35	−19.476	−42.699	83.828	1.00	36.45		O
ATOM	3559	N	TRP	C	36	−20.611	−46.515	85.359	1.00	24.98		N
ATOM	3560	CA	TRP	C	36	−20.914	−47.468	86.419	1.00	22.69		C
ATOM	3561	C	TRP	C	36	−19.937	−47.262	87.567	1.00	26.01		C
ATOM	3562	O	TRP	C	36	−18.723	−47.189	87.354	1.00	30.88		O
ATOM	3563	CB	TRP	C	36	−20.829	−48.911	85.911	1.00	27.21		C
ATOM	3564	CG	TRP	C	36	−21.922	−49.263	84.951	1.00	31.29		C
ATOM	3565	CD1	TRP	C	36	−21.856	−49.288	83.581	1.00	27.11		C
ATOM	3566	CD2	TRP	C	36	−23.263	−49.599	85.293	1.00	28.25		C
ATOM	3567	NE1	TRP	C	36	−23.082	−49.636	83.050	1.00	25.91		N
ATOM	3568	CE2	TRP	C	36	−23.959	−49.843	84.083	1.00	31.98		C
ATOM	3569	CE3	TRP	C	36	−23.942	−49.732	86.504	1.00	23.12		C
ATOM	3570	CZ2	TRP	C	36	−25.310	−50.203	84.059	1.00	30.86		C
ATOM	3571	CZ3	TRP	C	36	−25.280	−50.087	86.479	1.00	26.83		C
ATOM	3572	CH2	TRP	C	36	−25.954	−50.315	85.266	1.00	26.13		C
ATOM	3573	N	ILE	C	37	−20.469	−47.181	88.779	1.00	27.24		N
ATOM	3574	CA	ILE	C	37	−19.713	−46.954	90.007	1.00	25.13		C
ATOM	3575	C	ILE	C	37	−20.228	−47.955	91.036	1.00	26.55		C
ATOM	3576	O	ILE	C	37	−21.442	−48.138	91.155	1.00	29.45		O
ATOM	3577	CB	ILE	C	37	−19.904	−45.502	90.503	1.00	24.76		C
ATOM	3578	CG1	ILE	C	37	−19.417	−44.509	89.444	1.00	26.03		C
ATOM	3579	CG2	ILE	C	37	−19.245	−45.259	91.853	1.00	28.36		C
ATOM	3580	CD1	ILE	C	37	−20.031	−43.142	89.552	1.00	27.83		C
ATOM	3581	N	ARG	C	38	−19.328	−48.630	91.755	1.00	21.22		N
ATOM	3582	CA	ARG	C	38	−19.764	−49.538	92.810	1.00	25.95		C
ATOM	3583	C	ARG	C	38	−19.274	−49.069	94.183	1.00	31.35		C
ATOM	3584	O	ARG	C	38	−18.283	−48.340	94.308	1.00	26.88		O
ATOM	3585	CB	ARG	C	38	−19.314	−50.993	92.559	1.00	23.96		C
ATOM	3586	CG	ARG	C	38	−17.834	−51.151	92.450	1.00	33.62		C
ATOM	3587	CD	ARG	C	38	−17.312	−52.176	93.382	1.00	31.96		C
ATOM	3588	NE	ARG	C	38	−17.339	−53.503	92.796	1.00	36.58		N
ATOM	3589	CZ	ARG	C	38	−16.278	−54.294	92.657	1.00	33.65		C
ATOM	3590	NH1	ARG	C	38	−15.072	−53.910	93.057	1.00	31.68		N1+
ATOM	3591	NH2	ARG	C	38	−16.436	−55.483	92.123	1.00	28.23		N
ATOM	3592	N	GLN	C	39	−20.015	−49.467	95.215	1.00	27.22		N
ATOM	3593	CA	GLN	C	39	−19.688	−49.135	96.599	1.00	29.87		C
ATOM	3594	C	GLN	C	39	−19.795	−50.406	97.437	1.00	28.44		C
ATOM	3595	O	GLN	C	39	−20.911	−50.833	97.779	1.00	29.08		O
ATOM	3596	CB	GLN	C	39	−20.621	−48.042	97.105	1.00	24.56		C
ATOM	3597	CG	GLN	C	39	−20.252	−47.429	98.435	1.00	28.85		C
ATOM	3598	CD	GLN	C	39	−21.101	−46.198	98.718	1.00	36.48		C
ATOM	3599	OE1	GLN	C	39	−22.318	−46.187	98.497	1.00	42.72		O
ATOM	3600	NE2	GLN	C	39	−20.459	−45.144	99.169	1.00	38.36		N
ATOM	3601	N	PRO	C	40	−18.674	−51.040	97.791	1.00	30.67		N
ATOM	3602	CA	PRO	C	40	−18.757	−52.243	98.625	1.00	27.55		C
ATOM	3603	C	PRO	C	40	−19.218	−51.877	100.021	1.00	33.77		C
ATOM	3604	O	PRO	C	40	−18.964	−50.757	100.496	1.00	34.43		O
ATOM	3605	CB	PRO	C	40	−17.315	−52.776	98.621	1.00	27.60		C
ATOM	3606	CG	PRO	C	40	−16.645	−52.058	97.420	1.00	26.34		C
ATOM	3607	CD	PRO	C	40	−17.294	−50.736	97.371	1.00	28.79		C
ATOM	3608	N	PRO	C	41	−19.933	−52.772	100.711	1.00	38.11		N
ATOM	3609	CA	PRO	C	41	−20.568	−52.374	101.976	1.00	33.02		C
ATOM	3610	C	PRO	C	41	−19.528	−51.959	103.001	1.00	40.48		C
ATOM	3611	O	PRO	C	41	−18.509	−52.636	103.187	1.00	40.42		O
ATOM	3612	CB	PRO	C	41	−21.327	−53.631	102.408	1.00	37.98		C
ATOM	3613	CG	PRO	C	41	−20.611	−54.752	101.751	1.00	37.85		C
ATOM	3614	CD	PRO	C	41	−20.123	−54.207	100.431	1.00	37.87		C
ATOM	3615	N	GLY	C	42	−19.761	−50.786	103.604	1.00	40.56		N
ATOM	3616	CA	GLY	C	42	−18.805	−50.159	104.482	1.00	38.30		C
ATOM	3617	C	GLY	C	42	−17.794	−49.262	103.801	1.00	45.76		C
ATOM	3618	O	GLY	C	42	−17.212	−48.400	104.462	1.00	47.20		O
ATOM	3619	N	LYS	C	43	−17.557	−49.445	102.505	1.00	44.96		N
ATOM	3620	CA	LYS	C	43	−16.391	−48.889	101.836	1.00	42.23		C
ATOM	3621	C	LYS	C	43	−16.754	−47.617	101.060	1.00	40.08		C
ATOM	3622	O	LYS	C	43	−17.835	−47.040	101.222	1.00	39.81		O
ATOM	3623	CB	LYS	C	43	−15.764	−49.967	100.939	1.00	39.38		C
ATOM	3624	CG	LYS	C	43	−15.348	−51.222	101.710	1.00	43.20		C
ATOM	3625	CD	LYS	C	43	−14.763	−50.832	103.075	1.00	44.43		C
ATOM	3626	CE	LYS	C	43	−14.563	−52.031	103.993	1.00	51.32		C
ATOM	3627	NZ	LYS	C	43	−13.263	−52.735	103.784	1.00	55.64		N1+
ATOM	3628	N	GLY	C	44	−15.827	−47.168	100.217	1.00	38.92		N
ATOM	3629	CA	GLY	C	44	−16.003	−45.991	99.404	1.00	38.32		C
ATOM	3630	C	GLY	C	44	−16.454	−46.330	98.000	1.00	39.62		C
ATOM	3631	O	GLY	C	44	−17.012	−47.402	97.737	1.00	42.04		O
ATOM	3632	N	LEU	C	45	−16.159	−45.425	97.075	1.00	32.83		N
ATOM	3633	CA	LEU	C	45	−16.642	−45.491	95.709	1.00	27.76		C
ATOM	3634	C	LEU	C	45	−15.528	−45.909	94.759	1.00	30.80		C
ATOM	3635	O	LEU	C	45	−14.385	−45.473	94.905	1.00	37.23		O
ATOM	3636	CB	LEU	C	45	−17.213	−44.134	95.309	1.00	28.31		C
ATOM	3637	CG	LEU	C	45	−18.413	−43.760	96.186	1.00	29.60		C
ATOM	3638	CD1	LEU	C	45	−18.761	−42.284	96.033	1.00	25.47		C
ATOM	3639	CD2	LEU	C	45	−19.619	−44.621	95.903	1.00	26.22		C
ATOM	3640	N	GLU	C	46	−15.834	−46.819	93.839	1.00	25.91		N
ATOM	3641	CA	GLU	C	46	−14.895	−47.185	92.791	1.00	30.55		C
ATOM	3642	C	GLU	C	46	−15.566	−47.029	91.433	1.00	35.38		C
ATOM	3643	O	GLU	C	46	−16.677	−47.523	91.215	1.00	35.98		O
ATOM	3644	CB	GLU	C	46	−14.340	−48.609	92.936	1.00	34.86		C
ATOM	3645	CG	GLU	C	46	−14.868	−49.426	94.118	1.00	42.88		C
ATOM	3646	CD	GLU	C	46	−14.142	−50.792	94.274	1.00	55.29		C
ATOM	3647	OE1	GLU	C	46	−13.692	−51.365	93.231	1.00	52.24		O
ATOM	3648	OE2	GLU	C	46	−14.010	−51.261	95.444	1.00	42.79		O1−
ATOM	3649	N	TRP	C	47	−14.880	−46.345	90.524	1.00	35.22		N
ATOM	3650	CA	TRP	C	47	−15.389	−46.093	89.189	1.00	31.80		C
ATOM	3651	C	TRP	C	47	−15.070	−47.293	88.313	1.00	32.40		C
ATOM	3652	O	TRP	C	47	−13.919	−47.720	88.238	1.00	34.10		O
ATOM	3653	CB	TRP	C	47	−14.750	−44.817	88.647	1.00	27.85		C
ATOM	3654	CG	TRP	C	47	−15.028	−44.369	87.213	1.00	29.38		C
ATOM	3655	CD1	TRP	C	47	−16.066	−43.591	86.769	1.00	28.35		C
ATOM	3656	CD2	TRP	C	47	−14.194	−44.605	86.072	1.00	31.89		C
ATOM	3657	NE1	TRP	C	47	−15.932	−43.340	85.418	1.00	29.56		N
ATOM	3658	CE2	TRP	C	47	−14.792	−43.954	84.970	1.00	29.80		C
ATOM	3659	CE3	TRP	C	47	−12.996	−45.312	85.873	1.00	29.70		C
ATOM	3660	CZ2	TRP	C	47	−14.234	−43.990	83.699	1.00	30.22		C
ATOM	3661	CZ3	TRP	C	47	−12.455	−45.356	84.615	1.00	26.84		C
ATOM	3662	CH2	TRP	C	47	−13.068	−44.696	83.541	1.00	31.06		C
ATOM	3663	N	PHE	C	48	−16.096	−47.849	87.666	1.00	29.92		N
ATOM	3664	CA	PHE	C	48	−15.868	−48.990	86.792	1.00	29.20		C
ATOM	3665	C	PHE	C	48	−15.444	−48.547	85.397	1.00	29.36		C
ATOM	3666	O	PHE	C	48	−14.536	−49.142	84.808	1.00	30.45		O
ATOM	3667	CB	PHE	C	48	−17.123	−49.875	86.744	1.00	27.65		C
ATOM	3668	CG	PHE	C	48	−17.029	−51.079	87.638	1.00	30.68		C
ATOM	3669	CD1	PHE	C	48	−16.381	−50.992	88.876	1.00	34.82		C
ATOM	3670	CD2	PHE	C	48	−17.539	−52.300	87.246	1.00	31.72		C
ATOM	3671	CE1	PHE	C	48	−16.247	−52.101	89.705	1.00	32.25		C
ATOM	3672	CE2	PHE	C	48	−17.423	−53.420	88.075	1.00	30.94		C
ATOM	3673	CZ	PHE	C	48	−16.775	−53.319	89.298	1.00	33.98		C
ATOM	3674	N	GLY	C	49	−16.078	−47.519	84.858	1.00	28.11		N
ATOM	3675	CA	GLY	C	49	−15.826	−47.128	83.488	1.00	29.63		C
ATOM	3676	C	GLY	C	49	−16.967	−46.291	82.950	1.00	32.96		C
ATOM	3677	O	GLY	C	49	−17.956	−46.032	83.640	1.00	32.51		O
ATOM	3678	N	GLU	C	50	−16.831	−45.916	81.674	1.00	31.40		N
ATOM	3679	CA	GLU	C	50	−17.768	−45.012	81.011	1.00	31.61		C
ATOM	3680	C	GLU	C	50	−17.854	−45.334	79.519	1.00	30.45		C
ATOM	3681	O	GLU	C	50	−16.891	−45.819	78.920	1.00	31.68		O
ATOM	3682	CB	GLU	C	50	−17.341	−43.542	81.204	1.00	28.42		C
ATOM	3683	CG	GLU	C	50	−15.895	−43.237	80.715	1.00	27.97		C
ATOM	3684	CD	GLU	C	50	−15.501	−41.745	80.792	1.00	33.91		C
ATOM	3685	OE1	GLU	C	50	−14.488	−41.342	80.144	1.00	32.01		O
ATOM	3686	OE2	GLU	C	50	−16.189	−40.969	81.511	1.00	33.87		O1−
ATOM	3687	N	ILE	C	51	−19.006	−45.009	78.914	1.00	31.49		N
ATOM	3688	CA	ILE	C	51	−19.254	−45.162	77.481	1.00	29.58		C
ATOM	3689	C	ILE	C	51	−19.904	−43.883	76.949	1.00	36.19		C
ATOM	3690	O	ILE	C	51	−20.636	−43.193	77.666	1.00	32.17		O
ATOM	3691	CB	ILE	C	51	−20.128	−46.407	77.173	1.00	30.54		C
ATOM	3692	CG1	ILE	C	51	−20.175	−46.709	75.657	1.00	30.91		C
ATOM	3693	CG2	ILE	C	51	−21.541	−46.263	77.756	1.00	22.08		C
ATOM	3694	CD1	ILE	C	51	−20.472	−48.177	75.340	1.00	21.13		C
ATOM	3695	N	SER	C	52	−19.687	−43.604	75.652	1.00	44.18		N
ATOM	3696	CA	SER	C	52	−19.747	−42.237	75.128	1.00	42.64		C
ATOM	3697	C	SER	C	52	−21.001	−41.880	74.342	1.00	41.94		C
ATOM	3698	O	SER	C	52	−21.272	−40.681	74.190	1.00	50.21		O
ATOM	3699	CB	SER	C	52	−18.545	−41.962	74.210	1.00	46.91		C
ATOM	3700	OG	SER	C	52	−18.720	−42.561	72.930	1.00	51.82		O
ATOM	3701	N	HIS	C	53	−21.739	−42.865	73.831	1.00	36.80		N
ATOM	3702	CA	HIS	C	53	−22.860	−42.688	72.900	1.00	46.33		C
ATOM	3703	C	HIS	C	53	−22.439	−43.129	71.515	1.00	45.86		C
ATOM	3704	O	HIS	C	53	−23.241	−43.704	70.781	1.00	49.43		O
ATOM	3705	CB	HIS	C	53	−23.410	−41.251	72.789	1.00	46.91		C
ATOM	3706	CG	HIS	C	53	−24.569	−41.127	71.846	1.00	52.45		C
ATOM	3707	ND1	HIS	C	53	−24.405	−40.953	70.488	1.00	47.45		N
ATOM	3708	CD2	HIS	C	53	−25.907	−41.185	72.059	1.00	50.31		C
ATOM	3709	CE1	HIS	C	53	−25.590	−40.915	69.905	1.00	43.08		C
ATOM	3710	NE2	HIS	C	53	−26.519	−41.054	70.835	1.00	45.78		N
ATOM	3711	N	SER	C	54	−21.183	−42.881	71.170	1.00	47.96		N
ATOM	3712	CA	SER	C	54	−20.637	−43.213	69.863	1.00	43.93		C
ATOM	3713	C	SER	C	54	−20.189	−44.668	69.568	1.00	48.52		C
ATOM	3714	O	SER	C	54	−19.920	−44.942	68.399	1.00	63.14		O
ATOM	3715	CB	SER	C	54	−19.464	−42.299	69.569	1.00	40.27		C
ATOM	3716	OG	SER	C	54	−18.399	−42.599	70.436	1.00	55.03		O
ATOM	3717	N	GLY	C	55	−19.968	−45.572	70.529	1.00	41.03		N
ATOM	3718	CA	GLY	C	55	−19.813	−45.352	71.953	1.00	41.92		C
ATOM	3719	C	GLY	C	55	−18.437	−45.851	72.360	1.00	42.37		C
ATOM	3720	O	GLY	C	55	−18.224	−47.051	72.578	1.00	27.61		O
ATOM	3721	N	SER	C	56	−17.483	−44.927	72.441	1.00	44.03		N
ATOM	3722	CA	SER	C	56	−16.156	−45.301	72.891	1.00	40.77		C
ATOM	3723	C	SER	C	56	−16.173	−45.524	74.394	1.00	39.74		C
ATOM	3724	O	SER	C	56	−17.034	−45.019	75.114	1.00	41.06		O
ATOM	3725	CB	SER	C	56	−15.122	−44.243	72.520	1.00	39.37		C
ATOM	3726	OG	SER	C	56	−15.509	−42.986	73.018	1.00	48.88		O
ATOM	3727	N	THR	C	57	−15.206	−46.299	74.857	1.00	38.23		N
ATOM	3728	CA	THR	C	57	−15.193	−46.845	76.196	1.00	29.07		C
ATOM	3729	C	THR	C	57	−13.912	−46.459	76.932	1.00	32.82		C
ATOM	3730	O	THR	C	57	−12.865	−46.266	76.312	1.00	34.18		O
ATOM	3731	CB	THR	C	57	−15.325	−48.352	76.054	1.00	31.23		C
ATOM	3732	OG1	THR	C	57	−16.527	−48.801	76.681	1.00	34.61		O
ATOM	3733	CG2	THR	C	57	−14.109	−49.052	76.571	1.00	31.55		C
ATOM	3734	N	ASN	C	58	−14.002	−46.318	78.257	1.00	31.01		N
ATOM	3735	CA	ASN	C	58	−12.838	−46.118	79.121	1.00	27.41		C
ATOM	3736	C	ASN	C	58	−13.078	−46.909	80.389	1.00	30.68		C
ATOM	3737	O	ASN	C	58	−14.007	−46.592	81.136	1.00	31.50		O
ATOM	3738	CB	ASN	C	58	−12.590	−44.649	79.491	1.00	24.84		C
ATOM	3739	CG	ASN	C	58	−12.449	−43.760	78.297	1.00	28.91		C
ATOM	3740	OD1	ASN	C	58	−11.439	−43.792	77.598	1.00	34.90		O
ATOM	3741	ND2	ASN	C	58	−13.458	−42.937	78.055	1.00	33.30		N
ATOM	3742	N	TYR	C	59	−12.249	−47.915	80.640	1.00	29.82		N
ATOM	3743	CA	TYR	C	59	−12.450	−48.796	81.775	1.00	33.27		C
ATOM	3744	C	TYR	C	59	−11.447	−48.512	82.871	1.00	30.48		C
ATOM	3745	O	TYR	C	59	−10.402	−47.903	82.644	1.00	32.69		O
ATOM	3746	CB	TYR	C	59	−12.326	−50.263	81.379	1.00	31.17		C
ATOM	3747	CG	TYR	C	59	−13.321	−50.726	80.367	1.00	34.24		C
ATOM	3748	CD1	TYR	C	59	−14.679	−50.757	80.670	1.00	35.71		C
ATOM	3749	CD2	TYR	C	59	−12.913	−51.192	79.125	1.00	34.28		C
ATOM	3750	CE1	TYR	C	59	−15.611	−51.214	79.741	1.00	37.87		C
ATOM	3751	CE2	TYR	C	59	−13.837	−51.665	78.194	1.00	33.51		C
ATOM	3752	CZ	TYR	C	59	−15.183	−51.659	78.498	1.00	33.62		C
ATOM	3753	OH	TYR	C	59	−16.095	−52.115	77.572	1.00	34.03		O
ATOM	3754	N	ASN	C	60	−11.765	−48.993	84.060	1.00	29.37		N
ATOM	3755	CA	ASN	C	60	−10.778	−48.990	85.128	1.00	38.84		C
ATOM	3756	C	ASN	C	60	−9.747	−50.095	84.877	1.00	40.23		C
ATOM	3757	O	ASN	C	60	−10.119	−51.280	84.829	1.00	38.66		O
ATOM	3758	CB	ASN	C	60	−11.437	−49.191	86.480	1.00	32.03		C
ATOM	3759	CG	ASN	C	60	−10.484	−48.942	87.617	1.00	34.48		C
ATOM	3760	OD1	ASN	C	60	−9.270	−48.906	87.422	1.00	34.69		O
ATOM	3761	ND2	ASN	C	60	−11.018	−48.808	88.819	1.00	30.93		N
ATOM	3762	N	PRO	C	61	−8.458	−49.763	84.741	1.00	38.19		N
ATOM	3763	CA	PRO	C	61	−7.459	−50.799	84.419	1.00	38.23		C
ATOM	3764	C	PRO	C	61	−7.385	−51.943	85.412	1.00	36.76		C
ATOM	3765	O	PRO	C	61	−6.981	−53.047	85.035	1.00	42.26		O
ATOM	3766	CB	PRO	C	61	−6.156	−49.991	84.368	1.00	37.21		C
ATOM	3767	CG	PRO	C	61	−6.609	−48.658	83.864	1.00	35.33		C
ATOM	3768	CD	PRO	C	61	−7.870	−48.412	84.660	1.00	38.00		C
ATOM	3769	N	SER	C	62	−7.766	−51.718	86.663	1.00	37.94		N
ATOM	3770	CA	SER	C	62	−7.755	−52.781	87.665	1.00	41.69		C
ATOM	3771	C	SER	C	62	−8.781	−53.878	87.376	1.00	45.04		C
ATOM	3772	O	SER	C	62	−8.587	−55.025	87.790	1.00	52.57		O
ATOM	3773	CB	SER	C	62	−8.016	−52.197	89.039	1.00	36.72		C
ATOM	3774	OG	SER	C	62	−9.370	−51.807	89.106	1.00	43.47		O
ATOM	3775	N	LEU	C	63	−9.927	−53.530	86.792	1.00	39.84		N
ATOM	3776	CA	LEU	C	63	−10.881	−54.557	86.394	1.00	42.71		C
ATOM	3777	C	LEU	C	63	−10.311	−55.431	85.298	1.00	47.05		C
ATOM	3778	O	LEU	C	63	−10.608	−56.635	85.235	1.00	44.87		O
ATOM	3779	CB	LEU	C	63	−12.177	−53.929	85.914	1.00	39.14		C
ATOM	3780	CG	LEU	C	63	−12.942	−53.409	87.106	1.00	41.14		C
ATOM	3781	CD1	LEU	C	63	−14.324	−52.965	86.651	1.00	39.64		C
ATOM	3782	CD2	LEU	C	63	−13.003	−54.481	88.194	1.00	37.86		C
ATOM	3783	N	LYS	C	64	−9.555	−54.816	84.389	1.00	50.10		N
ATOM	3784	CA	LYS	C	64	−8.831	−55.520	83.346	1.00	45.99		C
ATOM	3785	C	LYS	C	64	−9.797	−56.175	82.376	1.00	46.14		C
ATOM	3786	O	LYS	C	64	−10.663	−55.500	81.805	1.00	47.95		O
ATOM	3787	CB	LYS	C	64	−7.875	−56.515	84.000	1.00	45.38		C
ATOM	3788	CG	LYS	C	64	−6.494	−56.522	83.397	1.00	56.60		C
ATOM	3789	CD	LYS	C	64	−5.651	−57.503	84.141	1.00	57.39		C
ATOM	3790	CE	LYS	C	64	−5.450	−56.943	85.551	1.00	64.49		C
ATOM	3791	NZ	LYS	C	64	−4.775	−57.891	86.483	1.00	75.39		N1+
ATOM	3792	N	ALA	C	65	−9.676	−57.484	82.203	1.00	43.80		N
ATOM	3793	CA	ALA	C	65	−10.484	−58.168	81.210	1.00	43.71		C
ATOM	3794	C	ALA	C	65	−11.908	−58.474	81.670	1.00	40.71		C
ATOM	3795	O	ALA	C	65	−12.730	−58.856	80.830	1.00	46.79		O
ATOM	3796	CB	ALA	C	65	−9.789	−59.462	80.808	1.00	46.98		C
ATOM	3797	N	ARG	C	66	−12.232	−58.303	82.958	1.00	34.69		N
ATOM	3798	CA	ARG	C	66	−13.508	−58.800	83.490	1.00	35.91		C
ATOM	3799	C	ARG	C	66	−14.721	−57.969	83.088	1.00	34.48		C
ATOM	3800	O	ARG	C	66	−15.841	−58.467	83.207	1.00	34.86		O
ATOM	3801	CB	ARG	C	66	−13.467	−58.840	85.013	1.00	37.25		C
ATOM	3802	CG	ARG	C	66	−12.241	−59.497	85.584	1.00	41.56		C
ATOM	3803	CD	ARG	C	66	−12.258	−59.442	87.090	1.00	33.48		C
ATOM	3804	NE	ARG	C	66	−13.537	−59.870	87.586	1.00	36.42		N
ATOM	3805	CZ	ARG	C	66	−14.096	−59.444	88.710	1.00	31.00		C
ATOM	3806	NH1	ARG	C	66	−15.275	−59.921	89.045	1.00	32.67		N
ATOM	3807	NH2	ARG	C	66	−13.499	−58.556	89.483	1.00	29.13		N
ATOM	3808	N	VAL	C	67	−14.545	−56.720	82.650	1.00	36.81		N
ATOM	3809	CA	VAL	C	67	−15.642	−55.760	82.552	1.00	33.37		C
ATOM	3810	C	VAL	C	67	−15.923	−55.381	81.104	1.00	38.37		C
ATOM	3811	O	VAL	C	67	−15.005	−55.251	80.288	1.00	41.21		O
ATOM	3812	CB	VAL	C	67	−15.353	−54.501	83.391	1.00	36.36		C
ATOM	3813	CG1	VAL	C	67	−14.134	−53.780	82.865	1.00	34.65		C
ATOM	3814	CG2	VAL	C	67	−16.552	−53.582	83.346	1.00	36.14		C
ATOM	3815	N	THR	C	68	−17.203	−55.212	80.792	1.00	35.08		N
ATOM	3816	CA	THR	C	68	−17.654	−54.712	79.510	1.00	32.85		C
ATOM	3817	C	THR	C	68	−18.769	−53.715	79.758	1.00	29.58		C
ATOM	3818	O	THR	C	68	−19.686	−53.981	80.536	1.00	30.01		O
ATOM	3819	CB	THR	C	68	−18.196	−55.829	78.605	1.00	36.95		C
ATOM	3820	OG1	THR	C	68	−17.324	−56.957	78.657	1.00	39.01		O
ATOM	3821	CG2	THR	C	68	−18.339	−55.320	77.154	1.00	28.49		C
ATOM	3822	N	ILE	C	69	−18.719	−52.595	79.060	1.00	33.88		N
ATOM	3823	CA	ILE	C	69	−19.792	−51.617	79.088	1.00	33.76		C
ATOM	3824	C	ILE	C	69	−20.257	−51.398	77.658	1.00	34.31		C
ATOM	3825	O	ILE	C	69	−19.439	−51.192	76.757	1.00	34.33		O
ATOM	3826	CB	ILE	C	69	−19.349	−50.307	79.752	1.00	25.14		C
ATOM	3827	CG1	ILE	C	69	−19.047	−50.590	81.218	1.00	24.64		C
ATOM	3828	CG2	ILE	C	69	−20.418	−49.246	79.567	1.00	21.90		C
ATOM	3829	CD1	ILE	C	69	−18.299	−49.486	81.965	1.00	29.90		C
ATOM	3830	N	SER	C	70	−21.567	−51.459	77.455	1.00	35.47		N
ATOM	3831	CA	SER	C	70	−22.170	−51.319	76.141	1.00	33.35		C
ATOM	3832	C	SER	C	70	−23.321	−50.323	76.226	1.00	31.43		C
ATOM	3833	O	SER	C	70	−23.862	−50.073	77.305	1.00	30.39		O
ATOM	3834	CB	SER	C	70	−22.654	−52.668	75.638	1.00	23.50		C
ATOM	3835	OG	SER	C	70	−23.508	−53.222	76.609	1.00	35.38		O
ATOM	3836	N	ILE	C	71	−23.683	−49.755	75.074	1.00	30.99		N
ATOM	3837	CA	ILE	C	71	−24.705	−48.722	74.981	1.00	30.48		C
ATOM	3838	C	ILE	C	71	−25.660	−49.058	73.838	1.00	34.95		C
ATOM	3839	O	ILE	C	71	−25.246	−49.587	72.806	1.00	34.86		O
ATOM	3840	CB	ILE	C	71	−24.064	−47.335	74.790	1.00	32.81		C
ATOM	3841	CG1	ILE	C	71	−25.061	−46.237	75.120	1.00	29.16		C
ATOM	3842	CG2	ILE	C	71	−23.480	−47.167	73.376	1.00	30.88		C
ATOM	3843	CD1	ILE	C	71	−24.442	−44.876	75.149	1.00	30.80		C
ATOM	3844	N	ASP	C	72	−26.949	−48.798	74.042	1.00	39.76		N
ATOM	3845	CA	ASP	C	72	−27.988	−48.981	73.025	1.00	35.04		C
ATOM	3846	C	ASP	C	72	−28.651	−47.630	72.771	1.00	39.02		C
ATOM	3847	O	ASP	C	72	−29.552	−47.241	73.518	1.00	43.96		O
ATOM	3848	CB	ASP	C	72	−29.012	−50.011	73.491	1.00	37.61		C
ATOM	3849	CG	ASP	C	72	−30.119	−50.283	72.465	1.00	45.97		C
ATOM	3850	OD1	ASP	C	72	−30.612	−49.345	71.798	1.00	48.11		O
ATOM	3851	OD2	ASP	C	72	−30.518	−51.461	72.346	1.00	49.16		O1−
ATOM	3852	N	THR	C	73	−28.231	−46.910	71.726	1.00	38.09		N
ATOM	3853	CA	THR	C	73	−28.807	−45.586	71.501	1.00	40.83		C
ATOM	3854	C	THR	C	73	−30.255	−45.626	71.029	1.00	44.67		C
ATOM	3855	O	THR	C	73	−30.892	−44.568	70.997	1.00	48.41		O
ATOM	3856	CB	THR	C	73	−27.996	−44.759	70.502	1.00	39.06		C
ATOM	3857	OG1	THR	C	73	−27.774	−45.521	69.308	1.00	46.00		O
ATOM	3858	CG2	THR	C	73	−26.679	−44.327	71.114	1.00	40.64		C
ATOM	3859	O	SER	C	74	−33.984	−45.804	71.487	1.00	55.05		O
ATOM	3860	N	SER	C	74	−30.781	−46.782	70.622	1.00	41.41		N
ATOM	3861	CA	SER	C	74	−32.194	−46.829	70.244	1.00	49.65		C
ATOM	3862	C	SER	C	74	−33.087	−46.665	71.466	1.00	55.28		C
ATOM	3863	CB	SER	C	74	−32.524	−48.149	69.539	1.00	50.83		C
ATOM	3864	OG	SER	C	74	−31.745	−48.338	68.375	1.00	60.96		O
ATOM	3865	O	LYS	C	75	−33.672	−46.626	75.929	1.00	49.05		O
ATOM	3866	N	LYS	C	75	−32.833	−47.481	72.498	1.00	48.96		N
ATOM	3867	CA	LYS	C	75	−33.603	−47.551	73.730	1.00	48.48		C
ATOM	3868	C	LYS	C	75	−33.120	−46.598	74.819	1.00	45.98		C
ATOM	3869	CB	LYS	C	75	−33.594	−48.986	74.274	1.00	47.37		C
ATOM	3870	CG	LYS	C	75	−34.202	−49.988	73.320	1.00	54.32		C
ATOM	3871	CD	LYS	C	75	−34.219	−51.397	73.886	1.00	53.30		C
ATOM	3872	CE	LYS	C	75	−34.656	−52.383	72.819	1.00	62.19		C
ATOM	3873	NZ	LYS	C	75	−35.421	−53.518	73.409	1.00	63.45		N
ATOM	3874	O	ASN	C	76	−31.622	−45.589	77.918	1.00	39.83		O
ATOM	3875	N	ASN	C	76	−32.109	−45.772	74.550	1.00	41.83		N
ATOM	3876	CA	ASN	C	76	−31.496	−44.951	75.593	1.00	43.47		C
ATOM	3877	C	ASN	C	76	−31.146	−45.811	76.807	1.00	36.05		C
ATOM	3878	CB	ASN	C	76	−32.402	−43.771	75.976	1.00	36.10		C
ATOM	3879	CG	ASN	C	76	−32.342	−42.656	74.963	1.00	38.85		C
ATOM	3880	OD1	ASN	C	76	−31.821	−42.833	73.857	1.00	46.14		O
ATOM	3881	ND2	ASN	C	76	−32.863	−41.498	75.326	1.00	45.02		N
ATOM	3882	N	GLN	C	77	−30.384	−46.868	76.554	1.00	35.70		N
ATOM	3883	CA	GLN	C	77	−29.976	−47.812	77.580	1.00	35.90		C
ATOM	3884	C	GLN	C	77	−28.472	−48.013	77.506	1.00	36.92		C
ATOM	3885	O	GLN	C	77	−27.858	−47.827	76.452	1.00	34.91		O
ATOM	3886	CB	GLN	C	77	−30.697	−49.147	77.409	1.00	33.22		C
ATOM	3887	CG	GLN	C	77	−32.184	−49.061	77.707	1.00	37.44		C
ATOM	3888	CD	GLN	C	77	−32.889	−50.386	77.542	1.00	35.36		C
ATOM	3889	OE1	GLN	C	77	−32.301	−51.358	77.088	1.00	30.09		O
ATOM	3890	NE2	GLN	C	77	−34.154	−50.431	77.919	1.00	37.97		N
ATOM	3891	N	PHE	C	78	−27.882	−48.404	78.638	1.00	30.45		N
ATOM	3892	CA	PHE	C	78	−26.495	−48.839	78.650	1.00	28.00		C
ATOM	3893	C	PHE	C	78	−26.342	−49.884	79.739	1.00	32.46		C
ATOM	3894	O	PHE	C	78	−27.128	−49.933	80.686	1.00	33.14		O
ATOM	3895	CB	PHE	C	78	−25.501	−47.668	78.812	1.00	29.59		C
ATOM	3896	CG	PHE	C	78	−25.617	−46.911	80.109	1.00	29.92		C
ATOM	3897	CD1	PHE	C	78	−26.541	−45.898	80.252	1.00	28.69		C
ATOM	3898	CD2	PHE	C	78	−24.767	−47.182	81.160	1.00	29.77		C
ATOM	3899	CE1	PHE	C	78	−26.635	−45.191	81.422	1.00	31.87		C
ATOM	3900	CE2	PHE	C	78	−24.865	−46.484	82.343	1.00	32.84		C
ATOM	3901	CZ	PHE	C	78	−25.800	−45.481	82.475	1.00	32.57		C
ATOM	3902	N	SER	C	79	−25.321	−50.732	79.595	1.00	30.53		N
ATOM	3903	CA	SER	C	79	−25.288	−51.973	80.344	1.00	27.00		C
ATOM	3904	C	SER	C	79	−23.887	−52.250	80.869	1.00	29.56		C
ATOM	3905	O	SER	C	79	−22.890	−51.729	80.365	1.00	29.66		O
ATOM	3906	CB	SER	C	79	−25.778	−53.134	79.474	1.00	30.28		C
ATOM	3907	OG	SER	C	79	−27.128	−52.938	79.104	1.00	31.71		O
ATOM	3908	N	LEU	C	80	−23.833	−53.114	81.879	1.00	24.67		N
ATOM	3909	CA	LEU	C	80	−22.595	−53.502	82.522	1.00	26.25		C
ATOM	3910	C	LEU	C	80	−22.509	−55.012	82.551	1.00	31.30		C
ATOM	3911	O	LEU	C	80	−23.454	−55.677	82.982	1.00	32.63		O
ATOM	3912	CB	LEU	C	80	−22.519	−52.968	83.957	1.00	30.49		C
ATOM	3913	CG	LEU	C	80	−21.310	−53.471	84.764	1.00	31.84		C
ATOM	3914	CD1	LEU	C	80	−19.986	−52.935	84.206	1.00	24.42		C
ATOM	3915	CD2	LEU	C	80	−21.459	−53.149	86.240	1.00	29.26		C
ATOM	3916	N	LYS	C	81	−21.377	−55.549	82.111	1.00	29.00		N
ATOM	3917	CA	LYS	C	81	−21.065	−56.958	82.299	1.00	31.81		C
ATOM	3918	C	LYS	C	81	−19.803	−57.045	83.139	1.00	31.17		C
ATOM	3919	O	LYS	C	81	−18.822	−56.361	82.845	1.00	34.99		O
ATOM	3920	CB	LYS	C	81	−20.864	−57.684	80.964	1.00	28.39		C
ATOM	3921	CG	LYS	C	81	−22.140	−57.880	80.163	1.00	33.95		C
ATOM	3922	CD	LYS	C	81	−22.873	−59.151	80.545	1.00	40.33		C
ATOM	3923	CE	LYS	C	81	−24.202	−59.282	79.817	1.00	42.26		C
ATOM	3924	NZ	LYS	C	81	−24.025	−59.096	78.349	1.00	53.78		N1+
ATOM	3925	N	LEU	C	82	−19.835	−57.857	84.193	1.00	30.70		N
ATOM	3926	CA	LEU	C	82	−18.652	−58.141	85.004	1.00	28.52		C
ATOM	3927	C	LEU	C	82	−18.571	−59.645	85.180	1.00	31.87		C
ATOM	3928	O	LEU	C	82	−19.434	−60.247	85.824	1.00	37.82		O
ATOM	3929	CB	LEU	C	82	−18.701	−57.439	86.356	1.00	33.35		C
ATOM	3930	CG	LEU	C	82	−17.543	−57.699	87.330	1.00	35.28		C
ATOM	3931	CD1	LEU	C	82	−16.244	−57.034	86.881	1.00	26.92		C
ATOM	3932	CD2	LEU	C	82	−17.950	−57.297	88.741	1.00	25.50		C
ATOM	3933	N	ARG	C	83	−17.554	−60.251	84.600	1.00	36.83		N
ATOM	3934	CA	ARG	C	83	−17.451	−61.703	84.527	1.00	39.83		C
ATOM	3935	C	ARG	C	83	−16.737	−62.289	85.745	1.00	38.25		C
ATOM	3936	O	ARG	C	83	−16.042	−61.586	86.490	1.00	34.22		O
ATOM	3937	CB	ARG	C	83	−16.745	−62.101	83.221	1.00	31.30		C
ATOM	3938	CG	ARG	C	83	−17.726	−62.259	82.070	1.00	37.56		C
ATOM	3939	CD	ARG	C	83	−17.165	−62.116	80.661	1.00	34.40		C
ATOM	3940	NE	ARG	C	83	−17.224	−60.730	80.213	1.00	37.07		N
ATOM	3941	CZ	ARG	C	83	−16.174	−59.946	80.029	1.00	39.95		C
ATOM	3942	NH1	ARG	C	83	−16.359	−58.701	79.618	1.00	31.66		N1+
ATOM	3943	NH2	ARG	C	83	−14.947	−60.412	80.249	1.00	46.34		N
ATOM	3944	N	SER	C	84	−16.975	−63.586	85.964	1.00	35.95		N
ATOM	3945	CA	SER	C	84	−16.215	−64.416	86.908	1.00	36.75		C
ATOM	3946	C	SER	C	84	−16.089	−63.725	88.271	1.00	37.32		C
ATOM	3947	O	SER	C	84	−15.020	−63.344	88.754	1.00	41.30		O
ATOM	3948	CB	SER	C	84	−14.857	−64.809	86.316	1.00	31.04		C
ATOM	3949	OG	SER	C	84	−14.036	−63.687	86.179	1.00	38.56		O
ATOM	3950	N	VAL	C	85	−17.235	−63.589	88.856	1.00	33.08		N
ATOM	3951	CA	VAL	C	85	−17.473	−62.751	90.014	1.00	32.08		C
ATOM	3952	C	VAL	C	85	−17.088	−63.499	91.292	1.00	32.80		C
ATOM	3953	O	VAL	C	85	−17.190	−64.723	91.359	1.00	32.85		O
ATOM	3954	CB	VAL	C	85	−18.965	−62.372	89.921	1.00	32.31		C
ATOM	3955	CG1	VAL	C	85	−19.791	−63.006	90.981	1.00	35.43		C
ATOM	3956	CG2	VAL	C	85	−19.159	−60.893	89.771	1.00	33.02		C
ATOM	3957	N	THR	C	86	−16.596	−62.785	92.310	1.00	36.06		N
ATOM	3958	CA	THR	C	86	−16.263	−63.389	93.614	1.00	32.42		C
ATOM	3959	C	THR	C	86	−16.976	−62.624	94.727	1.00	32.82		C
ATOM	3960	O	THR	C	86	−17.644	−61.619	94.485	1.00	32.02		O
ATOM	3961	CB	THR	C	86	−14.760	−63.395	93.919	1.00	32.77		C
ATOM	3962	OG1	THR	C	86	−14.390	−62.115	94.438	1.00	35.84		O
ATOM	3963	CG2	THR	C	86	−13.914	−63.727	92.683	1.00	31.07		C
ATOM	3964	N	ALA	C	87	−16.813	−63.084	95.972	1.00	34.97		N
ATOM	3965	CA	ALA	C	87	−17.533	−62.446	97.079	1.00	35.92		C
ATOM	3966	C	ALA	C	87	−17.170	−60.978	97.205	1.00	36.06		C
ATOM	3967	O	ALA	C	87	−18.015	−60.163	97.593	1.00	34.31		O
ATOM	3968	CB	ALA	C	87	−17.241	−63.146	98.407	1.00	24.03		C
ATOM	3969	N	ALA	C	88	−15.927	−60.626	96.853	1.00	32.27		N
ATOM	3970	CA	ALA	C	88	−15.448	−59.255	96.922	1.00	32.44		C
ATOM	3971	C	ALA	C	88	−16.179	−58.331	95.964	1.00	35.33		C
ATOM	3972	O	ALA	C	88	−15.973	−57.119	96.027	1.00	41.10		O
ATOM	3973	CB	ALA	C	88	−13.953	−59.211	96.632	1.00	26.07		C
ATOM	3974	N	ASP	C	89	−17.024	−58.861	95.090	1.00	31.77		N
ATOM	3975	CA	ASP	C	89	−17.818	−58.037	94.203	1.00	29.68		C
ATOM	3976	C	ASP	C	89	−19.198	−57.735	94.785	1.00	28.71		C
ATOM	3977	O	ASP	C	89	−20.017	−57.099	94.115	1.00	29.06		O
ATOM	3978	CB	ASP	C	89	−17.943	−58.712	92.825	1.00	36.29		C
ATOM	3979	CG	ASP	C	89	−16.584	−58.922	92.122	1.00	33.46		C
ATOM	3980	OD1	ASP	C	89	−15.893	−57.927	91.817	1.00	37.02		O
ATOM	3981	OD2	ASP	C	89	−16.209	−60.092	91.867	1.00	34.16		O1−
ATOM	3982	N	THR	C	90	−19.454	−58.137	96.028	1.00	27.76		N
ATOM	3983	CA	THR	C	90	−20.653	−57.712	96.747	1.00	34.87		C
ATOM	3984	C	THR	C	90	−20.606	−56.194	96.997	1.00	27.98		C
ATOM	3985	O	THR	C	90	−19.694	−55.699	97.659	1.00	27.17		O
ATOM	3986	CB	THR	C	90	−20.747	−58.492	98.058	1.00	32.97		C
ATOM	3987	OG1	THR	C	90	−20.912	−59.884	97.753	1.00	34.09		O
ATOM	3988	CG2	THR	C	90	−21.914	−58.010	98.923	1.00	24.31		C
ATOM	3989	N	ALA	C	91	−21.575	−55.456	96.461	1.00	24.84		N
ATOM	3990	CA	ALA	C	91	−21.553	−53.998	96.516	1.00	25.95		C
ATOM	3991	C	ALA	C	91	−22.876	−53.467	95.992	1.00	29.10		C
ATOM	3992	O	ALA	C	91	−23.667	−54.198	95.393	1.00	30.38		O
ATOM	3993	CB	ALA	C	91	−20.408	−53.408	95.698	1.00	27.41		C
ATOM	3994	N	VAL	C	92	−23.121	−52.183	96.249	1.00	28.41		N
ATOM	3995	CA	VAL	C	92	−24.154	−51.471	95.517	1.00	25.07		C
ATOM	3996	C	VAL	C	92	−23.533	−50.973	94.227	1.00	26.45		C
ATOM	3997	O	VAL	C	92	−22.473	−50.348	94.242	1.00	29.34		O
ATOM	3998	CB	VAL	C	92	−24.746	−50.313	96.338	1.00	25.04		C
ATOM	3999	CG1	VAL	C	92	−25.682	−49.486	95.466	1.00	22.80		C
ATOM	4000	CG2	VAL	C	92	−25.542	−50.843	97.503	1.00	26.44		C
ATOM	4001	N	TYR	C	93	−24.177	−51.270	93.107	1.00	29.41		N
ATOM	4002	CA	TYR	C	93	−23.720	−50.835	91.800	1.00	25.88		C
ATOM	4003	C	TYR	C	93	−24.646	−49.722	91.336	1.00	24.87		C
ATOM	4004	O	TYR	C	93	−25.854	−49.927	91.241	1.00	28.12		O
ATOM	4005	CB	TYR	C	93	−23.703	−52.015	90.826	1.00	23.05		C
ATOM	4006	CG	TYR	C	93	−22.607	−53.020	91.156	1.00	28.89		C
ATOM	4007	CD1	TYR	C	93	−22.704	−53.859	92.280	1.00	24.24		C
ATOM	4008	CD2	TYR	C	93	−21.462	−53.115	90.359	1.00	26.34		C
ATOM	4009	CE1	TYR	C	93	−21.702	−54.752	92.593	1.00	23.55		C
ATOM	4010	CE2	TYR	C	93	−20.449	−53.996	90.670	1.00	26.02		C
ATOM	4011	CZ	TYR	C	93	−20.566	−54.818	91.783	1.00	26.56		C
ATOM	4012	OH	TYR	C	93	−19.535	−55.695	92.078	1.00	23.40		O
ATOM	4013	N	TYR	C	94	−24.085	−48.550	91.070	1.00	23.22		N
ATOM	4014	CA	TYR	C	94	−24.829	−47.415	90.541	1.00	28.65		C
ATOM	4015	C	TYR	C	94	−24.425	−47.179	89.097	1.00	25.80		C
ATOM	4016	O	TYR	C	94	−23.241	−47.248	88.766	1.00	24.60		O
ATOM	4017	CB	TYR	C	94	−24.547	−46.097	91.309	1.00	25.22		C
ATOM	4018	CG	TYR	C	94	−24.796	−46.109	92.775	1.00	22.71		C
ATOM	4019	CD1	TYR	C	94	−26.082	−45.978	93.280	1.00	24.72		C
ATOM	4020	CD2	TYR	C	94	−23.738	−46.219	93.672	1.00	20.09		C
ATOM	4021	CE1	TYR	C	94	−26.311	−45.997	94.640	1.00	22.52		C
ATOM	4022	CE2	TYR	C	94	−23.950	−46.237	95.020	1.00	17.42		C
ATOM	4023	CZ	TYR	C	94	−25.240	−46.119	95.508	1.00	27.12		C
ATOM	4024	OH	TYR	C	94	−25.463	−46.130	96.877	1.00	35.58		O
ATOM	4025	N	CYS	C	95	−25.391	−46.795	88.272	1.00	25.05		N
ATOM	4026	CA	CYS	C	95	−25.096	−46.099	87.030	1.00	26.50		C
ATOM	4027	C	CYS	C	95	−25.220	−44.602	87.287	1.00	28.56		C
ATOM	4028	O	CYS	C	95	−25.943	−44.161	88.192	1.00	25.46		O
ATOM	4029	CB	CYS	C	95	−26.022	−46.563	85.883	1.00	27.62		C
ATOM	4030	SG	CYS	C	95	−27.838	−46.477	86.215	1.00	41.12		S
ATOM	4031	N	ALA	C	96	−24.469	−43.816	86.520	1.00	26.44		N
ATOM	4032	CA	ALA	C	96	−24.522	−42.377	86.723	1.00	27.54		C
ATOM	4033	C	ALA	C	96	−24.302	−41.656	85.408	1.00	32.97		C
ATOM	4034	O	ALA	C	96	−23.727	−42.202	84.464	1.00	34.61		O
ATOM	4035	CB	ALA	C	96	−23.493	−41.909	87.746	1.00	24.37		C
ATOM	4036	N	ARG	C	97	−24.772	−40.412	85.364	1.00	35.37		N
ATOM	4037	CA	ARG	C	97	−24.529	−39.520	84.244	1.00	26.30		C
ATOM	4038	C	ARG	C	97	−23.290	−38.679	84.524	1.00	28.79		C
ATOM	4039	O	ARG	C	97	−23.208	−38.000	85.551	1.00	27.36		O
ATOM	4040	CB	ARG	C	97	−25.732	−38.630	83.997	1.00	29.64		C
ATOM	4041	CG	ARG	C	97	−25.581	−37.755	82.773	1.00	32.76		C
ATOM	4042	CD	ARG	C	97	−26.887	−37.112	82.453	1.00	32.80		C
ATOM	4043	NE	ARG	C	97	−26.856	−35.720	82.854	1.00	39.43		N
ATOM	4044	CZ	ARG	C	97	−27.927	−34.974	83.090	1.00	37.66		C
ATOM	4045	NH1	ARG	C	97	−27.763	−33.707	83.447	1.00	44.97		N1+
ATOM	4046	NH2	ARG	C	97	−29.146	−35.483	82.978	1.00	39.25		N
ATOM	4047	N	ASP	C	98	−22.322	−38.755	83.621	1.00	30.15		N
ATOM	4048	CA	ASP	C	98	−21.054	−38.053	83.724	1.00	29.73		C
ATOM	4049	C	ASP	C	98	−21.145	−36.751	82.929	1.00	33.62		C
ATOM	4050	O	ASP	C	98	−21.487	−36.781	81.742	1.00	31.03		O
ATOM	4051	CB	ASP	C	98	−19.936	−38.949	83.190	1.00	30.30		C
ATOM	4052	CG	ASP	C	98	−18.555	−38.414	83.490	1.00	31.40		C
ATOM	4053	OD1	ASP	C	98	−18.240	−37.292	83.033	1.00	31.40		O1−
ATOM	4054	OD2	ASP	C	98	−17.779	−39.139	84.160	1.00	32.47		O
ATOM	4055	N	TYR	C	99	−20.901	−35.610	83.601	1.00	32.07		N
ATOM	4056	CA	TYR	C	99	−20.981	−34.283	82.971	1.00	29.21		C
ATOM	4057	C	TYR	C	99	−20.323	−33.081	83.723	1.00	28.12		C
ATOM	4058	O	TYR	C	99	−21.081	−32.255	84.196	1.00	36.95		O
ATOM	4059	CB	TYR	C	99	−22.484	−33.958	82.761	1.00	35.21		C
ATOM	4060	CG	TYR	C	99	−22.884	−32.899	81.729	1.00	37.19		C
ATOM	4061	CD1	TYR	C	99	−22.518	−33.004	80.378	1.00	37.05		C
ATOM	4062	CD2	TYR	C	99	−23.629	−31.784	82.114	1.00	38.73		C
ATOM	4063	CE1	TYR	C	99	−22.905	−32.034	79.447	1.00	36.99		C
ATOM	4064	CE2	TYR	C	99	−24.008	−30.801	81.195	1.00	32.76		C
ATOM	4065	CZ	TYR	C	99	−23.652	−30.924	79.871	1.00	40.53		C
ATOM	4066	OH	TYR	C	99	−24.045	−29.934	78.971	1.00	41.60		O
ATOM	4067	N	GLY	C	100	−19.003	−32.924	83.921	1.00	28.67		N
ATOM	4068	CA	GLY	C	100	−17.960	−33.926	83.970	1.00	29.97		C
ATOM	4069	C	GLY	C	100	−17.825	−34.458	85.387	1.00	28.43		C
ATOM	4070	O	GLY	C	100	−17.023	−35.343	85.668	1.00	35.72		O
ATOM	4071	N	ALA	C	101	−18.638	−33.941	86.294	1.00	28.13		N
ATOM	4072	CA	ALA	C	101	−18.846	−34.644	87.546	1.00	23.31		C
ATOM	4073	C	ALA	C	101	−20.080	−35.531	87.385	1.00	29.38		C
ATOM	4074	O	ALA	C	101	−20.763	−35.484	86.363	1.00	31.34		O
ATOM	4075	CB	ALA	C	101	−19.026	−33.659	88.689	1.00	26.55		C
ATOM	4076	N	PHE	C	102	−20.379	−36.347	88.395	1.00	25.69		N
ATOM	4077	CA	PHE	C	102	−21.562	−37.213	88.337	1.00	30.27		C
ATOM	4078	C	PHE	C	102	−22.754	−36.480	88.948	1.00	27.72		C
ATOM	4079	O	PHE	C	102	−22.912	−36.444	90.170	1.00	25.66		O
ATOM	4080	CB	PHE	C	102	−21.314	−38.547	89.035	1.00	28.00		C
ATOM	4081	CG	PHE	C	102	−20.216	−39.368	88.406	1.00	28.82		C
ATOM	4082	CD1	PHE	C	102	−20.377	−39.915	87.135	1.00	26.74		C
ATOM	4083	CD2	PHE	C	102	−19.002	−39.556	89.069	1.00	25.45		C
ATOM	4084	CE1	PHE	C	102	−19.376	−40.658	86.548	1.00	23.07		C
ATOM	4085	CE2	PHE	C	102	−17.987	−40.307	88.488	1.00	27.62		C
ATOM	4086	CZ	PHE	C	102	−18.173	−40.859	87.220	1.00	24.95		C
ATOM	4087	N	ASP	C	103	−23.611	−35.906	88.097	1.00	25.30		N
ATOM	4088	CA	ASP	C	103	−24.746	−35.131	88.591	1.00	29.00		C
ATOM	4089	C	ASP	C	103	−26.021	−35.943	88.801	1.00	32.32		C
ATOM	4090	O	ASP	C	103	−26.862	−35.523	89.596	1.00	36.85		O
ATOM	4091	CB	ASP	C	103	−25.067	−33.937	87.671	1.00	26.81		C
ATOM	4092	CG	ASP	C	103	−25.328	−34.341	86.198	1.00	41.22		C
ATOM	4093	OD1	ASP	C	103	−25.539	−35.538	85.880	1.00	33.40		O1−
ATOM	4094	OD2	ASP	C	103	−25.333	−33.419	85.338	1.00	51.21		O
ATOM	4095	N	ILE	C	104	−26.213	−37.077	88.127	1.00	29.34		N
ATOM	4096	CA	ILE	C	104	−27.410	−37.884	88.337	1.00	28.45		C
ATOM	4097	C	ILE	C	104	−27.007	−39.332	88.536	1.00	30.33		C
ATOM	4098	O	ILE	C	104	−26.120	−39.840	87.842	1.00	31.30		O
ATOM	4099	CB	ILE	C	104	−28.406	−37.758	87.170	1.00	31.09		C
ATOM	4100	CG1	ILE	C	104	−28.861	−36.309	87.017	1.00	29.48		C
ATOM	4101	CG2	ILE	C	104	−29.583	−38.689	87.387	1.00	25.98		C
ATOM	4102	CD1	ILE	C	104	−29.838	−36.138	85.943	1.00	31.56		C
ATOM	4103	N	TRP	C	105	−27.666	−39.992	89.480	1.00	27.28		N
ATOM	4104	CA	TRP	C	105	−27.361	−41.357	89.855	1.00	27.66		C
ATOM	4105	C	TRP	C	105	−28.599	−42.236	89.754	1.00	29.36		C
ATOM	4106	O	TRP	C	105	−29.720	−41.789	90.005	1.00	31.41		O
ATOM	4107	CB	TRP	C	105	−26.830	−41.398	91.288	1.00	28.75		C
ATOM	4108	CG	TRP	C	105	−25.559	−40.624	91.483	1.00	27.49		C
ATOM	4109	CD1	TRP	C	105	−25.394	−39.267	91.400	1.00	27.23		C
ATOM	4110	CD2	TRP	C	105	−24.276	−41.167	91.802	1.00	25.31		C
ATOM	4111	NE1	TRP	C	105	−24.078	−38.935	91.650	1.00	25.97		N
ATOM	4112	CE2	TRP	C	105	−23.373	−40.083	91.900	1.00	25.23		C
ATOM	4113	CE3	TRP	C	105	−23.801	−42.466	92.016	1.00	25.04		C
ATOM	4114	CZ2	TRP	C	105	−22.026	−40.259	92.188	1.00	22.01		C
ATOM	4115	CZ3	TRP	C	105	−22.461	−42.639	92.307	1.00	27.62		C
ATOM	4116	CH2	TRP	C	105	−21.586	−41.532	92.389	1.00	24.95		C
ATOM	4117	N	GLY	C	106	−28.381	−43.504	89.436	1.00	29.88		N
ATOM	4118	CA	GLY	C	106	−29.424	−44.496	89.587	1.00	34.79		C
ATOM	4119	C	GLY	C	106	−29.697	−44.833	91.048	1.00	34.11		C
ATOM	4120	O	GLY	C	106	−28.952	−44.456	91.951	1.00	31.75		O
ATOM	4121	N	GLN	C	107	−30.828	−45.525	91.277	1.00	37.10		N
ATOM	4122	CA	GLN	C	107	−31.137	−46.052	92.607	1.00	33.95		C
ATOM	4123	C	GLN	C	107	−30.005	−46.904	93.124	1.00	30.12		C
ATOM	4124	O	GLN	C	107	−29.773	−46.956	94.331	1.00	31.44		O
ATOM	4125	CB	GLN	C	107	−32.411	−46.921	92.621	1.00	38.95		C
ATOM	4126	CG	GLN	C	107	−33.442	−46.732	91.485	1.00	53.38		C
ATOM	4127	CD	GLN	C	107	−33.137	−47.557	90.207	1.00	55.26		C
ATOM	4128	OE1	GLN	C	107	−33.665	−48.666	89.992	1.00	51.28		O
ATOM	4129	NE2	GLN	C	107	−32.299	−46.993	89.348	1.00	50.94		N
ATOM	4130	N	GLY	C	108	−29.311	−47.597	92.233	1.00	30.68		N
ATOM	4131	CA	GLY	C	108	−28.376	−48.619	92.628	1.00	25.20		C
ATOM	4132	C	GLY	C	108	−29.039	−49.981	92.689	1.00	28.53		C
ATOM	4133	O	GLY	C	108	−30.254	−50.110	92.792	1.00	32.61		O
ATOM	4134	N	THR	C	109	−28.203	−51.008	92.614	1.00	26.94		N
ATOM	4135	CA	THR	C	109	−28.607	−52.403	92.680	1.00	22.92		C
ATOM	4136	C	THR	C	109	−27.757	−53.086	93.740	1.00	30.47		C
ATOM	4137	O	THR	C	109	−26.523	−53.049	93.674	1.00	32.40		O
ATOM	4138	CB	THR	C	109	−28.418	−53.094	91.321	1.00	29.24		C
ATOM	4139	OG1	THR	C	109	−29.226	−52.453	90.327	1.00	29.50		O
ATOM	4140	CG2	THR	C	109	−28.754	−54.591	91.395	1.00	25.49		C
ATOM	4141	N	MET	C	110	−28.402	−53.685	94.726	1.00	30.19		N
ATOM	4142	CA	MET	C	110	−27.674	−54.400	95.765	1.00	31.87		C
ATOM	4143	C	MET	C	110	−27.271	−55.749	95.187	1.00	30.25		C
ATOM	4144	O	MET	C	110	−28.133	−56.548	94.818	1.00	31.68		O
ATOM	4145	CB	MET	C	110	−28.571	−54.546	96.991	1.00	38.09		C
ATOM	4146	CG	MET	C	110	−27.925	−54.739	98.362	1.00	38.26		C
ATOM	4147	SD	MET	C	110	−29.296	−54.935	99.598	1.00	60.00		S
ATOM	4148	CE	MET	C	110	−30.587	−53.829	98.963	1.00	28.36		C
ATOM	4149	N	VAL	C	111	−25.971	−55.986	95.049	1.00	30.68		N
ATOM	4150	CA	VAL	C	111	−25.467	−57.191	94.399	1.00	30.46		C
ATOM	4151	C	VAL	C	111	−24.685	−57.989	95.422	1.00	30.94		C
ATOM	4152	O	VAL	C	111	−23.698	−57.495	95.978	1.00	34.81		O
ATOM	4153	CB	VAL	C	111	−24.601	−56.875	93.164	1.00	34.32		C
ATOM	4154	CG1	VAL	C	111	−23.821	−58.100	92.745	1.00	28.86		C
ATOM	4155	CG2	VAL	C	111	−25.462	−56.397	91.995	1.00	24.78		C
ATOM	4156	N	THR	C	112	−25.136	−59.214	95.676	1.00	33.49		N
ATOM	4157	CA	THR	C	112	−24.495	−60.147	96.593	1.00	29.04		C
ATOM	4158	C	THR	C	112	−23.993	−61.341	95.798	1.00	31.99		C
ATOM	4159	O	THR	C	112	−24.749	−61.926	95.013	1.00	28.19		O
ATOM	4160	CB	THR	C	112	−25.483	−60.629	97.670	1.00	27.70		C
ATOM	4161	OG1	THR	C	112	−26.126	−59.513	98.275	1.00	27.51		O
ATOM	4162	CG2	THR	C	112	−24.800	−61.447	98.736	1.00	30.55		C
ATOM	4163	N	VAL	C	113	−22.726	−61.696	95.985	1.00	29.97		N
ATOM	4164	CA	VAL	C	113	−22.185	−62.918	95.405	1.00	36.12		C
ATOM	4165	C	VAL	C	113	−21.678	−63.780	96.550	1.00	33.41		C
ATOM	4166	O	VAL	C	113	−20.902	−63.312	97.392	1.00	31.40		O
ATOM	4167	CB	VAL	C	113	−21.119	−62.648	94.319	1.00	37.87		C
ATOM	4168	CG1	VAL	C	113	−20.582	−61.246	94.423	1.00	37.11		C
ATOM	4169	CG2	VAL	C	113	−20.016	−63.719	94.288	1.00	28.90		C
ATOM	4170	N	SER	C	114	−22.171	−65.019	96.610	1.00	33.34		N
ATOM	4171	CA	SER	C	114	−21.991	−65.863	97.781	1.00	37.36		C
ATOM	4172	C	SER	C	114	−22.309	−67.316	97.449	1.00	34.25		C
ATOM	4173	O	SER	C	114	−23.113	−67.606	96.563	1.00	32.33		O
ATOM	4174	CB	SER	C	114	−22.886	−65.382	98.932	1.00	34.37		C
ATOM	4175	OG	SER	C	114	−22.928	−66.326	99.983	1.00	36.36		O
ATOM	4176	N	SER	C	115	−21.682	−68.224	98.195	1.00	38.98		N
ATOM	4177	CA	SER	C	115	−22.065	−69.629	98.129	1.00	38.55		C
ATOM	4178	C	SER	C	115	−23.430	−69.890	98.753	1.00	44.22		C
ATOM	4179	O	SER	C	115	−24.069	−70.889	98.410	1.00	48.62		O
ATOM	4180	CB	SER	C	115	−21.032	−70.491	98.847	1.00	40.98		C
ATOM	4181	OG	SER	C	115	−19.794	−70.465	98.158	1.00	57.58		O
ATOM	4182	N	ALA	C	116	−23.912	−69.003	99.620	1.00	34.12		N
ATOM	4183	CA	ALA	C	116	−25.140	−69.269	100.348	1.00	37.60		C
ATOM	4184	C	ALA	C	116	−26.347	−69.330	99.415	1.00	39.26		C
ATOM	4185	O	ALA	C	116	−26.329	−68.827	98.282	1.00	36.17		O
ATOM	4186	CB	ALA	C	116	−25.366	−68.194	101.413	1.00	33.12		C
ATOM	4187	N	SER	C	117	−27.414	−69.957	99.915	1.00	36.37		N
ATOM	4188	CA	SER	C	117	−28.684	−70.042	99.206	1.00	39.66		C
ATOM	4189	C	SER	C	117	−29.745	−69.252	99.960	1.00	36.99		C
ATOM	4190	O	SER	C	117	−29.660	−69.069	101.179	1.00	40.67		O
ATOM	4191	CB	SER	C	117	−29.137	−71.504	99.021	1.00	40.84		C
ATOM	4192	OG	SER	C	117	−28.239	−72.218	98.172	1.00	42.49		O
ATOM	4193	N	THR	C	118	−30.735	−68.770	99.215	1.00	35.22		N
ATOM	4194	CA	THR	C	118	−31.796	−67.963	99.796	1.00	34.00		C
ATOM	4195	C	THR	C	118	−32.453	−68.705	100.953	1.00	37.86		C
ATOM	4196	O	THR	C	118	−32.680	−69.912	100.889	1.00	37.72		O
ATOM	4197	CB	THR	C	118	−32.829	−67.600	98.724	1.00	27.84		C
ATOM	4198	OG1	THR	C	118	−32.225	−66.729	97.771	1.00	31.08		O
ATOM	4199	CG2	THR	C	118	−34.051	−66.887	99.332	1.00	36.20		C
ATOM	4200	N	LYS	C	119	−32.740	−67.973	102.024	1.00	38.37		N
ATOM	4201	CA	LYS	C	119	−33.239	−68.569	103.256	1.00	37.26		C
ATOM	4202	C	LYS	C	119	−33.922	−67.486	104.079	1.00	34.75		C
ATOM	4203	O	LYS	C	119	−33.332	−66.432	104.331	1.00	32.89		O
ATOM	4204	CB	LYS	C	119	−32.093	−69.201	104.040	1.00	32.21		C
ATOM	4205	CG	LYS	C	119	−32.520	−69.868	105.295	1.00	32.82		C
ATOM	4206	CD	LYS	C	119	−31.299	−70.193	106.108	1.00	34.06		C
ATOM	4207	CE	LYS	C	119	−31.675	−70.872	107.411	1.00	37.24		C
ATOM	4208	NZ	LYS	C	119	−32.670	−70.086	108.181	1.00	41.53		N1+
ATOM	4209	N	GLY	C	120	−35.166	−67.738	104.474	1.00	34.46		N
ATOM	4210	CA	GLY	C	120	−35.906	−66.796	105.275	1.00	30.62		C
ATOM	4211	C	GLY	C	120	−35.395	−66.829	106.696	1.00	30.67		C
ATOM	4212	O	GLY	C	120	−34.703	−67.767	107.102	1.00	29.23		O
ATOM	4213	N	PRO	C	121	−35.705	−65.792	107.467	1.00	28.30		N
ATOM	4214	CA	PRO	C	121	−35.198	−65.683	108.838	1.00	30.58		C
ATOM	4215	C	PRO	C	121	−36.084	−66.380	109.863	1.00	30.35		C
ATOM	4216	O	PRO	C	121	−37.286	−66.554	109.668	1.00	31.40		O
ATOM	4217	CB	PRO	C	121	−35.223	−64.172	109.082	1.00	29.17		C
ATOM	4218	CG	PRO	C	121	−36.377	−63.701	108.245	1.00	27.47		C
ATOM	4219	CD	PRO	C	121	−36.411	−64.578	107.029	1.00	27.41		C
ATOM	4220	N	SER	C	122	−35.465	−66.726	110.991	1.00	27.52		N
ATOM	4221	CA	SER	C	122	−36.176	−67.066	112.219	1.00	26.31		C
ATOM	4222	C	SER	C	122	−36.157	−65.874	113.165	1.00	30.19		C
ATOM	4223	O	SER	C	122	−35.108	−65.263	113.389	1.00	33.03		O
ATOM	4224	CB	SER	C	122	−35.553	−68.272	112.920	1.00	33.10		C
ATOM	4225	OG	SER	C	122	−35.607	−69.425	112.115	1.00	42.58		O
ATOM	4226	N	VAL	C	123	−37.305	−65.555	113.736	1.00	30.40		N
ATOM	4227	CA	VAL	C	123	−37.439	−64.392	114.599	1.00	29.30		C
ATOM	4228	C	VAL	C	123	−37.651	−64.870	116.038	1.00	28.97		C
ATOM	4229	O	VAL	C	123	−38.681	−65.469	116.368	1.00	37.16		O
ATOM	4230	CB	VAL	C	123	−38.576	−63.481	114.123	1.00	27.97		C
ATOM	4231	CG1	VAL	C	123	−38.600	−62.206	114.971	1.00	29.32		C
ATOM	4232	CG2	VAL	C	123	−38.448	−63.196	112.593	1.00	23.94		C
ATOM	4233	N	PHE	C	124	−36.703	−64.598	116.890	1.00	27.59		N
ATOM	4234	CA	PHE	C	124	−36.791	−64.961	118.289	1.00	30.52		C
ATOM	4235	C	PHE	C	124	−36.968	−63.708	119.143	1.00	32.03		C
ATOM	4236	O	PHE	C	124	−36.508	−62.623	118.771	1.00	29.31		O
ATOM	4237	CB	PHE	C	124	−35.539	−65.723	118.760	1.00	34.19		C
ATOM	4238	CG	PHE	C	124	−35.145	−66.879	117.868	1.00	33.33		C
ATOM	4239	CD1	PHE	C	124	−35.968	−67.985	117.730	1.00	37.57		C
ATOM	4240	CD2	PHE	C	124	−33.956	−66.851	117.163	1.00	31.04		C
ATOM	4241	CE1	PHE	C	124	−35.618	−69.033	116.892	1.00	34.49		C
ATOM	4242	CE2	PHE	C	124	−33.596	−67.901	116.333	1.00	34.61		C
ATOM	4243	CZ	PHE	C	124	−34.430	−68.991	116.196	1.00	33.73		C
ATOM	4244	N	PRO	C	125	−37.636	−63.815	120.285	1.00	34.51		N
ATOM	4245	CA	PRO	C	125	−37.839	−62.633	121.124	1.00	30.32		C
ATOM	4246	C	PRO	C	125	−36.613	−62.280	121.951	1.00	32.51		C
ATOM	4247	O	PRO	C	125	−35.832	−63.136	122.369	1.00	36.65		O
ATOM	4248	CB	PRO	C	125	−39.010	−63.039	122.025	1.00	29.69		C
ATOM	4249	CG	PRO	C	125	−38.894	−64.526	122.107	1.00	32.87		C
ATOM	4250	CD	PRO	C	125	−38.363	−64.991	120.794	1.00	34.01		C
ATOM	4251	N	LEU	C	126	−36.434	−60.985	122.134	1.00	26.85		N
ATOM	4252	CA	LEU	C	126	−35.595	−60.422	123.175	1.00	26.86		C
ATOM	4253	C	LEU	C	126	−36.568	−59.902	124.234	1.00	31.33		C
ATOM	4254	O	LEU	C	126	−37.153	−58.825	124.081	1.00	27.81		O
ATOM	4255	CB	LEU	C	126	−34.714	−59.324	122.596	1.00	31.15		C
ATOM	4256	CG	LEU	C	126	−33.839	−59.786	121.435	1.00	29.11		C
ATOM	4257	CD1	LEU	C	126	−33.179	−58.601	120.808	1.00	26.98		C
ATOM	4258	CD2	LEU	C	126	−32.786	−60.749	121.950	1.00	28.83		C
ATOM	4259	N	ALA	C	127	−36.784	−60.706	125.302	1.00	34.13		N
ATOM	4260	CA	ALA	C	127	−37.874	−60.477	126.253	1.00	34.68		C
ATOM	4261	C	ALA	C	127	−37.515	−59.383	127.258	1.00	38.36		C
ATOM	4262	O	ALA	C	127	−36.400	−59.366	127.792	1.00	34.45		O
ATOM	4263	CB	ALA	C	127	−38.229	−61.756	126.999	1.00	34.71		C
ATOM	4264	N	PRO	C	128	−38.453	−58.480	127.552	1.00	43.79		N
ATOM	4265	CA	PRO	C	128	−38.163	−57.410	128.513	1.00	43.68		C
ATOM	4266	C	PRO	C	128	−37.732	−57.972	129.856	1.00	54.93		C
ATOM	4267	O	PRO	C	128	−38.285	−58.961	130.350	1.00	50.70		O
ATOM	4268	CB	PRO	C	128	−39.481	−56.625	128.600	1.00	40.46		C
ATOM	4269	CG	PRO	C	128	−40.513	−57.526	128.054	1.00	44.62		C
ATOM	4270	CD	PRO	C	128	−39.823	−58.379	127.020	1.00	37.96		C
ATOM	4271	N	SER	C	129	−36.668	−57.356	130.389	1.00	69.23		N
ATOM	4272	CA	SER	C	129	−36.026	−57.680	131.657	1.00	73.37		C
ATOM	4273	C	SER	C	129	−37.065	−57.798	132.767	1.00	80.23		C
ATOM	4274	O	SER	C	129	−37.700	−56.804	133.139	1.00	81.02		O
ATOM	4275	CB	SER	C	129	−34.983	−56.595	131.987	1.00	71.73		C
ATOM	4276	OG	SER	C	129	−34.000	−57.018	132.909	1.00	63.19		O
ATOM	4277	N	SER	C	130	−37.246	−59.018	133.289	1.00	83.03		N
ATOM	4278	CA	SER	C	130	−38.109	−59.226	134.446	1.00	85.79		C
ATOM	4279	C	SER	C	130	−37.714	−58.318	135.603	1.00	95.78		C
ATOM	4280	O	SER	C	130	−38.566	−57.941	136.424	1.00	93.56		O
ATOM	4281	CB	SER	C	130	−38.040	−60.696	134.882	1.00	88.42		C
ATOM	4282	OG	SER	C	130	−36.688	−61.134	135.021	1.00	84.37		O
ATOM	4283	N	LYS	C	131	−36.428	−57.953	135.673	1.00	96.01		N
ATOM	4284	CA	LYS	C	131	−35.860	−57.111	136.721	1.00	92.69		C
ATOM	4285	C	LYS	C	131	−35.737	−55.631	136.334	1.00	88.64		C
ATOM	4286	O	LYS	C	131	−34.824	−54.957	136.820	1.00	93.47		O
ATOM	4287	CB	LYS	C	131	−34.490	−57.660	137.135	1.00	85.98		C
ATOM	4288	CG	LYS	C	131	−34.512	−59.018	137.841	1.00	83.85		C
ATOM	4289	CD	LYS	C	131	−33.113	−59.398	138.328	1.00	86.44		C
ATOM	4290	CE	LYS	C	131	−33.162	−60.359	139.509	1.00	81.44		C
ATOM	4291	NZ	LYS	C	131	−31.802	−60.691	140.021	1.00	67.72		N1+
ATOM	4292	N	SER	C	132	−36.625	−55.088	135.498	1.00	91.44		N
ATOM	4293	CA	SER	C	132	−36.567	−53.651	135.224	1.00	88.79		C
ATOM	4294	C	SER	C	132	−36.967	−52.857	136.461	1.00	93.64		C
ATOM	4295	O	SER	C	132	−37.915	−53.218	137.168	1.00	97.31		O
ATOM	4296	CB	SER	C	132	−37.472	−53.256	134.048	1.00	75.72		C
ATOM	4297	OG	SER	C	132	−36.862	−53.513	132.797	1.00	71.83		O
ATOM	4298	N	THR	C	133	−36.229	−51.769	136.723	1.00	99.77		N
ATOM	4299	CA	THR	C	133	−36.569	−50.845	137.806	1.00	97.90		C
ATOM	4300	C	THR	C	133	−38.009	−50.364	137.611	1.00	93.15		C
ATOM	4301	O	THR	C	133	−38.291	−49.593	136.684	1.00	89.44		O
ATOM	4302	CB	THR	C	133	−35.563	−49.669	137.882	1.00	87.55		C
ATOM	4303	OG1	THR	C	133	−35.179	−49.234	136.565	1.00	83.45		O
ATOM	4304	CG2	THR	C	133	−34.303	−50.077	138.653	1.00	84.85		C
ATOM	4305	N	SER	C	134	−38.929	−50.829	138.466	1.00	93.26		N
ATOM	4306	CA	SER	C	134	−40.352	−50.635	138.210	1.00	87.74		C
ATOM	4307	C	SER	C	134	−40.679	−49.153	138.274	1.00	85.43		C
ATOM	4308	O	SER	C	134	−40.329	−48.472	139.242	1.00	87.73		O
ATOM	4309	CB	SER	C	134	−41.195	−51.410	139.224	1.00	74.42		C
ATOM	4310	OG	SER	C	134	−42.211	−52.150	138.567	1.00	81.41		O
ATOM	4311	N	GLY	C	135	−41.314	−48.643	137.223	1.00	80.04		N
ATOM	4312	CA	GLY	C	135	−41.395	−47.211	137.051	1.00	78.15		C
ATOM	4313	C	GLY	C	135	−40.279	−46.614	136.227	1.00	80.05		C
ATOM	4314	O	GLY	C	135	−40.186	−45.381	136.144	1.00	77.05		O
ATOM	4315	N	GLY	C	136	−39.414	−47.444	135.639	1.00	72.87		N
ATOM	4316	CA	GLY	C	136	−38.350	−46.962	134.783	1.00	61.44		C
ATOM	4317	C	GLY	C	136	−38.489	−47.391	133.333	1.00	56.58		C
ATOM	4318	O	GLY	C	136	−39.592	−47.407	132.771	1.00	51.45		O
ATOM	4319	N	THR	C	137	−37.382	−47.773	132.713	1.00	53.14		N
ATOM	4320	CA	THR	C	137	−37.361	−48.017	131.279	1.00	47.91		C
ATOM	4321	C	THR	C	137	−37.015	−49.473	131.008	1.00	48.48		C
ATOM	4322	O	THR	C	137	−36.090	−50.028	131.617	1.00	47.97		O
ATOM	4323	CB	THR	C	137	−36.370	−47.081	130.592	1.00	48.09		C
ATOM	4324	OG1	THR	C	137	−36.886	−45.745	130.650	1.00	54.06		O
ATOM	4325	CG2	THR	C	137	−36.140	−47.485	129.123	1.00	43.01		C
ATOM	4326	N	ALA	C	138	−37.781	−50.087	130.110	1.00	38.89		N
ATOM	4327	CA	ALA	C	138	−37.598	−51.469	129.714	1.00	38.16		C
ATOM	4328	C	ALA	C	138	−37.117	−51.516	128.268	1.00	36.59		C
ATOM	4329	O	ALA	C	138	−37.541	−50.708	127.437	1.00	36.87		O
ATOM	4330	CB	ALA	C	138	−38.908	−52.249	129.871	1.00	31.25		C
ATOM	4331	N	ALA	C	139	−36.232	−52.454	127.964	1.00	33.10		N
ATOM	4332	CA	ALA	C	139	−35.886	−52.755	126.582	1.00	30.90		C
ATOM	4333	C	ALA	C	139	−36.522	−54.080	126.199	1.00	30.77		C
ATOM	4334	O	ALA	C	139	−36.619	−54.986	127.028	1.00	31.77		O
ATOM	4335	CB	ALA	C	139	−34.371	−52.823	126.376	1.00	25.95		C
ATOM	4336	N	LEU	C	140	−36.978	−54.176	124.952	1.00	29.69		N
ATOM	4337	CA	LEU	C	140	−37.426	−55.439	124.376	1.00	30.12		C
ATOM	4338	C	LEU	C	140	−37.081	−55.420	122.891	1.00	30.17		C
ATOM	4339	O	LEU	C	140	−36.795	−54.369	122.319	1.00	29.86		O
ATOM	4340	CB	LEU	C	140	−38.930	−55.666	124.605	1.00	29.80		C
ATOM	4341	CG	LEU	C	140	−39.844	−54.591	124.028	1.00	30.15		C
ATOM	4342	CD1	LEU	C	140	−40.427	−55.049	122.720	1.00	29.13		C
ATOM	4343	CD2	LEU	C	140	−40.945	−54.256	125.007	1.00	30.43		C
ATOM	4344	N	GLY	C	141	−37.135	−56.581	122.250	1.00	27.97		N
ATOM	4345	CA	GLY	C	141	−36.809	−56.584	120.844	1.00	27.01		C
ATOM	4346	C	GLY	C	141	−37.043	−57.919	120.174	1.00	30.67		C
ATOM	4347	O	GLY	C	141	−37.628	−58.835	120.754	1.00	31.90		O
ATOM	4348	N	CYS	C	142	−36.604	−57.978	118.908	1.00	28.16		N
ATOM	4349	CA	CYS	C	142	−36.633	−59.156	118.051	1.00	31.74		C
ATOM	4350	C	CYS	C	142	−35.238	−59.467	117.527	1.00	28.43		C
ATOM	4351	O	CYS	C	142	−34.478	−58.563	117.193	1.00	24.09		O
ATOM	4352	CB	CYS	C	142	−37.563	−58.947	116.858	1.00	32.06		C
ATOM	4353	SG	CYS	C	142	−39.293	−59.136	117.287	1.00	49.90		S
ATOM	4354	N	LEU	C	143	−34.903	−60.747	117.447	1.00	28.84		N
ATOM	4355	CA	LEU	C	143	−33.651	−61.187	116.845	1.00	26.55		C
ATOM	4356	C	LEU	C	143	−33.989	−61.904	115.550	1.00	27.72		C
ATOM	4357	O	LEU	C	143	−34.719	−62.892	115.562	1.00	29.16		O
ATOM	4358	CB	LEU	C	143	−32.849	−62.069	117.805	1.00	29.85		C
ATOM	4359	CG	LEU	C	143	−31.504	−62.623	117.312	1.00	31.81		C
ATOM	4360	CD1	LEU	C	143	−30.634	−61.539	116.821	1.00	29.50		C
ATOM	4361	CD2	LEU	C	143	−30.809	−63.273	118.476	1.00	34.71		C
ATOM	4362	N	VAL	C	144	−33.506	−61.374	114.434	1.00	24.21		N
ATOM	4363	CA	VAL	C	144	−33.850	−61.888	113.121	1.00	25.88		C
ATOM	4364	C	VAL	C	144	−32.632	−62.683	112.650	1.00	31.73		C
ATOM	4365	O	VAL	C	144	−31.676	−62.122	112.104	1.00	27.35		O
ATOM	4366	CB	VAL	C	144	−34.237	−60.756	112.162	1.00	29.39		C
ATOM	4367	CG1	VAL	C	144	−34.620	−61.297	110.801	1.00	29.56		C
ATOM	4368	CG2	VAL	C	144	−35.395	−59.939	112.721	1.00	21.42		C
ATOM	4369	N	LYS	C	145	−32.658	−64.003	112.849	1.00	26.44		N
ATOM	4370	CA	LYS	C	145	−31.455	−64.811	112.726	1.00	29.06		C
ATOM	4371	C	LYS	C	145	−31.472	−65.687	111.476	1.00	30.53		C
ATOM	4372	O	LYS	C	145	−32.513	−66.244	111.098	1.00	29.40		O
ATOM	4373	CB	LYS	C	145	−31.253	−65.686	113.974	1.00	29.44		C
ATOM	4374	CG	LYS	C	145	−29.832	−66.217	114.070	1.00	30.84		C
ATOM	4375	CD	LYS	C	145	−29.511	−66.818	115.405	1.00	37.83		C
ATOM	4376	CE	LYS	C	145	−28.009	−67.086	115.543	1.00	43.25		C
ATOM	4377	NZ	LYS	C	145	−27.433	−67.955	114.471	1.00	39.52		N1+
ATOM	4378	N	ASP	C	146	−30.298	−65.782	110.837	1.00	28.14		N
ATOM	4379	CA	ASP	C	146	−30.003	−66.758	109.784	1.00	33.06		C
ATOM	4380	C	ASP	C	146	−30.862	−66.564	108.531	1.00	33.58		C
ATOM	4381	O	ASP	C	146	−31.584	−67.465	108.102	1.00	36.23		O
ATOM	4382	CB	ASP	C	146	−30.185	−68.177	110.330	1.00	36.19		C
ATOM	4383	CG	ASP	C	146	−29.226	−68.502	111.441	1.00	38.83		C
ATOM	4384	OD1	ASP	C	146	−28.041	−68.058	111.404	1.00	37.01		O
ATOM	4385	OD2	ASP	C	146	−29.716	−69.135	112.405	1.00	41.05		O1−
ATOM	4386	N	TYR	C	147	−30.735	−65.405	107.905	1.00	29.04		N
ATOM	4387	CA	TYR	C	147	−31.400	−65.202	106.626	1.00	29.40		C
ATOM	4388	C	TYR	C	147	−30.361	−64.899	105.547	1.00	29.62		C
ATOM	4389	O	TYR	C	147	−29.186	−64.645	105.826	1.00	30.41		O
ATOM	4390	CB	TYR	C	147	−32.443	−64.080	106.711	1.00	26.97		C
ATOM	4391	CG	TYR	C	147	−31.863	−62.715	106.999	1.00	28.14		C
ATOM	4392	CD1	TYR	C	147	−31.628	−62.304	108.303	1.00	28.44		C
ATOM	4393	CD2	TYR	C	147	−31.529	−61.840	105.963	1.00	29.70		C
ATOM	4394	CE1	TYR	C	147	−31.098	−61.071	108.575	1.00	30.16		C
ATOM	4395	CE2	TYR	C	147	−30.994	−60.586	106.226	1.00	29.35		C
ATOM	4396	CZ	TYR	C	147	−30.788	−60.204	107.538	1.00	32.07		C
ATOM	4397	OH	TYR	C	147	−30.269	−58.954	107.832	1.00	32.73		O
ATOM	4398	N	PHE	C	148	−30.808	−64.941	104.298	1.00	31.56		N
ATOM	4399	CA	PHE	C	148	−29.950	−64.658	103.161	1.00	31.89		C
ATOM	4400	C	PHE	C	148	−30.781	−64.535	101.900	1.00	31.76		C
ATOM	4401	O	PHE	C	148	−31.634	−65.367	101.661	1.00	30.72		O
ATOM	4402	CB	PHE	C	148	−28.910	−65.765	102.977	1.00	30.49		C
ATOM	4403	CG	PHE	C	148	−27.980	−65.524	101.839	1.00	32.65		C
ATOM	4404	CD1	PHE	C	148	−28.316	−65.923	100.550	1.00	30.37		C
ATOM	4405	CD2	PHE	C	148	−26.766	−64.876	102.053	1.00	31.85		C
ATOM	4406	CE1	PHE	C	148	−27.460	−65.681	99.502	1.00	33.92		C
ATOM	4407	CE2	PHE	C	148	−25.903	−64.629	101.010	1.00	31.05		C
ATOM	4408	CZ	PHE	C	148	−26.244	−65.032	99.734	1.00	36.04		C
ATOM	4409	N	PRO	C	149	−30.503	−63.514	101.066	1.00	37.13		N
ATOM	4410	CA	PRO	C	149	−29.514	−62.453	101.301	1.00	34.36		C
ATOM	4411	C	PRO	C	149	−30.136	−61.270	102.025	1.00	31.13		C
ATOM	4412	O	PRO	C	149	−31.294	−61.362	102.414	1.00	33.18		O
ATOM	4413	CB	PRO	C	149	−29.116	−62.050	99.885	1.00	28.91		C
ATOM	4414	CG	PRO	C	149	−30.384	−62.167	99.146	1.00	26.99		C
ATOM	4415	CD	PRO	C	149	−31.093	−63.390	99.717	1.00	27.60		C
ATOM	4416	N	GLU	C	150	−29.394	−60.176	102.157	1.00	27.31		N
ATOM	4417	CA	GLU	C	150	−29.961	−58.888	102.552	1.00	30.44		C
ATOM	4418	C	GLU	C	150	−30.938	−58.398	101.479	1.00	29.76		C
ATOM	4419	O	GLU	C	150	−30.806	−58.770	100.312	1.00	30.40		O
ATOM	4420	CB	GLU	C	150	−28.839	−57.872	102.761	1.00	29.87		C
ATOM	4421	CG	GLU	C	150	−27.928	−58.160	103.958	1.00	29.34		C
ATOM	4422	CD	GLU	C	150	−28.365	−57.400	105.210	1.00	38.78		C
ATOM	4423	OE1	GLU	C	150	−27.573	−56.543	105.699	1.00	37.11		O
ATOM	4424	OE2	GLU	C	150	−29.512	−57.629	105.680	1.00	39.42		O1−
ATOM	4425	N	PRO	C	151	−31.930	−57.571	101.855	1.00	28.20		N
ATOM	4426	CA	PRO	C	151	−32.224	−57.019	103.180	1.00	28.76		C
ATOM	4427	C	PRO	C	151	−33.460	−57.594	103.883	1.00	32.34		C
ATOM	4428	O	PRO	C	151	−34.284	−58.288	103.291	1.00	27.74		O
ATOM	4429	CB	PRO	C	151	−32.488	−55.554	102.867	1.00	21.65		C
ATOM	4430	CG	PRO	C	151	−33.145	−55.605	101.554	1.00	15.86		C
ATOM	4431	CD	PRO	C	151	−32.640	−56.807	100.810	1.00	20.18		C
ATOM	4432	N	VAL	C	152	−33.572	−57.269	105.165	1.00	31.09		N
ATOM	4433	CA	VAL	C	152	−34.798	−57.431	105.925	1.00	31.79		C
ATOM	4434	C	VAL	C	152	−35.215	−56.053	106.399	1.00	32.70		C
ATOM	4435	O	VAL	C	152	−34.378	−55.174	106.625	1.00	38.99		O
ATOM	4436	CB	VAL	C	152	−34.616	−58.366	107.130	1.00	32.39		C
ATOM	4437	CG1	VAL	C	152	−34.480	−59.798	106.688	1.00	34.75		C
ATOM	4438	CG2	VAL	C	152	−33.386	−57.962	107.854	1.00	32.91		C
ATOM	4439	N	THR	C	153	−36.513	−55.863	106.552	1.00	30.59		N
ATOM	4440	CA	THR	C	153	−37.032	−54.660	107.178	1.00	33.61		C
ATOM	4441	C	THR	C	153	−37.799	−55.060	108.426	1.00	32.20		C
ATOM	4442	O	THR	C	153	−38.455	−56.108	108.450	1.00	30.80		O
ATOM	4443	CB	THR	C	153	−37.918	−53.848	106.212	1.00	32.33		C
ATOM	4444	OG1	THR	C	153	−38.950	−54.679	105.683	1.00	37.08		O
ATOM	4445	CG2	THR	C	153	−37.089	−53.315	105.061	1.00	33.42		C
ATOM	4446	N	VAL	C	154	−37.709	−54.221	109.459	1.00	27.86		N
ATOM	4447	CA	VAL	C	154	−38.401	−54.438	110.727	1.00	29.82		C
ATOM	4448	C	VAL	C	154	−39.162	−53.168	111.090	1.00	26.12		C
ATOM	4449	O	VAL	C	154	−38.574	−52.085	111.121	1.00	30.95		O
ATOM	4450	CB	VAL	C	154	−37.414	−54.808	111.861	1.00	29.46		C
ATOM	4451	CG1	VAL	C	154	−38.155	−55.064	113.142	1.00	29.26		C
ATOM	4452	CG2	VAL	C	154	−36.547	−56.023	111.485	1.00	24.20		C
ATOM	4453	N	SER	C	155	−40.459	−53.293	111.373	1.00	28.07		N
ATOM	4454	CA	SER	C	155	−41.207	−52.221	112.033	1.00	29.61		C
ATOM	4455	C	SER	C	155	−41.832	−52.750	113.315	1.00	35.01		C
ATOM	4456	O	SER	C	155	−41.790	−53.949	113.616	1.00	36.17		O
ATOM	4457	CB	SER	C	155	−42.310	−51.632	111.151	1.00	25.87		C
ATOM	4458	OG	SER	C	155	−43.302	−52.591	110.859	1.00	28.75		O
ATOM	4459	N	TRP	C	156	−42.424	−51.846	114.080	1.00	29.64		N
ATOM	4460	CA	TRP	C	156	−43.029	−52.229	115.344	1.00	33.60		C
ATOM	4461	C	TRP	C	156	−44.490	−51.793	115.369	1.00	34.15		C
ATOM	4462	O	TRP	C	156	−44.813	−50.652	115.017	1.00	33.36		O
ATOM	4463	CB	TRP	C	156	−42.226	−51.655	116.514	1.00	31.35		C
ATOM	4464	CG	TRP	C	156	−40.969	−52.463	116.781	1.00	31.98		C
ATOM	4465	CD1	TRP	C	156	−39.734	−52.302	116.196	1.00	33.14		C
ATOM	4466	CD2	TRP	C	156	−40.836	−53.564	117.686	1.00	30.45		C
ATOM	4467	NE1	TRP	C	156	−38.849	−53.230	116.690	1.00	25.96		N
ATOM	4468	CE2	TRP	C	156	−39.498	−54.008	117.616	1.00	30.62		C
ATOM	4469	CE3	TRP	C	156	−41.717	−54.213	118.566	1.00	32.88		C
ATOM	4470	CZ2	TRP	C	156	−39.025	−55.076	118.391	1.00	31.18		C
ATOM	4471	CZ3	TRP	C	156	−41.243	−55.274	119.341	1.00	27.61		C
ATOM	4472	CH2	TRP	C	156	−39.914	−55.694	119.242	1.00	30.88		C
ATOM	4473	N	ASN	C	157	−45.370	−52.719	115.757	1.00	34.57		N
ATOM	4474	CA	ASN	C	157	−46.805	−52.459	115.826	1.00	28.72		C
ATOM	4475	C	ASN	C	157	−47.299	−51.895	114.495	1.00	36.26		C
ATOM	4476	O	ASN	C	157	−47.997	−50.880	114.432	1.00	35.07		O
ATOM	4477	CB	ASN	C	157	−47.133	−51.515	116.989	1.00	31.99		C
ATOM	4478	CG	ASN	C	157	−46.897	−52.156	118.368	1.00	33.31		C
ATOM	4479	OD1	ASN	C	157	−46.496	−53.318	118.479	1.00	34.80		O
ATOM	4480	ND2	ASN	C	157	−47.136	−51.387	119.418	1.00	32.04		N
ATOM	4481	N	SER	C	158	−46.870	−52.540	113.410	1.00	39.26		N
ATOM	4482	CA	SER	C	158	−47.310	−52.190	112.062	1.00	36.22		C
ATOM	4483	C	SER	C	158	−46.991	−50.739	111.719	1.00	35.47		C
ATOM	4484	O	SER	C	158	−47.673	−50.119	110.908	1.00	39.31		O
ATOM	4485	CB	SER	C	158	−48.807	−52.459	111.895	1.00	33.86		C
ATOM	4486	OG	SER	C	158	−49.145	−53.743	112.399	1.00	43.34		O
ATOM	4487	N	GLY	C	159	−45.938	−50.192	112.306	1.00	35.45		N
ATOM	4488	CA	GLY	C	159	−45.566	−48.813	112.078	1.00	33.17		C
ATOM	4489	C	GLY	C	159	−46.053	−47.833	113.124	1.00	36.82		C
ATOM	4490	O	GLY	C	159	−45.608	−46.684	113.114	1.00	41.61		O
ATOM	4491	N	ALA	C	160	−46.919	−48.260	114.048	1.00	38.45		N
ATOM	4492	CA	ALA	C	160	−47.469	−47.347	115.047	1.00	32.99		C
ATOM	4493	C	ALA	C	160	−46.449	−46.967	116.108	1.00	41.51		C
ATOM	4494	O	ALA	C	160	−46.566	−45.903	116.718	1.00	49.03		O
ATOM	4495	CB	ALA	C	160	−48.695	−47.977	115.719	1.00	29.64		C
ATOM	4496	N	LEU	C	161	−45.463	−47.818	116.362	1.00	40.25		N
ATOM	4497	CA	LEU	C	161	−44.450	−47.562	117.372	1.00	30.64		C
ATOM	4498	C	LEU	C	161	−43.161	−47.174	116.659	1.00	33.32		C
ATOM	4499	O	LEU	C	161	−42.702	−47.877	115.757	1.00	31.89		O
ATOM	4500	CB	LEU	C	161	−44.269	−48.786	118.270	1.00	31.29		C
ATOM	4501	CG	LEU	C	161	−43.229	−48.759	119.395	1.00	38.45		C
ATOM	4502	CD1	LEU	C	161	−43.249	−47.451	120.164	1.00	23.88		C
ATOM	4503	CD2	LEU	C	161	−43.494	−49.922	120.328	1.00	32.82		C
ATOM	4504	N	THR	C	162	−42.606	−46.032	117.032	1.00	37.42		N
ATOM	4505	CA	THR	C	162	−41.535	−45.418	116.262	1.00	33.06		C
ATOM	4506	C	THR	C	162	−40.497	−44.859	117.219	1.00	29.92		C
ATOM	4507	O	THR	C	162	−39.296	−45.096	117.071	1.00	28.52		O
ATOM	4508	CB	THR	C	162	−42.139	−44.328	115.362	1.00	36.32		C
ATOM	4509	OG1	THR	C	162	−42.104	−44.761	113.998	1.00	34.07		O
ATOM	4510	CG2	THR	C	162	−41.443	−42.968	115.527	1.00	36.07		C
ATOM	4511	N	SER	C	163	−40.981	−44.153	118.234	1.00	30.45		N
ATOM	4512	CA	SER	C	163	−40.121	−43.634	119.272	1.00	26.52		C
ATOM	4513	C	SER	C	163	−39.452	−44.780	120.014	1.00	30.83		C
ATOM	4514	O	SER	C	163	−40.117	−45.724	120.461	1.00	32.58		O
ATOM	4515	CB	SER	C	163	−40.954	−42.786	120.226	1.00	28.23		C
ATOM	4516	OG	SER	C	163	−40.230	−42.404	121.384	1.00	40.32		O
ATOM	4517	N	GLY	C	164	−38.137	−44.673	120.178	1.00	30.58		N
ATOM	4518	CA	GLY	C	164	−37.364	−45.625	120.941	1.00	29.23		C
ATOM	4519	C	GLY	C	164	−36.839	−46.804	120.153	1.00	31.45		C
ATOM	4520	O	GLY	C	164	−36.059	−47.589	120.704	1.00	33.69		O
ATOM	4521	N	VAL	C	165	−37.207	−46.930	118.878	1.00	27.51		N
ATOM	4522	CA	VAL	C	165	−36.793	−48.069	118.070	1.00	28.93		C
ATOM	4523	C	VAL	C	165	−35.357	−47.887	117.587	1.00	28.12		C
ATOM	4524	O	VAL	C	165	−34.979	−46.831	117.081	1.00	37.17		O
ATOM	4525	CB	VAL	C	165	−37.748	−48.269	116.884	1.00	26.69		C
ATOM	4526	CG1	VAL	C	165	−37.278	−49.432	116.023	1.00	24.04		C
ATOM	4527	CG2	VAL	C	165	−39.163	−48.502	117.367	1.00	24.09		C
ATOM	4528	N	HIS	C	166	−34.566	−48.942	117.693	1.00	30.28		N
ATOM	4529	CA	HIS	C	166	−33.290	−49.052	116.999	1.00	27.00		C
ATOM	4530	C	HIS	C	166	−33.270	−50.379	116.259	1.00	23.79		C
ATOM	4531	O	HIS	C	166	−33.286	−51.436	116.895	1.00	25.39		O
ATOM	4532	CB	HIS	C	166	−32.105	−49.007	117.975	1.00	27.83		C
ATOM	4533	CG	HIS	C	166	−32.009	−47.759	118.809	1.00	31.08		C
ATOM	4534	ND1	HIS	C	166	−31.757	−46.516	118.271	1.00	32.94		N
ATOM	4535	CD2	HIS	C	166	−32.070	−47.578	120.153	1.00	30.56		C
ATOM	4536	CE1	HIS	C	166	−31.681	−45.622	119.242	1.00	30.93		C
ATOM	4537	NE2	HIS	C	166	−31.861	−46.242	120.395	1.00	27.04		N
ATOM	4538	N	THR	C	167	−33.209	−50.338	114.928	1.00	24.71		N
ATOM	4539	CA	THR	C	167	−32.896	−51.526	114.139	1.00	22.25		C
ATOM	4540	C	THR	C	167	−31.455	−51.439	113.637	1.00	24.53		C
ATOM	4541	O	THR	C	167	−31.093	−50.498	112.927	1.00	26.79		O
ATOM	4542	CB	THR	C	167	−33.857	−51.694	112.980	1.00	20.41		C
ATOM	4543	OG1	THR	C	167	−35.176	−51.829	113.501	1.00	28.97		O
ATOM	4544	CG2	THR	C	167	−33.529	−52.967	112.219	1.00	21.90		C
ATOM	4545	N	PHE	C	168	−30.658	−52.417	113.986	1.00	25.58		N
ATOM	4546	CA	PHE	C	168	−29.210	−52.471	113.865	1.00	26.05		C
ATOM	4547	C	PHE	C	168	−28.807	−53.018	112.505	1.00	21.09		C
ATOM	4548	O	PHE	C	168	−29.560	−53.760	111.890	1.00	25.00		O
ATOM	4549	CB	PHE	C	168	−28.623	−53.352	114.969	1.00	23.55		C
ATOM	4550	CG	PHE	C	168	−28.681	−52.722	116.316	1.00	22.06		C
ATOM	4551	CD1	PHE	C	168	−29.812	−52.855	117.113	1.00	23.76		C
ATOM	4552	CD2	PHE	C	168	−27.617	−51.958	116.788	1.00	24.14		C
ATOM	4553	CE1	PHE	C	168	−29.892	−52.232	118.390	1.00	24.66		C
ATOM	4554	CE2	PHE	C	168	−27.683	−51.341	118.064	1.00	28.11		C
ATOM	4555	CZ	PHE	C	168	−28.828	−51.482	118.866	1.00	22.06		C
ATOM	4556	N	PRO	C	169	−27.626	−52.662	112.009	1.00	26.60		N
ATOM	4557	CA	PRO	C	169	−27.121	−53.295	110.778	1.00	25.79		C
ATOM	4558	C	PRO	C	169	−26.907	−54.793	110.988	1.00	26.33		C
ATOM	4559	O	PRO	C	169	−26.457	−55.228	112.050	1.00	23.48		O
ATOM	4560	CB	PRO	C	169	−25.790	−52.569	110.525	1.00	17.06		C
ATOM	4561	CG	PRO	C	169	−25.829	−51.348	111.350	1.00	17.09		C
ATOM	4562	CD	PRO	C	169	−26.686	−51.660	112.546	1.00	22.12		C
ATOM	4563	N	ALA	C	170	−27.222	−55.586	109.966	1.00	23.48		N
ATOM	4564	CA	ALA	C	170	−27.009	−57.027	110.064	1.00	26.56		C
ATOM	4565	C	ALA	C	170	−25.523	−57.369	110.178	1.00	25.54		C
ATOM	4566	O	ALA	C	170	−24.650	−56.604	109.782	1.00	26.69		O
ATOM	4567	CB	ALA	C	170	−27.591	−57.744	108.847	1.00	29.48		C
ATOM	4568	N	VAL	C	171	−25.237	−58.531	110.747	1.00	26.07		N
ATOM	4569	CA	VAL	C	171	−23.899	−59.104	110.683	1.00	24.19		C
ATOM	4570	C	VAL	C	171	−23.934	−60.333	109.789	1.00	26.45		C
ATOM	4571	O	VAL	C	171	−24.935	−61.047	109.711	1.00	31.14		O
ATOM	4572	CB	VAL	C	171	−23.315	−59.455	112.072	1.00	29.65		C
ATOM	4573	CG1	VAL	C	171	−23.042	−58.193	112.858	1.00	27.11		C
ATOM	4574	CG2	VAL	C	171	−24.254	−60.404	112.853	1.00	25.85		C
ATOM	4575	N	LEU	C	172	−22.832	−60.571	109.101	1.00	31.64		N
ATOM	4576	CA	LEU	C	172	−22.658	−61.767	108.288	1.00	28.57		C
ATOM	4577	C	LEU	C	172	−21.868	−62.750	109.143	1.00	26.67		C
ATOM	4578	O	LEU	C	172	−20.718	−62.492	109.489	1.00	30.87		O
ATOM	4579	CB	LEU	C	172	−21.937	−61.442	106.982	1.00	27.30		C
ATOM	4580	CG	LEU	C	172	−21.662	−62.583	105.992	1.00	32.63		C
ATOM	4581	CD1	LEU	C	172	−22.971	−63.245	105.549	1.00	26.83		C
ATOM	4582	CD2	LEU	C	172	−20.839	−62.101	104.772	1.00	28.21		C
ATOM	4583	N	GLN	C	173	−22.503	−63.845	109.522	1.00	27.90		N
ATOM	4584	CA	GLN	C	173	−21.916	−64.862	110.372	1.00	32.35		C
ATOM	4585	C	GLN	C	173	−21.087	−65.824	109.528	1.00	36.44		C
ATOM	4586	O	GLN	C	173	−21.204	−65.870	108.294	1.00	34.30		O
ATOM	4587	CB	GLN	C	173	−23.010	−65.632	111.111	1.00	33.56		C
ATOM	4588	CG	GLN	C	173	−23.996	−64.769	111.851	1.00	29.57		C
ATOM	4589	CD	GLN	C	173	−25.319	−65.478	112.079	1.00	34.07		C
ATOM	4590	OE1	GLN	C	173	−25.724	−65.696	113.215	1.00	34.19		O
ATOM	4591	NE2	GLN	C	173	−26.002	−65.836	110.991	1.00	32.53		N
ATOM	4592	N	SER	C	174	−20.254	−66.622	110.208	1.00	36.04		N
ATOM	4593	CA	SER	C	174	−19.363	−67.525	109.481	1.00	33.82		C
ATOM	4594	C	SER	C	174	−20.138	−68.509	108.622	1.00	32.65		C
ATOM	4595	O	SER	C	174	−19.561	−69.087	107.697	1.00	35.26		O
ATOM	4596	CB	SER	C	174	−18.437	−68.272	110.441	1.00	31.17		C
ATOM	4597	OG	SER	C	174	−18.868	−68.133	111.788	1.00	51.22		O
ATOM	4598	N	SER	C	175	−21.438	−68.678	108.879	1.00	30.00		N
ATOM	4599	CA	SER	C	175	−22.267	−69.541	108.055	1.00	23.99		C
ATOM	4600	C	SER	C	175	−22.566	−68.950	106.691	1.00	33.95		C
ATOM	4601	O	SER	C	175	−23.018	−69.689	105.810	1.00	36.33		O
ATOM	4602	CB	SER	C	175	−23.588	−69.851	108.767	1.00	31.25		C
ATOM	4603	OG	SER	C	175	−24.482	−68.743	108.809	1.00	33.60		O
ATOM	4604	N	GLY	C	176	−22.299	−67.659	106.473	1.00	34.11		N
ATOM	4605	CA	GLY	C	176	−22.780	−67.006	105.275	1.00	26.57		C
ATOM	4606	C	GLY	C	176	−24.191	−66.479	105.380	1.00	33.77		C
ATOM	4607	O	GLY	C	176	−24.690	−65.897	104.409	1.00	34.08		O
ATOM	4608	N	LEU	C	177	−24.857	−66.682	106.515	1.00	32.19		N
ATOM	4609	CA	LEU	C	177	−26.185	−66.145	106.765	1.00	30.75		C
ATOM	4610	C	LEU	C	177	−26.072	−64.870	107.584	1.00	33.31		C
ATOM	4611	O	LEU	C	177	−25.122	−64.683	108.347	1.00	33.18		O
ATOM	4612	CB	LEU	C	177	−27.062	−67.141	107.512	1.00	35.99		C
ATOM	4613	CG	LEU	C	177	−27.316	−68.487	106.843	1.00	34.64		C
ATOM	4614	CD1	LEU	C	177	−28.208	−69.291	107.732	1.00	30.71		C
ATOM	4615	CD2	LEU	C	177	−27.932	−68.291	105.469	1.00	29.23		C
ATOM	4616	N	TYR	C	178	−27.048	−63.992	107.413	1.00	32.29		N
ATOM	4617	CA	TYR	C	178	−27.076	−62.736	108.138	1.00	29.56		C
ATOM	4618	C	TYR	C	178	−27.923	−62.834	109.408	1.00	32.53		C
ATOM	4619	O	TYR	C	178	−28.819	−63.665	109.535	1.00	33.61		O
ATOM	4620	CB	TYR	C	178	−27.616	−61.627	107.249	1.00	26.03		C
ATOM	4621	CG	TYR	C	178	−26.708	−61.260	106.096	1.00	32.82		C
ATOM	4622	CD1	TYR	C	178	−25.696	−60.309	106.248	1.00	25.25		C
ATOM	4623	CD2	TYR	C	178	−26.874	−61.855	104.843	1.00	28.59		C
ATOM	4624	CE1	TYR	C	178	−24.890	−59.978	105.188	1.00	27.51		C
ATOM	4625	CE2	TYR	C	178	−26.075	−61.526	103.785	1.00	25.14		C
ATOM	4626	CZ	TYR	C	178	−25.085	−60.589	103.952	1.00	33.10		C
ATOM	4627	OH	TYR	C	178	−24.299	−60.260	102.873	1.00	31.54		O
ATOM	4628	N	SER	C	179	−27.674	−61.906	110.316	1.00	30.12		N
ATOM	4629	CA	SER	C	179	−28.377	−61.836	111.580	1.00	26.37		C
ATOM	4630	C	SER	C	179	−28.484	−60.373	111.974	1.00	28.91		C
ATOM	4631	O	SER	C	179	−27.473	−59.669	112.014	1.00	33.49		O
ATOM	4632	CB	SER	C	179	−27.616	−62.615	112.653	1.00	31.79		C
ATOM	4633	OG	SER	C	179	−28.434	−63.550	113.310	1.00	36.87		O
ATOM	4634	N	LEU	C	180	−29.693	−59.908	112.244	1.00	24.41		N
ATOM	4635	CA	LEU	C	180	−29.847	−58.581	112.796	1.00	26.13		C
ATOM	4636	C	LEU	C	180	−30.787	−58.623	113.991	1.00	33.77		C
ATOM	4637	O	LEU	C	180	−31.507	−59.597	114.238	1.00	33.18		O
ATOM	4638	CB	LEU	C	180	−30.340	−57.570	111.757	1.00	32.63		C
ATOM	4639	CG	LEU	C	180	−31.742	−57.362	111.177	1.00	31.41		C
ATOM	4640	CD1	LEU	C	180	−32.886	−57.085	112.196	1.00	23.59		C
ATOM	4641	CD2	LEU	C	180	−31.574	−56.181	110.212	1.00	23.09		C
ATOM	4642	N	SER	C	181	−30.773	−57.531	114.735	1.00	33.23		N
ATOM	4643	CA	SER	C	181	−31.662	−57.356	115.859	1.00	28.03		C
ATOM	4644	C	SER	C	181	−32.311	−55.982	115.766	1.00	26.07		C
ATOM	4645	O	SER	C	181	−31.777	−55.063	115.154	1.00	28.63		O
ATOM	4646	CB	SER	C	181	−30.906	−57.540	117.184	1.00	30.44		C
ATOM	4647	OG	SER	C	181	−29.984	−56.493	117.391	1.00	31.22		O
ATOM	4648	N	SER	C	182	−33.506	−55.881	116.326	1.00	27.13		N
ATOM	4649	CA	SER	C	182	−34.271	−54.649	116.409	1.00	27.94		C
ATOM	4650	C	SER	C	182	−34.805	−54.551	117.827	1.00	28.64		C
ATOM	4651	O	SER	C	182	−35.302	−55.543	118.363	1.00	26.17		O
ATOM	4652	CB	SER	C	182	−35.424	−54.637	115.408	1.00	25.46		C
ATOM	4653	OG	SER	C	182	−36.221	−53.487	115.599	1.00	27.32		O
ATOM	4654	N	VAL	C	183	−34.683	−53.373	118.446	1.00	27.27		N
ATOM	4655	CA	VAL	C	183	−35.089	−53.201	119.837	1.00	30.94		C
ATOM	4656	C	VAL	C	183	−35.878	−51.909	120.005	1.00	30.82		C
ATOM	4657	O	VAL	C	183	−35.875	−51.032	119.142	1.00	33.72		O
ATOM	4658	CB	VAL	C	183	−33.886	−53.209	120.800	1.00	27.96		C
ATOM	4659	CG1	VAL	C	183	−33.091	−54.486	120.621	1.00	17.87		C
ATOM	4660	CG2	VAL	C	183	−33.031	−51.953	120.585	1.00	29.36		C
ATOM	4661	N	VAL	C	184	−36.585	−51.813	121.122	1.00	25.36		N
ATOM	4662	CA	VAL	C	184	−37.315	−50.601	121.452	1.00	29.08		C
ATOM	4663	C	VAL	C	184	−37.320	−50.459	122.968	1.00	33.22		C
ATOM	4664	O	VAL	C	184	−37.476	−51.444	123.700	1.00	34.38		O
ATOM	4665	CB	VAL	C	184	−38.734	−50.602	120.812	1.00	30.67		C
ATOM	4666	CG1	VAL	C	184	−39.523	−51.866	121.135	1.00	28.94		C
ATOM	4667	CG2	VAL	C	184	−39.531	−49.352	121.221	1.00	30.72		C
ATOM	4668	N	THR	C	185	−37.102	−49.234	123.440	1.00	31.38		N
ATOM	4669	CA	THR	C	185	−37.213	−48.922	124.854	1.00	29.00		C
ATOM	4670	C	THR	C	185	−38.591	−48.319	125.074	1.00	30.90		C
ATOM	4671	O	THR	C	185	−39.048	−47.490	124.284	1.00	37.29		O
ATOM	4672	CB	THR	C	185	−36.102	−47.977	125.330	1.00	24.92		C
ATOM	4673	OG1	THR	C	185	−35.966	−46.874	124.424	1.00	32.54		O
ATOM	4674	CG2	THR	C	185	−34.779	−48.706	125.402	1.00	26.78		C
ATOM	4675	N	VAL	C	186	−39.273	−48.800	126.103	1.00	29.32		N
ATOM	4676	CA	VAL	C	186	−40.625	−48.377	126.458	1.00	34.69		C
ATOM	4677	C	VAL	C	186	−40.698	−48.292	127.970	1.00	36.57		C
ATOM	4678	O	VAL	C	186	−39.835	−48.836	128.675	1.00	34.20		O
ATOM	4679	CB	VAL	C	186	−41.699	−49.358	125.944	1.00	36.77		C
ATOM	4680	CG1	VAL	C	186	−41.645	−49.516	124.421	1.00	27.93		C
ATOM	4681	CG2	VAL	C	186	−41.571	−50.715	126.679	1.00	32.35		C
ATOM	4682	N	PRO	C	187	−41.717	−47.608	128.499	1.00	38.80		N
ATOM	4683	CA	PRO	C	187	−41.851	−47.521	129.958	1.00	40.40		C
ATOM	4684	C	PRO	C	187	−42.128	−48.886	130.574	1.00	43.67		C
ATOM	4685	O	PRO	C	187	−42.872	−49.703	130.024	1.00	42.12		O
ATOM	4686	CB	PRO	C	187	−43.033	−46.566	130.145	1.00	36.03		C
ATOM	4687	CG	PRO	C	187	−43.095	−45.798	128.889	1.00	29.12		C
ATOM	4688	CD	PRO	C	187	−42.697	−46.739	127.820	1.00	34.04		C
ATOM	4689	N	SER	C	188	−41.501	−49.128	131.728	1.00	47.08		N
ATOM	4690	CA	SER	C	188	−41.753	−50.348	132.489	1.00	48.24		C
ATOM	4691	C	SER	C	188	−43.244	−50.561	132.733	1.00	47.93		C
ATOM	4692	O	SER	C	188	−43.776	−51.660	132.523	1.00	45.02		O
ATOM	4693	CB	SER	C	188	−41.011	−50.260	133.813	1.00	50.96		C
ATOM	4694	OG	SER	C	188	−39.631	−50.377	133.576	1.00	59.84		O
ATOM	4695	N	SER	C	189	−43.941	−49.495	133.134	1.00	46.10		N
ATOM	4696	CA	SER	C	189	−45.363	−49.574	133.444	1.00	51.64		C
ATOM	4697	C	SER	C	189	−46.222	−50.037	132.263	1.00	51.86		C
ATOM	4698	O	SER	C	189	−47.344	−50.512	132.481	1.00	58.15		O
ATOM	4699	CB	SER	C	189	−45.834	−48.218	133.976	1.00	51.35		C
ATOM	4700	OG	SER	C	189	−45.680	−47.208	133.001	1.00	55.98		O
ATOM	4701	N	SER	C	190	−45.740	−49.918	131.022	1.00	51.05		N
ATOM	4702	CA	SER	C	190	−46.558	−50.310	129.870	1.00	50.46		C
ATOM	4703	C	SER	C	190	−46.527	−51.807	129.570	1.00	49.06		C
ATOM	4704	O	SER	C	190	−47.396	−52.279	128.830	1.00	45.72		O
ATOM	4705	CB	SER	C	190	−46.113	−49.566	128.610	1.00	40.88		C
ATOM	4706	OG	SER	C	190	−44.817	−49.995	128.218	1.00	41.80		O
ATOM	4707	N	LEU	C	191	−45.553	−52.559	130.096	1.00	47.92		N
ATOM	4708	CA	LEU	C	191	−45.508	−53.993	129.838	1.00	42.80		C
ATOM	4709	C	LEU	C	191	−46.706	−54.670	130.475	1.00	48.54		C
ATOM	4710	O	LEU	C	191	−47.206	−54.244	131.517	1.00	56.38		O
ATOM	4711	CB	LEU	C	191	−44.230	−54.612	130.387	1.00	39.21		C
ATOM	4712	CG	LEU	C	191	−42.884	−54.023	129.982	1.00	44.80		C
ATOM	4713	CD1	LEU	C	191	−41.792	−54.654	130.804	1.00	34.81		C
ATOM	4714	CD2	LEU	C	191	−42.634	−54.240	128.501	1.00	37.00		C
ATOM	4715	N	GLY	C	192	−47.170	−55.743	129.856	1.00	48.62		N
ATOM	4716	CA	GLY	C	192	−48.335	−56.412	130.386	1.00	56.13		C
ATOM	4717	C	GLY	C	192	−49.643	−55.692	130.132	1.00	55.78		C
ATOM	4718	O	GLY	C	192	−50.704	−56.327	130.177	1.00	56.01		O
ATOM	4719	N	THR	C	193	−49.601	−54.388	129.869	1.00	48.97		N
ATOM	4720	CA	THR	C	193	−50.727	−53.607	129.378	1.00	49.79		C
ATOM	4721	C	THR	C	193	−50.644	−53.332	127.883	1.00	49.11		C
ATOM	4722	O	THR	C	193	−51.669	−53.324	127.197	1.00	53.12		O
ATOM	4723	CB	THR	C	193	−50.780	−52.266	130.114	1.00	58.23		C
ATOM	4724	OG1	THR	C	193	−50.126	−52.405	131.385	1.00	58.05		O
ATOM	4725	CG2	THR	C	193	−52.227	−51.790	130.293	1.00	53.04		C
ATOM	4726	N	GLN	C	194	−49.443	−53.103	127.361	1.00	48.44		N
ATOM	4727	CA	GLN	C	194	−49.241	−52.741	125.967	1.00	42.09		C
ATOM	4728	C	GLN	C	194	−48.676	−53.911	125.177	1.00	37.51		C
ATOM	4729	O	GLN	C	194	−47.808	−54.636	125.660	1.00	40.92		O
ATOM	4730	CB	GLN	C	194	−48.324	−51.517	125.873	1.00	43.18		C
ATOM	4731	CG	GLN	C	194	−48.013	−51.097	124.469	1.00	46.41		C
ATOM	4732	CD	GLN	C	194	−49.252	−50.772	123.679	1.00	49.54		C
ATOM	4733	OE1	GLN	C	194	−49.610	−51.489	122.735	1.00	42.75		O
ATOM	4734	NE2	GLN	C	194	−49.939	−49.707	124.080	1.00	49.73		N
ATOM	4735	N	THR	C	195	−49.176	−54.093	123.963	1.00	36.34		N
ATOM	4736	CA	THR	C	195	−48.744	−55.181	123.101	1.00	39.27		C
ATOM	4737	C	THR	C	195	−47.657	−54.704	122.151	1.00	39.62		C
ATOM	4738	O	THR	C	195	−47.782	−53.650	121.523	1.00	38.44		O
ATOM	4739	CB	THR	C	195	−49.921	−55.761	122.312	1.00	43.59		C
ATOM	4740	OG1	THR	C	195	−50.568	−56.759	123.110	1.00	45.10		O
ATOM	4741	CG2	THR	C	195	−49.470	−56.364	120.984	1.00	36.94		C
ATOM	4742	N	TYR	C	196	−46.604	−55.500	122.044	1.00	39.64		N
ATOM	4743	CA	TYR	C	196	−45.452	−55.182	121.224	1.00	31.97		C
ATOM	4744	C	TYR	C	196	−45.224	−56.327	120.252	1.00	32.44		C
ATOM	4745	O	TYR	C	196	−44.912	−57.445	120.668	1.00	28.81		O
ATOM	4746	CB	TYR	C	196	−44.231	−54.930	122.098	1.00	33.73		C
ATOM	4747	CG	TYR	C	196	−44.426	−53.737	123.002	1.00	38.32		C
ATOM	4748	CD1	TYR	C	196	−44.552	−52.458	122.474	1.00	33.41		C
ATOM	4749	CD2	TYR	C	196	−44.483	−53.884	124.380	1.00	37.95		C
ATOM	4750	CE1	TYR	C	196	−44.728	−51.370	123.289	1.00	33.25		C
ATOM	4751	CE2	TYR	C	196	−44.660	−52.788	125.201	1.00	36.63		C
ATOM	4752	CZ	TYR	C	196	−44.781	−51.541	124.647	1.00	33.58		C
ATOM	4753	OH	TYR	C	196	−44.966	−50.453	125.459	1.00	38.73		O
ATOM	4754	N	ILE	C	197	−45.395	−56.038	118.964	1.00	31.69		N
ATOM	4755	CA	ILE	C	197	−45.176	−56.988	117.885	1.00	31.54		C
ATOM	4756	C	ILE	C	197	−44.163	−56.386	116.919	1.00	33.20		C
ATOM	4757	O	ILE	C	197	−44.321	−55.239	116.484	1.00	33.69		O
ATOM	4758	CB	ILE	C	197	−46.476	−57.288	117.131	1.00	31.06		C
ATOM	4759	CG1	ILE	C	197	−47.516	−57.886	118.042	1.00	33.48		C
ATOM	4760	CG2	ILE	C	197	−46.201	−58.193	115.952	1.00	33.02		C
ATOM	4761	CD1	ILE	C	197	−48.862	−57.783	117.425	1.00	24.92		C
ATOM	4762	N	CYS	C	198	−43.163	−57.165	116.533	1.00	28.72		N
ATOM	4763	CA	CYS	C	198	−42.254	−56.721	115.489	1.00	35.10		C
ATOM	4764	C	CYS	C	198	−42.613	−57.390	114.159	1.00	33.06		C
ATOM	4765	O	CYS	C	198	−42.986	−58.566	114.107	1.00	34.76		O
ATOM	4766	CB	CYS	C	198	−40.798	−56.986	115.869	1.00	35.03		C
ATOM	4767	SG	CYS	C	198	−40.302	−58.637	115.586	1.00	44.99		S
ATOM	4768	N	ASN	C	199	−42.585	−56.609	113.098	1.00	28.45		N
ATOM	4769	CA	ASN	C	199	−43.018	−57.057	111.786	1.00	29.27		C
ATOM	4770	C	ASN	C	199	−41.775	−57.159	110.921	1.00	28.88		C
ATOM	4771	O	ASN	C	199	−41.126	−56.148	110.645	1.00	34.72		O
ATOM	4772	CB	ASN	C	199	−44.058	−56.094	111.214	1.00	29.40		C
ATOM	4773	CG	ASN	C	199	−45.068	−55.631	112.274	1.00	35.22		C
ATOM	4774	OD1	ASN	C	199	−45.044	−54.468	112.719	1.00	33.27		O
ATOM	4775	ND2	ASN	C	199	−45.951	−56.546	112.693	1.00	28.65		N
ATOM	4776	N	VAL	C	200	−41.435	−58.381	110.521	1.00	26.15		N
ATOM	4777	CA	VAL	C	200	−40.230	−58.679	109.758	1.00	28.67		C
ATOM	4778	C	VAL	C	200	−40.617	−59.030	108.329	1.00	30.60		C
ATOM	4779	O	VAL	C	200	−41.478	−59.890	108.106	1.00	28.53		O
ATOM	4780	CB	VAL	C	200	−39.450	−59.841	110.388	1.00	21.99		C
ATOM	4781	CG1	VAL	C	200	−38.183	−60.065	109.624	1.00	27.77		C
ATOM	4782	CG2	VAL	C	200	−39.182	−59.577	111.849	1.00	26.33		C
ATOM	4783	N	ASN	C	201	−39.960	−58.406	107.359	1.00	31.19		N
ATOM	4784	CA	ASN	C	201	−40.153	−58.800	105.970	1.00	33.45		C
ATOM	4785	C	ASN	C	201	−38.805	−59.085	105.341	1.00	35.94		C
ATOM	4786	O	ASN	C	201	−37.952	−58.195	105.238	1.00	38.25		O
ATOM	4787	CB	ASN	C	201	−40.899	−57.739	105.160	1.00	34.65		C
ATOM	4788	CG	ASN	C	201	−41.430	−58.284	103.832	1.00	38.40		C
ATOM	4789	OD1	ASN	C	201	−42.045	−57.555	103.074	1.00	47.99		O
ATOM	4790	ND2	ASN	C	201	−41.203	−59.568	103.557	1.00	39.32		N
ATOM	4791	N	HIS	C	202	−38.630	−60.310	104.893	1.00	35.27		N
ATOM	4792	CA	HIS	C	202	−37.474	−60.692	104.107	1.00	32.39		C
ATOM	4793	C	HIS	C	202	−38.047	−60.925	102.719	1.00	34.80		C
ATOM	4794	O	HIS	C	202	−38.424	−62.043	102.375	1.00	35.23		O
ATOM	4795	CB	HIS	C	202	−36.777	−61.922	104.669	1.00	29.35		C
ATOM	4796	CG	HIS	C	202	−35.529	−62.276	103.935	1.00	32.95		C
ATOM	4797	ND1	HIS	C	202	−35.318	−63.520	103.385	1.00	37.12		N
ATOM	4798	CD2	HIS	C	202	−34.440	−61.537	103.623	1.00	31.23		C
ATOM	4799	CE1	HIS	C	202	−34.145	−63.538	102.778	1.00	33.20		C
ATOM	4800	NE2	HIS	C	202	−33.593	−62.346	102.905	1.00	32.51		N
ATOM	4801	N	LYS	C	203	−38.159	−59.837	101.948	1.00	37.66		N
ATOM	4802	CA	LYS	C	203	−38.635	−59.928	100.569	1.00	34.00		C
ATOM	4803	C	LYS	C	203	−37.907	−60.983	99.750	1.00	36.61		C
ATOM	4804	O	LYS	C	203	−38.585	−61.707	99.002	1.00	36.77		O
ATOM	4805	CB	LYS	C	203	−38.464	−58.583	99.854	1.00	31.21		C
ATOM	4806	CG	LYS	C	203	−39.438	−57.458	100.162	1.00	39.44		C
ATOM	4807	CD	LYS	C	203	−40.808	−57.621	99.534	1.00	41.59		C
ATOM	4808	CE	LYS	C	203	−41.815	−56.681	100.199	1.00	47.06		C
ATOM	4809	NZ	LYS	C	203	−41.248	−55.297	100.259	1.00	45.84		N1+
ATOM	4810	N	PRO	C	204	−36.574	−61.155	99.854	1.00	38.41		N
ATOM	4811	CA	PRO	C	204	−35.907	−62.124	98.962	1.00	33.23		C
ATOM	4812	C	PRO	C	204	−36.392	−63.552	99.111	1.00	37.59		C
ATOM	4813	O	PRO	C	204	−36.358	−64.297	98.129	1.00	44.57		O
ATOM	4814	CB	PRO	C	204	−34.425	−61.994	99.342	1.00	28.63		C
ATOM	4815	CG	PRO	C	204	−34.306	−60.634	99.898	1.00	32.37		C
ATOM	4816	CD	PRO	C	204	−35.587	−60.346	100.603	1.00	28.15		C
ATOM	4817	N	SER	C	205	−36.857	−63.964	100.287	1.00	37.25		N
ATOM	4818	CA	SER	C	205	−37.381	−65.312	100.469	1.00	37.14		C
ATOM	4819	C	SER	C	205	−38.895	−65.320	100.574	1.00	38.83		C
ATOM	4820	O	SER	C	205	−39.480	−66.367	100.869	1.00	37.58		O
ATOM	4821	CB	SER	C	205	−36.771	−65.963	101.709	1.00	34.91		C
ATOM	4822	OG	SER	C	205	−37.253	−65.348	102.893	1.00	33.36		O
ATOM	4823	N	ASN	C	206	−39.532	−64.173	100.334	1.00	40.37		N
ATOM	4824	CA	ASN	C	206	−40.974	−63.989	100.466	1.00	40.89		C
ATOM	4825	C	ASN	C	206	−41.484	−64.469	101.827	1.00	44.23		C
ATOM	4826	O	ASN	C	206	−42.478	−65.192	101.926	1.00	46.80		O
ATOM	4827	CB	ASN	C	206	−41.703	−64.684	99.332	1.00	49.25		C
ATOM	4828	CG	ASN	C	206	−42.643	−63.766	98.626	1.00	60.95		C
ATOM	4829	OD1	ASN	C	206	−42.272	−63.130	97.632	1.00	64.04		O
ATOM	4830	ND2	ASN	C	206	−43.871	−63.660	99.141	1.00	62.21		N
ATOM	4831	N	THR	C	207	−40.773	−64.069	102.880	1.00	37.63		N
ATOM	4832	CA	THR	C	207	−41.070	−64.446	104.256	1.00	33.70		C
ATOM	4833	C	THR	C	207	−41.518	−63.223	105.044	1.00	35.76		C
ATOM	4834	O	THR	C	207	−40.806	−62.218	105.096	1.00	34.16		O
ATOM	4835	CB	THR	C	207	−39.844	−65.055	104.920	1.00	30.61		C
ATOM	4836	OG1	THR	C	207	−39.390	−66.163	104.140	1.00	32.93		O
ATOM	4837	CG2	THR	C	207	−40.164	−65.490	106.323	1.00	30.98		C
ATOM	4838	N	LYS	C	208	−42.686	−63.311	105.663	1.00	35.22		N
ATOM	4839	CA	LYS	C	208	−43.154	−62.277	106.565	1.00	31.98		C
ATOM	4840	C	LYS	C	208	−43.461	−62.906	107.915	1.00	33.42		C
ATOM	4841	O	LYS	C	208	−44.079	−63.966	107.977	1.00	34.80		O
ATOM	4842	CB	LYS	C	208	−44.375	−61.587	105.990	1.00	29.96		C
ATOM	4843	CG	LYS	C	208	−44.038	−60.590	104.902	1.00	34.70		C
ATOM	4844	CD	LYS	C	208	−45.215	−59.721	104.524	1.00	37.48		C
ATOM	4845	CE	LYS	C	208	−46.304	−60.544	103.838	1.00	44.32		C
ATOM	4846	NZ	LYS	C	208	−47.529	−59.739	103.513	1.00	56.22		N1+
ATOM	4847	N	VAL	C	209	−43.064	−62.232	108.994	1.00	29.95		N
ATOM	4848	CA	VAL	C	209	−43.234	−62.745	110.348	1.00	29.28		C
ATOM	4849	C	VAL	C	209	−43.711	−61.614	111.255	1.00	31.89		C
ATOM	4850	O	VAL	C	209	−43.177	−60.501	111.209	1.00	33.86		O
ATOM	4851	CB	VAL	C	209	−41.930	−63.382	110.883	1.00	29.99		C
ATOM	4852	CG1	VAL	C	209	−42.024	−63.631	112.364	1.00	29.51		C
ATOM	4853	CG2	VAL	C	209	−41.659	−64.720	110.193	1.00	28.13		C
ATOM	4854	N	ASP	C	210	−44.744	−61.888	112.051	1.00	32.06		N
ATOM	4855	CA	ASP	C	210	−45.187	−61.015	113.137	1.00	31.18		C
ATOM	4856	C	ASP	C	210	−44.963	−61.720	114.466	1.00	32.54		C
ATOM	4857	O	ASP	C	210	−45.627	−62.717	114.749	1.00	37.02		O
ATOM	4858	CB	ASP	C	210	−46.667	−60.664	112.988	1.00	32.07		C
ATOM	4859	CG	ASP	C	210	−46.950	−59.774	111.779	1.00	38.99		C
ATOM	4860	OD1	ASP	C	210	−46.283	−58.727	111.607	1.00	38.00		O
ATOM	4861	OD2	ASP	C	210	−47.851	−60.125	110.993	1.00	43.24		O1−
ATOM	4862	N	LYS	C	211	−44.090	−61.171	115.307	1.00	28.18		N
ATOM	4863	CA	LYS	C	211	−43.714	−61.808	116.561	1.00	27.79		C
ATOM	4864	C	LYS	C	211	−44.107	−60.919	117.735	1.00	35.35		C
ATOM	4865	O	LYS	C	211	−43.646	−59.778	117.840	1.00	31.15		O
ATOM	4866	CB	LYS	C	211	−42.214	−62.112	116.591	1.00	30.51		C
ATOM	4867	CG	LYS	C	211	−41.695	−62.682	117.906	1.00	29.62		C
ATOM	4868	CD	LYS	C	211	−42.354	−64.008	118.183	1.00	35.84		C
ATOM	4869	CE	LYS	C	211	−41.473	−64.913	119.014	1.00	40.39		C
ATOM	4870	NZ	LYS	C	211	−41.983	−66.295	118.890	1.00	39.30		N1+
ATOM	4871	N	LYS	C	212	−44.971	−61.439	118.608	1.00	33.29		N
ATOM	4872	CA	LYS	C	212	−45.256	−60.779	119.867	1.00	29.95		C
ATOM	4873	C	LYS	C	212	−44.162	−61.099	120.869	1.00	33.39		C
ATOM	4874	O	LYS	C	212	−43.713	−62.248	120.985	1.00	41.06		O
ATOM	4875	CB	LYS	C	212	−46.621	−61.213	120.394	1.00	33.65		C
ATOM	4876	CG	LYS	C	212	−47.235	−60.285	121.413	1.00	32.68		C
ATOM	4877	CD	LYS	C	212	−48.491	−60.893	122.040	1.00	34.32		C
ATOM	4878	CE	LYS	C	212	−49.020	−59.999	123.150	1.00	34.90		C
ATOM	4879	NZ	LYS	C	212	−50.184	−60.548	123.882	1.00	52.78		N1+
ATOM	4880	N	VAL	C	213	−43.742	−60.078	121.602	1.00	29.81		N
ATOM	4881	CA	VAL	C	213	−42.705	−60.195	122.612	1.00	28.67		C
ATOM	4882	C	VAL	C	213	−43.332	−59.803	123.948	1.00	35.48		C
ATOM	4883	O	VAL	C	213	−43.668	−58.634	124.170	1.00	34.53		O
ATOM	4884	CB	VAL	C	213	−41.493	−59.313	122.281	1.00	34.29		C
ATOM	4885	CG1	VAL	C	213	−40.355	−59.481	123.311	1.00	29.32		C
ATOM	4886	CG2	VAL	C	213	−41.022	−59.563	120.861	1.00	28.07		C
ATOM	4887	N	GLU	C	214	−43.503	−60.781	124.833	1.00	43.40		N
ATOM	4888	CA	GLU	C	214	−44.067	−60.573	126.149	1.00	43.27		C
ATOM	4889	C	GLU	C	214	−42.990	−60.735	127.209	1.00	49.50		C
ATOM	4890	O	GLU	C	214	−42.011	−61.461	126.997	1.00	50.46		O
ATOM	4891	CB	GLU	C	214	−45.206	−61.558	126.434	1.00	48.02		C
ATOM	4892	CG	GLU	C	214	−46.365	−61.449	125.439	1.00	53.85		C
ATOM	4893	CD	GLU	C	214	−47.489	−62.450	125.686	1.00	57.28		C
ATOM	4894	OE1	GLU	C	214	−48.525	−62.026	126.249	1.00	58.32		O
ATOM	4895	OE2	GLU	C	214	−47.343	−63.644	125.318	1.00	60.40		O1−
ATOM	4896	N	PRO	C	215	−43.109	−60.039	128.338	1.00	50.15		N
ATOM	4897	CA	PRO	C	215	−42.182	−60.293	129.452	1.00	50.10		C
ATOM	4898	C	PRO	C	215	−42.336	−61.727	129.928	1.00	54.89		C
ATOM	4899	O	PRO	C	215	−43.450	−62.225	130.077	1.00	62.80		O
ATOM	4900	CB	PRO	C	215	−42.606	−59.277	130.515	1.00	49.74		C
ATOM	4901	CG	PRO	C	215	−43.879	−58.612	129.977	1.00	51.15		C
ATOM	4902	CD	PRO	C	215	−43.892	−58.805	128.515	1.00	47.22		C
ATOM	4903	N	LYS	C	216	−41.208	−62.402	130.137	1.00	59.54		N
ATOM	4904	CA	LYS	C	216	−41.205	−63.833	130.410	1.00	68.05		C
ATOM	4905	C	LYS	C	216	−40.699	−64.127	131.820	1.00	79.82		C
ATOM	4906	O	LYS	C	216	−39.755	−63.482	132.304	1.00	68.19		O
ATOM	4907	CB	LYS	C	216	−40.371	−64.581	129.359	1.00	67.81		C
ATOM	4908	CG	LYS	C	216	−40.384	−66.093	129.519	1.00	71.95		C
ATOM	4909	CD	LYS	C	216	−39.957	−66.793	128.233	1.00	73.44		C
ATOM	4910	CE	LYS	C	216	−40.151	−68.301	128.345	1.00	66.41		C
ATOM	4911	NZ	LYS	C	216	−40.055	−68.966	127.016	1.00	77.32		N1+
ATOM	4912	N	SER	C	217	−41.360	−65.090	132.479	1.00	86.12		N
ATOM	4913	CA	SER	C	217	−41.015	−65.548	133.838	1.00	92.36		C
ATOM	4914	C	SER	C	217	−40.297	−66.901	133.836	1.00	83.50		C
ATOM	4915	O	SER	C	217	−40.341	−67.644	132.851	1.00	85.79		O
ATOM	4916	CB	SER	C	217	−42.273	−65.660	134.707	1.00	84.83		C
ATOM	4917	OG	SER	C	217	−43.144	−66.656	134.191	1.00	75.85		O
TER
ATOM	4918	N	GLU	D	1	−2.709	−44.362	88.539	1.00	46.38		N
ATOM	4919	CA	GLU	D	1	−3.927	−43.604	88.796	1.00	40.18		C
ATOM	4920	C	GLU	D	1	−3.692	−42.543	89.882	1.00	40.43		C
ATOM	4921	O	GLU	D	1	−2.818	−42.704	90.730	1.00	41.89		O
ATOM	4922	CB	GLU	D	1	−5.056	−44.548	89.205	1.00	33.14		C
ATOM	4923	CG	GLU	D	1	−5.071	−44.860	90.693	1.00	34.96		C
ATOM	4924	CD	GLU	D	1	−6.026	−45.981	91.081	1.00	47.71		C
ATOM	4925	OE1	GLU	D	1	−6.745	−46.523	90.207	1.00	56.37		O
ATOM	4926	OE2	GLU	D	1	−6.060	−46.324	92.281	1.00	57.65		O1−
ATOM	4927	N	ILE	D	2	−4.482	−41.470	89.840	1.00	35.77		N
ATOM	4928	CA	ILE	D	2	−4.431	−40.417	90.844	1.00	30.01		C
ATOM	4929	C	ILE	D	2	−5.055	−40.916	92.141	1.00	34.99		C
ATOM	4930	O	ILE	D	2	−6.246	−41.247	92.184	1.00	35.20		O
ATOM	4931	CB	ILE	D	2	−5.147	−39.166	90.336	1.00	32.58		C
ATOM	4932	CG1	ILE	D	2	−4.425	−38.645	89.088	1.00	29.66		C
ATOM	4933	CG2	ILE	D	2	−5.297	−38.133	91.458	1.00	29.46		C
ATOM	4934	CD1	ILE	D	2	−5.026	−37.400	88.488	1.00	28.66		C
ATOM	4935	N	VAL	D	3	−4.263	−40.933	93.219	1.00	34.76		N
ATOM	4936	CA	VAL	D	3	−4.726	−41.369	94.533	1.00	30.38		C
ATOM	4937	C	VAL	D	3	−5.153	−40.143	95.325	1.00	31.44		C
ATOM	4938	O	VAL	D	3	−4.409	−39.155	95.403	1.00	31.03		O
ATOM	4939	CB	VAL	D	3	−3.641	−42.166	95.278	1.00	29.88		C
ATOM	4940	CG1	VAL	D	3	−4.089	−42.450	96.695	1.00	25.14		C
ATOM	4941	CG2	VAL	D	3	−3.355	−43.479	94.565	1.00	22.24		C
ATOM	4942	N	LEU	D	4	−6.379	−40.174	95.851	1.00	30.04		N
ATOM	4943	CA	LEU	D	4	−6.942	−39.055	96.604	1.00	28.75		C
ATOM	4944	C	LEU	D	4	−7.087	−39.490	98.050	1.00	29.11		C
ATOM	4945	O	LEU	D	4	−7.809	−40.450	98.337	1.00	37.17		O
ATOM	4946	CB	LEU	D	4	−8.303	−38.607	96.057	1.00	27.56		C
ATOM	4947	CG	LEU	D	4	−8.478	−38.095	94.619	1.00	27.56		C
ATOM	4948	CD1	LEU	D	4	−9.887	−37.577	94.388	1.00	23.55		C
ATOM	4949	CD2	LEU	D	4	−7.477	−37.038	94.270	1.00	27.03		C
ATOM	4950	N	THR	D	5	−6.414	−38.795	98.956	1.00	27.89		N
ATOM	4951	CA	THR	D	5	−6.535	−39.071	100.382	1.00	27.95		C
ATOM	4952	C	THR	D	5	−7.291	−37.915	101.020	1.00	27.80		C
ATOM	4953	O	THR	D	5	−6.899	−36.752	100.880	1.00	29.84		O
ATOM	4954	CB	THR	D	5	−5.180	−39.257	101.067	1.00	25.13		C
ATOM	4955	OG1	THR	D	5	−4.610	−37.975	101.281	1.00	44.55		O
ATOM	4956	CG2	THR	D	5	−4.229	−40.091	100.229	1.00	22.72		C
ATOM	4957	N	GLN	D	6	−8.379	−38.229	101.693	1.00	26.25		N
ATOM	4958	CA	GLN	D	6	−9.154	−37.231	102.401	1.00	29.68		C
ATOM	4959	C	GLN	D	6	−8.770	−37.227	103.870	1.00	29.42		C
ATOM	4960	O	GLN	D	6	−8.596	−38.287	104.475	1.00	30.59		O
ATOM	4961	CB	GLN	D	6	−10.645	−37.515	102.260	1.00	28.59		C
ATOM	4962	CG	GLN	D	6	−11.199	−37.068	100.946	1.00	26.38		C
ATOM	4963	CD	GLN	D	6	−12.674	−37.347	100.825	1.00	28.44		C
ATOM	4964	OE1	GLN	D	6	−13.063	−38.310	100.182	1.00	30.52		O
ATOM	4965	NE2	GLN	D	6	−13.507	−36.497	101.430	1.00	23.50		N
ATOM	4966	N	SER	D	7	−8.646	−36.032	104.442	1.00	32.95		N
ATOM	4967	CA	SER	D	7	−8.474	−35.923	105.893	1.00	34.15		C
ATOM	4968	C	SER	D	7	−9.305	−34.779	106.507	1.00	36.23		C
ATOM	4969	O	SER	D	7	−9.692	−33.818	105.822	1.00	34.31		O
ATOM	4970	CB	SER	D	7	−7.007	−35.732	106.234	1.00	32.05		C
ATOM	4971	OG	SER	D	7	−6.622	−34.406	105.965	1.00	36.70		O
ATOM	4972	N	PRO	D	8	−9.657	−34.917	107.791	1.00	35.26		N
ATOM	4973	CA	PRO	D	8	−9.493	−36.114	108.627	1.00	31.68		C
ATOM	4974	C	PRO	D	8	−10.479	−37.209	108.218	1.00	35.24		C
ATOM	4975	O	PRO	D	8	−11.338	−36.963	107.380	1.00	34.44		O
ATOM	4976	CB	PRO	D	8	−9.812	−35.599	110.022	1.00	31.95		C
ATOM	4977	CG	PRO	D	8	−10.849	−34.538	109.772	1.00	33.10		C
ATOM	4978	CD	PRO	D	8	−10.446	−33.874	108.471	1.00	32.84		C
ATOM	4979	N	GLY	D	9	−10.345	−38.409	108.776	1.00	36.77		N
ATOM	4980	CA	GLY	D	9	−11.322	−39.448	108.496	1.00	26.26		C
ATOM	4981	C	GLY	D	9	−12.671	−39.170	109.129	1.00	26.81		C
ATOM	4982	O	GLY	D	9	−13.706	−39.472	108.541	1.00	29.93		O
ATOM	4983	N	THR	D	10	−12.681	−38.619	110.349	1.00	29.94		N
ATOM	4984	CA	THR	D	10	−13.909	−38.207	111.025	1.00	29.91		C
ATOM	4985	C	THR	D	10	−13.748	−36.800	111.602	1.00	35.08		C
ATOM	4986	O	THR	D	10	−12.672	−36.421	112.072	1.00	37.12		O
ATOM	4987	CB	THR	D	10	−14.324	−39.175	112.138	1.00	28.55		C
ATOM	4988	OG1	THR	D	10	−14.423	−40.503	111.612	1.00	29.83		O
ATOM	4989	CG2	THR	D	10	−15.682	−38.775	112.712	1.00	26.70		C
ATOM	4990	N	LEU	D	11	−14.823	−36.022	111.527	1.00	33.72		N
ATOM	4991	CA	LEU	D	11	−14.874	−34.646	111.997	1.00	30.12		C
ATOM	4992	C	LEU	D	11	−16.092	−34.516	112.895	1.00	32.24		C
ATOM	4993	O	LEU	D	11	−17.220	−34.659	112.407	1.00	35.42		O
ATOM	4994	CB	LEU	D	11	−15.010	−33.702	110.811	1.00	31.05		C
ATOM	4995	CG	LEU	D	11	−14.043	−32.578	110.566	1.00	35.03		C
ATOM	4996	CD1	LEU	D	11	−14.736	−31.626	109.611	1.00	32.51		C
ATOM	4997	CD2	LEU	D	11	−13.741	−31.926	111.890	1.00	32.63		C
ATOM	4998	N	SER	D	12	−15.880	−34.220	114.183	1.00	27.22		N
ATOM	4999	CA	SER	D	12	−16.969	−34.041	115.149	1.00	31.54		C
ATOM	5000	C	SER	D	12	−17.136	−32.563	115.466	1.00	26.28		C
ATOM	5001	O	SER	D	12	−16.200	−31.925	115.940	1.00	31.22		O
ATOM	5002	CB	SER	D	12	−16.711	−34.815	116.443	1.00	30.19		C
ATOM	5003	OG	SER	D	12	−16.413	−36.172	116.169	1.00	30.39		O
ATOM	5004	N	LEU	D	13	−18.320	−32.023	115.209	1.00	28.43		N
ATOM	5005	CA	LEU	D	13	−18.535	−30.588	115.335	1.00	32.40		C
ATOM	5006	C	LEU	D	13	−19.965	−30.311	115.779	1.00	32.08		C
ATOM	5007	O	LEU	D	13	−20.889	−31.062	115.463	1.00	33.15		O
ATOM	5008	CB	LEU	D	13	−18.229	−29.860	114.013	1.00	29.60		C
ATOM	5009	CG	LEU	D	13	−16.792	−29.909	113.449	1.00	31.08		C
ATOM	5010	CD1	LEU	D	13	−16.740	−29.357	112.045	1.00	34.57		C
ATOM	5011	CD2	LEU	D	13	−15.818	−29.128	114.313	1.00	19.13		C
ATOM	5012	N	SER	D	14	−20.148	−29.201	116.468	1.00	33.43		N
ATOM	5013	CA	SER	D	14	−21.515	−28.841	116.784	1.00	34.69		C
ATOM	5014	C	SER	D	14	−22.184	−28.181	115.589	1.00	30.63		C
ATOM	5015	O	SER	D	14	−21.528	−27.507	114.789	1.00	26.53		O
ATOM	5016	CB	SER	D	14	−21.563	−27.869	117.963	1.00	40.13		C
ATOM	5017	OG	SER	D	14	−21.315	−28.526	119.189	1.00	49.17		O
ATOM	5018	N	PRO	D	15	−23.496	−28.324	115.471	1.00	30.71		N
ATOM	5019	CA	PRO	D	15	−24.231	−27.513	114.495	1.00	30.71		C
ATOM	5020	C	PRO	D	15	−23.981	−26.030	114.753	1.00	33.52		C
ATOM	5021	O	PRO	D	15	−23.778	−25.598	115.892	1.00	30.44		O
ATOM	5022	CB	PRO	D	15	−25.694	−27.907	114.732	1.00	29.82		C
ATOM	5023	CG	PRO	D	15	−25.633	−29.250	115.357	1.00	27.19		C
ATOM	5024	CD	PRO	D	15	−24.368	−29.263	116.188	1.00	28.99		C
ATOM	5025	N	GLY	D	16	−23.917	−25.264	113.673	1.00	34.76		N
ATOM	5026	CA	GLY	D	16	−23.561	−23.872	113.725	1.00	30.06		C
ATOM	5027	C	GLY	D	16	−22.093	−23.615	113.489	1.00	32.57		C
ATOM	5028	O	GLY	D	16	−21.728	−22.532	113.024	1.00	34.09		O
ATOM	5029	N	GLU	D	17	−21.243	−24.599	113.748	1.00	30.04		N
ATOM	5030	CA	GLU	D	17	−19.828	−24.365	113.578	1.00	29.50		C
ATOM	5031	C	GLU	D	17	−19.442	−24.466	112.111	1.00	33.26		C
ATOM	5032	O	GLU	D	17	−20.236	−24.848	111.242	1.00	28.54		O
ATOM	5033	CB	GLU	D	17	−18.997	−25.365	114.370	1.00	30.61		C
ATOM	5034	CG	GLU	D	17	−18.967	−25.187	115.863	1.00	38.28		C
ATOM	5035	CD	GLU	D	17	−17.955	−26.152	116.491	1.00	47.48		C
ATOM	5036	OE1	GLU	D	17	−16.740	−25.933	116.281	1.00	51.97		O
ATOM	5037	OE2	GLU	D	17	−18.365	−27.154	117.143	1.00	47.45		O1−
ATOM	5038	N	ARG	D	18	−18.183	−24.132	111.861	1.00	33.39		N
ATOM	5039	CA	ARG	D	18	−17.585	−24.128	110.544	1.00	30.46		C
ATOM	5040	C	ARG	D	18	−16.823	−25.439	110.354	1.00	35.01		C
ATOM	5041	O	ARG	D	18	−16.148	−25.911	111.273	1.00	36.75		O
ATOM	5042	CB	ARG	D	18	−16.673	−22.903	110.427	1.00	30.90		C
ATOM	5043	CG	ARG	D	18	−15.935	−22.722	109.136	1.00	33.87		C
ATOM	5044	CD	ARG	D	18	−14.967	−21.575	109.278	1.00	28.90		C
ATOM	5045	NE	ARG	D	18	−14.168	−21.350	108.073	1.00	42.50		N
ATOM	5046	CZ	ARG	D	18	−14.603	−20.689	106.995	1.00	46.47		C
ATOM	5047	NH1	ARG	D	18	−15.851	−20.199	106.968	1.00	39.59		N1+
ATOM	5048	NH2	ARG	D	18	−13.799	−20.529	105.939	1.00	36.96		N
ATOM	5049	N	ALA	D	19	−16.955	−26.046	109.172	1.00	33.54		N
ATOM	5050	CA	ALA	D	19	−16.302	−27.317	108.864	1.00	31.96		C
ATOM	5051	C	ALA	D	19	−15.394	−27.131	107.661	1.00	27.02		C
ATOM	5052	O	ALA	D	19	−15.760	−26.443	106.707	1.00	28.38		O
ATOM	5053	CB	ALA	D	19	−17.319	−28.428	108.564	1.00	30.29		C
ATOM	5054	N	THR	D	20	−14.203	−27.715	107.720	1.00	24.79		N
ATOM	5055	CA	THR	D	20	−13.250	−27.647	106.619	1.00	25.95		C
ATOM	5056	C	THR	D	20	−12.657	−29.031	106.370	1.00	28.87		C
ATOM	5057	O	THR	D	20	−12.056	−29.619	107.272	1.00	27.37		O
ATOM	5058	CB	THR	D	20	−12.160	−26.618	106.920	1.00	33.57		C
ATOM	5059	OG1	THR	D	20	−12.678	−25.302	106.669	1.00	35.59		O
ATOM	5060	CG2	THR	D	20	−10.942	−26.842	106.026	1.00	35.30		C
ATOM	5061	N	LEU	D	21	−12.845	−29.553	105.153	1.00	27.92		N
ATOM	5062	CA	LEU	D	21	−12.408	−30.885	104.753	1.00	21.26		C
ATOM	5063	C	LEU	D	21	−11.291	−30.788	103.721	1.00	27.12		C
ATOM	5064	O	LEU	D	21	−11.276	−29.891	102.879	1.00	25.65		O
ATOM	5065	CB	LEU	D	21	−13.567	−31.688	104.171	1.00	24.71		C
ATOM	5066	CG	LEU	D	21	−14.800	−31.873	105.044	1.00	24.88		C
ATOM	5067	CD1	LEU	D	21	−15.745	−32.804	104.393	1.00	25.75		C
ATOM	5068	CD2	LEU	D	21	−14.358	−32.453	106.324	1.00	36.95		C
ATOM	5069	N	SER	D	22	−10.364	−31.732	103.777	1.00	25.30		N
ATOM	5070	CA	SER	D	22	−9.207	−31.718	102.906	1.00	29.86		C
ATOM	5071	C	SER	D	22	−9.228	−32.907	101.960	1.00	31.55		C
ATOM	5072	O	SER	D	22	−9.637	−34.010	102.338	1.00	32.22		O
ATOM	5073	CB	SER	D	22	−7.908	−31.743	103.711	1.00	29.48		C
ATOM	5074	OG	SER	D	22	−7.484	−30.430	103.983	1.00	48.01		O
ATOM	5075	N	CYS	D	23	−8.748	−32.668	100.743	1.00	23.08		N
ATOM	5076	CA	CYS	D	23	−8.493	−33.696	99.746	1.00	29.55		C
ATOM	5077	C	CYS	D	23	−7.132	−33.425	99.133	1.00	28.60		C
ATOM	5078	O	CYS	D	23	−6.927	−32.375	98.510	1.00	28.22		O
ATOM	5079	CB	CYS	D	23	−9.577	−33.692	98.661	1.00	32.45		C
ATOM	5080	SG	CYS	D	23	−9.448	−34.937	97.349	1.00	34.53		S
ATOM	5081	N	ARG	D	24	−6.215	−34.370	99.282	1.00	27.16		N
ATOM	5082	CA	ARG	D	24	−4.896	−34.261	98.682	1.00	30.26		C
ATOM	5083	C	ARG	D	24	−4.755	−35.243	97.517	1.00	29.93		C
ATOM	5084	O	ARG	D	24	−5.021	−36.442	97.663	1.00	32.04		O
ATOM	5085	CB	ARG	D	24	−3.830	−34.452	99.759	1.00	30.70		C
ATOM	5086	CG	ARG	D	24	−3.797	−33.212	100.656	1.00	40.46		C
ATOM	5087	CD	ARG	D	24	−3.107	−33.392	101.998	1.00	47.57		C
ATOM	5088	NE	ARG	D	24	−2.760	−32.094	102.596	1.00	64.41		N
ATOM	5089	CZ	ARG	D	24	−3.482	−31.436	103.512	1.00	65.33		C
ATOM	5090	NH1	ARG	D	24	−4.626	−31.944	103.967	1.00	59.49		N1+
ATOM	5091	NH2	ARG	D	24	−3.054	−30.259	103.979	1.00	59.83		N
ATOM	5092	N	ALA	D	25	−4.379	−34.715	96.351	1.00	25.59		N
ATOM	5093	CA	ALA	D	25	−4.224	−35.487	95.126	1.00	27.28		C
ATOM	5094	C	ALA	D	25	−2.745	−35.776	94.882	1.00	29.22		C
ATOM	5095	O	ALA	D	25	−1.914	−34.868	94.943	1.00	32.95		O
ATOM	5096	CB	ALA	D	25	−4.810	−34.736	93.927	1.00	21.36		C
ATOM	5097	N	SER	D	26	−2.428	−37.029	94.593	1.00	26.23		N
ATOM	5098	CA	SER	D	26	−1.100	−37.425	94.171	1.00	26.45		C
ATOM	5099	C	SER	D	26	−1.179	−38.425	93.014	1.00	36.59		C
ATOM	5100	O	SER	D	26	−1.636	−39.568	93.195	1.00	38.09		O
ATOM	5101	CB	SER	D	26	−0.330	−38.048	95.323	1.00	31.96		C
ATOM	5102	OG	SER	D	26	0.947	−38.468	94.888	1.00	40.33		O
ATOM	5103	N	PRO	D	27	−0.729	−38.019	91.817	1.00	33.93		N
ATOM	5104	CA	PRO	D	27	−0.176	−36.725	91.413	1.00	32.59		C
ATOM	5105	C	PRO	D	27	−1.180	−35.587	91.464	1.00	31.97		C
ATOM	5106	O	PRO	D	27	−2.361	−35.800	91.744	1.00	29.04		O
ATOM	5107	CB	PRO	D	27	0.255	−36.957	89.967	1.00	25.77		C
ATOM	5108	CG	PRO	D	27	0.295	−38.395	89.799	1.00	30.50		C
ATOM	5109	CD	PRO	D	27	−0.695	−38.986	90.712	1.00	33.60		C
ATOM	5110	N	SER	D	28	−0.691	−34.384	91.176	1.00	29.51		N
ATOM	5111	CA	SER	D	28	−1.531	−33.204	91.247	1.00	33.06		C
ATOM	5112	C	SER	D	28	−2.689	−33.306	90.258	1.00	31.21		C
ATOM	5113	O	SER	D	28	−2.658	−34.064	89.292	1.00	32.08		O
ATOM	5114	CB	SER	D	28	−0.708	−31.948	90.968	1.00	30.39		C
ATOM	5115	OG	SER	D	28	0.122	−31.650	92.075	1.00	39.06		O
ATOM	5116	N	VAL	D	29	−3.741	−32.552	90.537	1.00	31.26		N
ATOM	5117	CA	VAL	D	29	−4.834	−32.398	89.589	1.00	31.02		C
ATOM	5118	C	VAL	D	29	−4.828	−30.937	89.154	1.00	30.74		C
ATOM	5119	O	VAL	D	29	−5.671	−30.137	89.581	1.00	32.15		O
ATOM	5120	CB	VAL	D	29	−6.180	−32.849	90.199	1.00	28.79		C
ATOM	5121	CG1	VAL	D	29	−7.331	−32.660	89.220	1.00	29.57		C
ATOM	5122	CG2	VAL	D	29	−6.092	−34.296	90.584	1.00	28.20		C
ATOM	5123	N	ASN	D	30	−3.867	−30.579	88.300	1.00	29.06		N
ATOM	5124	CA	ASN	D	30	−3.706	−29.191	87.881	1.00	27.78		C
ATOM	5125	C	ASN	D	30	−4.829	−28.695	86.974	1.00	28.98		C
ATOM	5126	O	ASN	D	30	−4.903	−27.494	86.715	1.00	34.22		O
ATOM	5127	CB	ASN	D	30	−2.371	−29.012	87.165	1.00	25.95		C
ATOM	5128	CG	ASN	D	30	−1.177	−29.247	88.072	1.00	29.67		C
ATOM	5129	OD1	ASN	D	30	−1.142	−28.823	89.232	1.00	38.01		O
ATOM	5130	ND2	ASN	D	30	−0.188	−29.923	87.546	1.00	31.76		N
ATOM	5131	N	SER	D	31	−5.715	−29.565	86.496	1.00	32.77		N
ATOM	5132	CA	SER	D	31	−6.854	−29.076	85.733	1.00	29.44		C
ATOM	5133	C	SER	D	31	−7.919	−28.456	86.623	1.00	29.07		C
ATOM	5134	O	SER	D	31	−8.807	−27.763	86.115	1.00	30.00		O
ATOM	5135	CB	SER	D	31	−7.480	−30.207	84.911	1.00	30.70		C
ATOM	5136	OG	SER	D	31	−7.863	−31.300	85.728	1.00	28.68		O
ATOM	5137	N	GLY	D	32	−7.865	−28.708	87.928	1.00	26.73		N
ATOM	5138	CA	GLY	D	32	−8.956	−28.326	88.788	1.00	24.35		C
ATOM	5139	C	GLY	D	32	−10.205	−29.141	88.582	1.00	28.63		C
ATOM	5140	O	GLY	D	32	−11.275	−28.720	89.003	1.00	23.12		O
ATOM	5141	N	TYR	D	33	−10.109	−30.294	87.917	1.00	28.39		N
ATOM	5142	CA	TYR	D	33	−11.280	−31.144	87.695	1.00	27.10		C
ATOM	5143	C	TYR	D	33	−11.513	−31.989	88.947	1.00	25.88		C
ATOM	5144	O	TYR	D	33	−11.254	−33.194	88.991	1.00	26.06		O
ATOM	5145	CB	TYR	D	33	−11.095	−32.028	86.468	1.00	27.24		C
ATOM	5146	CG	TYR	D	33	−11.026	−31.318	85.121	1.00	30.30		C
ATOM	5147	CD1	TYR	D	33	−11.355	−29.972	84.977	1.00	24.29		C
ATOM	5148	CD2	TYR	D	33	−10.625	−32.014	83.988	1.00	29.73		C
ATOM	5149	CE1	TYR	D	33	−11.272	−29.351	83.739	1.00	29.00		C
ATOM	5150	CE2	TYR	D	33	−10.535	−31.403	82.757	1.00	27.95		C
ATOM	5151	CZ	TYR	D	33	−10.851	−30.083	82.626	1.00	29.77		C
ATOM	5152	OH	TYR	D	33	−10.753	−29.528	81.366	1.00	27.33		O
ATOM	5153	N	LEU	D	34	−11.990	−31.331	89.993	1.00	24.59		N
ATOM	5154	CA	LEU	D	34	−12.197	−32.008	91.264	1.00	22.23		C
ATOM	5155	C	LEU	D	34	−13.626	−31.783	91.730	1.00	22.58		C
ATOM	5156	O	LEU	D	34	−14.082	−30.644	91.811	1.00	30.13		O
ATOM	5157	CB	LEU	D	34	−11.211	−31.517	92.326	1.00	22.34		C
ATOM	5158	CG	LEU	D	34	−11.174	−32.540	93.472	1.00	25.73		C
ATOM	5159	CD1	LEU	D	34	−9.862	−33.273	93.510	1.00	24.20		C
ATOM	5160	CD2	LEU	D	34	−11.517	−31.936	94.803	1.00	22.15		C
ATOM	5161	N	ALA	D	35	−14.331	−32.856	92.019	1.00	19.87		N
ATOM	5162	CA	ALA	D	35	−15.711	−32.778	92.454	1.00	21.92		C
ATOM	5163	C	ALA	D	35	−15.824	−33.191	93.917	1.00	23.07		C
ATOM	5164	O	ALA	D	35	−14.962	−33.884	94.461	1.00	19.99		O
ATOM	5165	CB	ALA	D	35	−16.614	−33.657	91.593	1.00	18.13		C
ATOM	5166	N	TRP	D	36	−16.908	−32.743	94.544	1.00	22.34		N
ATOM	5167	CA	TRP	D	36	−17.251	−33.112	95.911	1.00	25.99		C
ATOM	5168	C	TRP	D	36	−18.673	−33.656	95.941	1.00	24.08		C
ATOM	5169	O	TRP	D	36	−19.573	−33.115	95.291	1.00	23.80		O
ATOM	5170	CB	TRP	D	36	−17.138	−31.920	96.890	1.00	24.75		C
ATOM	5171	CG	TRP	D	36	−15.751	−31.504	97.216	1.00	23.08		C
ATOM	5172	CD1	TRP	D	36	−15.013	−30.555	96.564	1.00	27.42		C
ATOM	5173	CD2	TRP	D	36	−14.917	−32.009	98.268	1.00	23.07		C
ATOM	5174	NE1	TRP	D	36	−13.774	−30.439	97.142	1.00	26.35		N
ATOM	5175	CE2	TRP	D	36	−13.685	−31.316	98.193	1.00	26.49		C
ATOM	5176	CE3	TRP	D	36	−15.096	−32.959	99.275	1.00	23.59		C
ATOM	5177	CZ2	TRP	D	36	−12.630	−31.546	99.092	1.00	24.68		C
ATOM	5178	CZ3	TRP	D	36	−14.049	−33.189	100.167	1.00	27.30		C
ATOM	5179	CH2	TRP	D	36	−12.829	−32.484	100.064	1.00	27.81		C
ATOM	5180	N	TYR	D	37	−18.861	−34.737	96.689	1.00	22.56		N
ATOM	5181	CA	TYR	D	37	−20.166	−35.347	96.873	1.00	23.04		C
ATOM	5182	C	TYR	D	37	−20.507	−35.457	98.354	1.00	24.32		C
ATOM	5183	O	TYR	D	37	−19.638	−35.621	99.213	1.00	21.76		O
ATOM	5184	CB	TYR	D	37	−20.222	−36.732	96.232	1.00	22.03		C
ATOM	5185	CG	TYR	D	37	−19.937	−36.707	94.768	1.00	22.72		C
ATOM	5186	CD1	TYR	D	37	−18.634	−36.802	94.302	1.00	19.01		C
ATOM	5187	CD2	TYR	D	37	−20.965	−36.569	93.840	1.00	22.13		C
ATOM	5188	CE1	TYR	D	37	−18.355	−36.772	92.962	1.00	20.66		C
ATOM	5189	CE2	TYR	D	37	−20.690	−36.541	92.487	1.00	21.78		C
ATOM	5190	CZ	TYR	D	37	−19.378	−36.642	92.056	1.00	23.03		C
ATOM	5191	OH	TYR	D	37	−19.071	−36.606	90.716	1.00	26.68		O
ATOM	5192	N	GLN	D	38	−21.790	−35.368	98.640	1.00	24.80		N
ATOM	5193	CA	GLN	D	38	−22.316	−35.653	99.956	1.00	24.70		C
ATOM	5194	C	GLN	D	38	−23.084	−36.960	99.888	1.00	25.31		C
ATOM	5195	O	GLN	D	38	−23.766	−37.233	98.901	1.00	29.60		O
ATOM	5196	CB	GLN	D	38	−23.231	−34.524	100.429	1.00	26.48		C
ATOM	5197	CG	GLN	D	38	−23.861	−34.780	101.757	1.00	29.22		C
ATOM	5198	CD	GLN	D	38	−24.925	−33.785	102.068	1.00	32.98		C
ATOM	5199	OE1	GLN	D	38	−26.040	−33.894	101.560	1.00	39.02		O
ATOM	5200	NE2	GLN	D	38	−24.591	−32.780	102.888	1.00	28.25		N
ATOM	5201	N	GLN	D	39	−22.956	−37.781	100.916	1.00	22.53		N
ATOM	5202	CA	GLN	D	39	−23.703	−39.024	100.962	1.00	27.58		C
ATOM	5203	C	GLN	D	39	−24.189	−39.277	102.379	1.00	28.58		C
ATOM	5204	O	GLN	D	39	−23.379	−39.372	103.304	1.00	23.07		O
ATOM	5205	CB	GLN	D	39	−22.875	−40.207	100.468	1.00	26.29		C
ATOM	5206	CG	GLN	D	39	−23.719	−41.455	100.412	1.00	24.76		C
ATOM	5207	CD	GLN	D	39	−23.000	−42.610	99.847	1.00	27.83		C
ATOM	5208	OE1	GLN	D	39	−21.818	−42.804	100.103	1.00	28.43		O
ATOM	5209	NE2	GLN	D	39	−23.697	−43.390	99.042	1.00	31.88		N
ATOM	5210	N	LYS	D	40	−25.520	−39.390	102.538	1.00	28.80		N
ATOM	5211	CA	LYS	D	40	−26.175	−39.790	103.771	1.00	29.70		C
ATOM	5212	C	LYS	D	40	−26.436	−41.289	103.763	1.00	34.10		C
ATOM	5213	O	LYS	D	40	−26.510	−41.910	102.691	1.00	30.33		O
ATOM	5214	CB	LYS	D	40	−27.478	−39.021	103.946	1.00	31.38		C
ATOM	5215	CG	LYS	D	40	−27.272	−37.656	104.529	1.00	32.07		C
ATOM	5216	CD	LYS	D	40	−28.432	−36.768	104.221	1.00	42.17		C
ATOM	5217	CE	LYS	D	40	−28.195	−35.363	104.744	1.00	44.38		C
ATOM	5218	NZ	LYS	D	40	−28.086	−35.382	106.237	1.00	45.69		N1+
ATOM	5219	N	PRO	D	41	−26.551	−41.899	104.951	1.00	33.47		N
ATOM	5220	CA	PRO	D	41	−26.573	−43.373	105.051	1.00	33.11		C
ATOM	5221	C	PRO	D	41	−27.702	−44.029	104.267	1.00	30.28		C
ATOM	5222	O	PRO	D	41	−28.872	−43.660	104.394	1.00	32.79		O
ATOM	5223	CB	PRO	D	41	−26.726	−43.612	106.558	1.00	34.12		C
ATOM	5224	CG	PRO	D	41	−26.096	−42.407	107.186	1.00	25.92		C
ATOM	5225	CD	PRO	D	41	−26.471	−41.265	106.280	1.00	26.33		C
ATOM	5226	N	GLY	D	42	−27.342	−45.026	103.460	1.00	29.14		N
ATOM	5227	CA	GLY	D	42	−28.337	−45.688	102.630	1.00	29.58		C
ATOM	5228	C	GLY	D	42	−28.914	−44.852	101.497	1.00	36.52		C
ATOM	5229	O	GLY	D	42	−29.956	−45.213	100.952	1.00	36.30		O
ATOM	5230	N	GLN	D	43	−28.242	−43.771	101.092	1.00	32.91		N
ATOM	5231	CA	GLN	D	43	−28.685	−42.898	100.016	1.00	27.04		C
ATOM	5232	C	GLN	D	43	−27.619	−42.825	98.930	1.00	27.93		C
ATOM	5233	O	GLN	D	43	−26.452	−43.162	99.153	1.00	27.99		O
ATOM	5234	CB	GLN	D	43	−28.952	−41.481	100.523	1.00	30.13		C
ATOM	5235	CG	GLN	D	43	−29.659	−41.422	101.838	1.00	33.40		C
ATOM	5236	CD	GLN	D	43	−31.073	−41.941	101.754	1.00	45.27		C
ATOM	5237	OE1	GLN	D	43	−31.760	−41.731	100.750	1.00	42.82		O
ATOM	5238	NE2	GLN	D	43	−31.511	−42.665	102.800	1.00	44.71		N
ATOM	5239	N	THR	D	44	−28.032	−42.367	97.742	1.00	25.68		N
ATOM	5240	CA	THR	D	44	−27.045	−42.187	96.692	1.00	30.33		C
ATOM	5241	C	THR	D	44	−26.306	−40.848	96.866	1.00	30.71		C
ATOM	5242	O	THR	D	44	−26.834	−39.904	97.464	1.00	26.05		O
ATOM	5243	CB	THR	D	44	−27.702	−42.278	95.303	1.00	28.63		C
ATOM	5244	OG1	THR	D	44	−28.240	−41.013	94.924	1.00	32.11		O
ATOM	5245	CG2	THR	D	44	−28.834	−43.319	95.292	1.00	29.12		C
ATOM	5246	N	PRO	D	45	−25.070	−40.756	96.375	1.00	25.93		N
ATOM	5247	CA	PRO	D	45	−24.312	−39.512	96.515	1.00	25.74		C
ATOM	5248	C	PRO	D	45	−24.977	−38.343	95.801	1.00	24.98		C
ATOM	5249	O	PRO	D	45	−25.616	−38.493	94.761	1.00	23.19		O
ATOM	5250	CB	PRO	D	45	−22.962	−39.857	95.878	1.00	28.44		C
ATOM	5251	CG	PRO	D	45	−22.886	−41.342	95.963	1.00	23.47		C
ATOM	5252	CD	PRO	D	45	−24.265	−41.820	95.764	1.00	23.77		C
ATOM	5253	N	ARG	D	46	−24.812	−37.163	96.382	1.00	28.06		N
ATOM	5254	CA	ARG	D	46	−25.306	−35.910	95.824	1.00	26.21		C
ATOM	5255	C	ARG	D	46	−24.120	−35.028	95.449	1.00	27.60		C
ATOM	5256	O	ARG	D	46	−23.212	−34.814	96.265	1.00	24.95		O
ATOM	5257	CB	ARG	D	46	−26.203	−35.199	96.836	1.00	28.93		C
ATOM	5258	CG	ARG	D	46	−26.747	−33.885	96.372	1.00	35.19		C
ATOM	5259	CD	ARG	D	46	−28.129	−33.660	96.926	1.00	42.94		C
ATOM	5260	NE	ARG	D	46	−28.813	−32.616	96.172	1.00	54.78		N
ATOM	5261	CZ	ARG	D	46	−28.994	−31.379	96.619	1.00	62.11		C
ATOM	5262	NH1	ARG	D	46	−29.621	−30.481	95.858	1.00	53.78		N1+
ATOM	5263	NH2	ARG	D	46	−28.553	−31.045	97.837	1.00	63.79		N
ATOM	5264	N	LEU	D	47	−24.116	−34.535	94.216	1.00	26.63		N
ATOM	5265	CA	LEU	D	47	−23.029	−33.680	93.772	1.00	24.56		C
ATOM	5266	C	LEU	D	47	−23.125	−32.333	94.474	1.00	23.50		C
ATOM	5267	O	LEU	D	47	−24.201	−31.746	94.529	1.00	28.69		O
ATOM	5268	CB	LEU	D	47	−23.083	−33.508	92.264	1.00	21.59		C
ATOM	5269	CG	LEU	D	47	−22.042	−32.542	91.689	1.00	28.11		C
ATOM	5270	CD1	LEU	D	47	−20.587	−33.047	91.831	1.00	23.37		C
ATOM	5271	CD2	LEU	D	47	−22.396	−32.293	90.251	1.00	26.58		C
ATOM	5272	N	LEU	D	48	−22.020	−31.872	95.064	1.00	25.20		N
ATOM	5273	CA	LEU	D	48	−21.967	−30.576	95.756	1.00	29.85		C
ATOM	5274	C	LEU	D	48	−21.153	−29.530	95.021	1.00	28.28		C
ATOM	5275	O	LEU	D	48	−21.553	−28.371	94.962	1.00	26.16		O
ATOM	5276	CB	LEU	D	48	−21.354	−30.705	97.156	1.00	24.38		C
ATOM	5277	CG	LEU	D	48	−22.032	−31.429	98.300	1.00	29.64		C
ATOM	5278	CD1	LEU	D	48	−21.124	−31.235	99.476	1.00	28.92		C
ATOM	5279	CD2	LEU	D	48	−23.421	−30.868	98.604	1.00	30.54		C
ATOM	5280	N	ILE	D	49	−19.998	−29.933	94.505	1.00	24.89		N
ATOM	5281	CA	ILE	D	49	−19.008	−29.059	93.903	1.00	25.06		C
ATOM	5282	C	ILE	D	49	−18.484	−29.781	92.672	1.00	28.83		C
ATOM	5283	O	ILE	D	49	−18.212	−30.986	92.726	1.00	25.60		O
ATOM	5284	CB	ILE	D	49	−17.833	−28.787	94.879	1.00	27.73		C
ATOM	5285	CG1	ILE	D	49	−18.307	−28.181	96.214	1.00	22.96		C
ATOM	5286	CG2	ILE	D	49	−16.678	−28.055	94.176	1.00	21.77		C
ATOM	5287	CD1	ILE	D	49	−18.656	−26.704	96.180	1.00	28.66		C
ATOM	5288	N	PHE	D	50	−18.308	−29.049	91.573	1.00	25.66		N
ATOM	5289	CA	PHE	D	50	−17.533	−29.563	90.460	1.00	23.52		C
ATOM	5290	C	PHE	D	50	−16.420	−28.576	90.149	1.00	30.77		C
ATOM	5291	O	PHE	D	50	−16.505	−27.377	90.451	1.00	26.94		O
ATOM	5292	CB	PHE	D	50	−18.381	−29.861	89.202	1.00	25.10		C
ATOM	5293	CG	PHE	D	50	−19.084	−28.669	88.645	1.00	29.89		C
ATOM	5294	CD2	PHE	D	50	−20.394	−28.380	89.034	1.00	28.85		C
ATOM	5295	CD1	PHE	D	50	−18.460	−27.848	87.720	1.00	26.32		C
ATOM	5296	CE2	PHE	D	50	−21.038	−27.263	88.538	1.00	33.45		C
ATOM	5297	CE1	PHE	D	50	−19.111	−26.747	87.212	1.00	31.34		C
ATOM	5298	CZ	PHE	D	50	−20.412	−26.457	87.616	1.00	33.07		C
ATOM	5299	N	GLY	D	51	−15.381	−29.125	89.536	1.00	29.64		N
ATOM	5300	CA	GLY	D	51	−14.110	−28.473	89.344	1.00	31.07		C
ATOM	5301	C	GLY	D	51	−13.912	−27.013	89.635	1.00	29.90		C
ATOM	5302	O	GLY	D	51	−14.299	−26.190	88.823	1.00	41.98		O
ATOM	5303	N	ALA	D	52	−13.331	−26.633	90.761	1.00	29.04		N
ATOM	5304	CA	ALA	D	52	−13.045	−27.404	91.963	1.00	27.42		C
ATOM	5305	C	ALA	D	52	−13.634	−26.483	93.033	1.00	31.29		C
ATOM	5306	O	ALA	D	52	−13.389	−26.630	94.242	1.00	26.21		O
ATOM	5307	CB	ALA	D	52	−11.545	−27.613	92.180	1.00	24.46		C
ATOM	5308	N	SER	D	53	−14.356	−25.473	92.528	1.00	25.45		N
ATOM	5309	CA	SER	D	53	−14.951	−24.408	93.321	1.00	29.64		C
ATOM	5310	C	SER	D	53	−16.366	−24.061	92.909	1.00	29.31		C
ATOM	5311	O	SER	D	53	−17.001	−23.251	93.595	1.00	29.52		O
ATOM	5312	CB	SER	D	53	−14.102	−23.144	93.229	1.00	24.22		C
ATOM	5313	OG	SER	D	53	−13.751	−22.931	91.878	1.00	30.08		O
ATOM	5314	N	SER	D	54	−16.872	−24.618	91.819	1.00	24.59		N
ATOM	5315	CA	SER	D	54	−18.183	−24.249	91.320	1.00	28.33		C
ATOM	5316	C	SER	D	54	−19.261	−25.017	92.073	1.00	29.42		C
ATOM	5317	O	SER	D	54	−19.261	−26.252	92.107	1.00	28.83		O
ATOM	5318	CB	SER	D	54	−18.294	−24.510	89.818	1.00	30.14		C
ATOM	5319	OG	SER	D	54	−17.503	−23.611	89.086	1.00	31.63		O
ATOM	5320	N	ARG	D	55	−20.185	−24.274	92.653	1.00	26.56		N
ATOM	5321	CA	ARG	D	55	−21.342	−24.858	93.293	1.00	26.99		C
ATOM	5322	C	ARG	D	55	−22.293	−25.465	92.261	1.00	31.42		C
ATOM	5323	O	ARG	D	55	−22.594	−24.854	91.230	1.00	34.25		O
ATOM	5324	CB	ARG	D	55	−22.033	−23.773	94.100	1.00	31.93		C
ATOM	5325	CG	ARG	D	55	−22.782	−24.249	95.296	1.00	39.96		C
ATOM	5326	CD	ARG	D	55	−23.378	−23.054	96.043	1.00	42.71		C
ATOM	5327	NE	ARG	D	55	−22.393	−22.357	96.853	1.00	39.62		N
ATOM	5328	CZ	ARG	D	55	−21.943	−21.142	96.574	1.00	42.81		C
ATOM	5329	NH1	ARG	D	55	−21.042	−20.564	97.367	1.00	46.41		N1+
ATOM	5330	NH2	ARG	D	55	−22.396	−20.516	95.497	1.00	41.95		N
ATOM	5331	N	ALA	D	56	−22.783	−26.668	92.562	1.00	29.25		N
ATOM	5332	CA	ALA	D	56	−23.814	−27.344	91.783	1.00	34.27		C
ATOM	5333	C	ALA	D	56	−25.176	−26.678	91.997	1.00	36.12		C
ATOM	5334	O	ALA	D	56	−25.355	−25.830	92.877	1.00	36.11		O
ATOM	5335	CB	ALA	D	56	−23.891	−28.823	92.166	1.00	31.23		C
ATOM	5336	N	THR	D	57	−26.154	−27.081	91.184	1.00	36.05		N
ATOM	5337	CA	THR	D	57	−27.475	−26.471	91.274	1.00	46.10		C
ATOM	5338	C	THR	D	57	−28.178	−26.905	92.546	1.00	41.98		C
ATOM	5339	O	THR	D	57	−28.091	−28.063	92.960	1.00	44.69		O
ATOM	5340	CB	THR	D	57	−28.345	−26.861	90.081	1.00	48.23		C
ATOM	5341	OG1	THR	D	57	−27.504	−27.188	88.968	1.00	51.51		O
ATOM	5342	CG2	THR	D	57	−29.281	−25.707	89.713	1.00	39.36		C
ATOM	5343	N	GLY	D	58	−28.898	−25.966	93.148	1.00	36.11		N
ATOM	5344	CA	GLY	D	58	−29.589	−26.198	94.396	1.00	36.25		C
ATOM	5345	C	GLY	D	58	−28.722	−26.367	95.629	1.00	35.95		C
ATOM	5346	O	GLY	D	58	−29.266	−26.615	96.706	1.00	46.21		O
ATOM	5347	N	ILE	D	59	−27.406	−26.270	95.526	1.00	35.23		N
ATOM	5348	CA	ILE	D	59	−26.552	−26.443	96.707	1.00	37.35		C
ATOM	5349	C	ILE	D	59	−26.499	−25.124	97.480	1.00	32.79		C
ATOM	5350	O	ILE	D	59	−26.110	−24.102	96.902	1.00	34.26		O
ATOM	5351	CB	ILE	D	59	−25.147	−26.884	96.291	1.00	34.60		C
ATOM	5352	CG1	ILE	D	59	−25.150	−28.289	95.658	1.00	33.46		C
ATOM	5353	CG2	ILE	D	59	−24.257	−26.892	97.511	1.00	28.92		C
ATOM	5354	CD1	ILE	D	59	−25.990	−29.321	96.371	1.00	33.20		C
ATOM	5355	N	PRO	D	60	−26.822	−25.098	98.776	1.00	35.94		N
ATOM	5356	CA	PRO	D	60	−26.753	−23.831	99.528	1.00	36.87		C
ATOM	5357	C	PRO	D	60	−25.384	−23.165	99.443	1.00	39.65		C
ATOM	5358	O	PRO	D	60	−24.357	−23.825	99.258	1.00	40.06		O
ATOM	5359	CB	PRO	D	60	−27.068	−24.261	100.967	1.00	39.32		C
ATOM	5360	CG	PRO	D	60	−27.875	−25.486	100.816	1.00	40.27		C
ATOM	5361	CD	PRO	D	60	−27.346	−26.199	99.601	1.00	37.18		C
ATOM	5362	N	ASP	D	61	−25.355	−21.841	99.615	1.00	37.82		N
ATOM	5363	CA	ASP	D	61	−24.047	−21.197	99.529	1.00	38.85		C
ATOM	5364	C	ASP	D	61	−23.271	−21.286	100.830	1.00	38.37		C
ATOM	5365	O	ASP	D	61	−22.161	−20.757	100.895	1.00	43.54		O
ATOM	5366	CB	ASP	D	61	−24.153	−19.736	99.070	1.00	39.37		C
ATOM	5367	CG	ASP	D	61	−25.124	−18.914	99.898	1.00	54.57		C
ATOM	5368	OD1	ASP	D	61	−25.360	−19.253	101.082	1.00	61.72		O
ATOM	5369	OD2	ASP	D	61	−25.635	−17.901	99.363	1.00	51.55		O1−
ATOM	5370	N	ARG	D	62	−23.833	−21.947	101.850	1.00	39.40		N
ATOM	5371	CA	ARG	D	62	−23.032	−22.496	102.939	1.00	36.54		C
ATOM	5372	C	ARG	D	62	−21.805	−23.229	102.414	1.00	34.81		C
ATOM	5373	O	ARG	D	62	−20.738	−23.199	103.037	1.00	31.24		O
ATOM	5374	CB	ARG	D	62	−23.837	−23.511	103.745	1.00	37.64		C
ATOM	5375	CG	ARG	D	62	−25.054	−23.076	104.366	1.00	36.64		C
ATOM	5376	CD	ARG	D	62	−25.298	−24.006	105.536	1.00	40.91		C
ATOM	5377	NE	ARG	D	62	−25.716	−25.370	105.214	1.00	38.63		N
ATOM	5378	CZ	ARG	D	62	−26.848	−25.692	104.593	1.00	43.76		C
ATOM	5379	NH1	ARG	D	62	−27.662	−24.743	104.160	1.00	45.94		N1+
ATOM	5380	NH2	ARG	D	62	−27.159	−26.964	104.383	1.00	41.39		N
ATOM	5381	N	PHE	D	63	−21.980	−23.979	101.323	1.00	34.78		N
ATOM	5382	CA	PHE	D	63	−20.936	−24.809	100.738	1.00	34.76		C
ATOM	5383	C	PHE	D	63	−20.101	−23.966	99.797	1.00	32.41		C
ATOM	5384	O	PHE	D	63	−20.646	−23.271	98.933	1.00	35.79		O
ATOM	5385	CB	PHE	D	63	−21.536	−26.013	99.992	1.00	29.42		C
ATOM	5386	CG	PHE	D	63	−22.210	−27.001	100.898	1.00	28.36		C
ATOM	5387	CD1	PHE	D	63	−23.504	−26.790	101.344	1.00	31.54		C
ATOM	5388	CD2	PHE	D	63	−21.537	−28.120	101.336	1.00	28.75		C
ATOM	5389	CE1	PHE	D	63	−24.117	−27.686	102.190	1.00	29.90		C
ATOM	5390	CE2	PHE	D	63	−22.149	−29.017	102.180	1.00	31.42		C
ATOM	5391	CZ	PHE	D	63	−23.441	−28.796	102.611	1.00	27.00		C
ATOM	5392	N	SER	D	64	−18.783	−24.021	99.986	1.00	32.03		N
ATOM	5393	CA	SER	D	64	−17.815	−23.408	99.081	1.00	33.91		C
ATOM	5394	C	SER	D	64	−16.566	−24.279	99.051	1.00	26.96		C
ATOM	5395	O	SER	D	64	−16.345	−25.111	99.934	1.00	29.99		O
ATOM	5396	CB	SER	D	64	−17.482	−21.975	99.511	1.00	31.16		C
ATOM	5397	OG	SER	D	64	−16.576	−21.995	100.592	1.00	35.76		O
ATOM	5398	N	ALA	D	65	−15.766	−24.128	98.007	1.00	21.94		N
ATOM	5399	CA	ALA	D	65	−14.588	−24.982	97.928	1.00	27.79		C
ATOM	5400	C	ALA	D	65	−13.547	−24.302	97.063	1.00	28.20		C
ATOM	5401	O	ALA	D	65	−13.859	−23.392	96.297	1.00	28.35		O
ATOM	5402	CB	ALA	D	65	−14.930	−26.370	97.382	1.00	26.70		C
ATOM	5403	N	SER	D	66	−12.305	−24.767	97.185	1.00	31.90		N
ATOM	5404	CA	SER	D	66	−11.196	−24.189	96.432	1.00	32.71		C
ATOM	5405	C	SER	D	66	−10.001	−25.141	96.468	1.00	32.60		C
ATOM	5406	O	SER	D	66	−10.005	−26.170	97.149	1.00	34.80		O
ATOM	5407	CB	SER	D	66	−10.787	−22.831	97.003	1.00	27.36		C
ATOM	5408	OG	SER	D	66	−10.156	−23.031	98.253	1.00	32.54		O
ATOM	5409	N	GLY	D	67	−8.948	−24.745	95.780	1.00	31.68		N
ATOM	5410	CA	GLY	D	67	−7.719	−25.498	95.795	1.00	28.89		C
ATOM	5411	C	GLY	D	67	−7.316	−25.711	94.364	1.00	38.37		C
ATOM	5412	O	GLY	D	67	−8.135	−25.485	93.466	1.00	39.57		O
ATOM	5413	N	SER	D	68	−6.057	−26.066	94.125	1.00	36.68		N
ATOM	5414	CA	SER	D	68	−5.677	−26.559	92.813	1.00	36.53		C
ATOM	5415	C	SER	D	68	−4.366	−27.296	92.959	1.00	30.07		C
ATOM	5416	O	SER	D	68	−3.660	−27.148	93.952	1.00	38.18		O
ATOM	5417	CB	SER	D	68	−5.559	−25.449	91.757	1.00	44.96		C
ATOM	5418	OG	SER	D	68	−5.439	−26.014	90.444	1.00	48.06		O
ATOM	5419	N	GLY	D	69	−4.062	−28.097	91.954	1.00	29.21		N
ATOM	5420	CA	GLY	D	69	−2.896	−28.929	91.987	1.00	29.40		C
ATOM	5421	C	GLY	D	69	−3.069	−30.067	92.949	1.00	31.99		C
ATOM	5422	O	GLY	D	69	−3.815	−31.018	92.687	1.00	33.63		O
ATOM	5423	N	ALA	D	70	−2.379	−29.966	94.080	1.00	31.64		N
ATOM	5424	CA	ALA	D	70	−2.287	−31.065	95.022	1.00	31.80		C
ATOM	5425	C	ALA	D	70	−3.275	−30.980	96.171	1.00	31.37		C
ATOM	5426	O	ALA	D	70	−3.550	−32.008	96.792	1.00	36.24		O
ATOM	5427	CB	ALA	D	70	−0.868	−31.140	95.594	1.00	28.13		C
ATOM	5428	N	ASP	D	71	−3.817	−29.803	96.471	1.00	30.57		N
ATOM	5429	CA	ASP	D	71	−4.565	−29.587	97.706	1.00	33.18		C
ATOM	5430	C	ASP	D	71	−5.945	−29.009	97.415	1.00	32.16		C
ATOM	5431	O	ASP	D	71	−6.063	−27.965	96.768	1.00	31.72		O
ATOM	5432	CB	ASP	D	71	−3.800	−28.638	98.622	1.00	31.72		C
ATOM	5433	CG	ASP	D	71	−2.722	−29.331	99.396	1.00	47.35		C
ATOM	5434	OD1	ASP	D	71	−3.025	−30.000	100.408	1.00	54.93		O
ATOM	5435	OD2	ASP	D	71	−1.553	−29.211	98.980	1.00	57.78		O1−
ATOM	5436	N	PHE	D	72	−6.981	−29.643	97.939	1.00	28.95		N
ATOM	5437	CA	PHE	D	72	−8.335	−29.145	97.771	1.00	25.33		C
ATOM	5438	C	PHE	D	72	−8.994	−29.122	99.135	1.00	24.96		C
ATOM	5439	O	PHE	D	72	−8.687	−29.939	100.005	1.00	21.64		O
ATOM	5440	CB	PHE	D	72	−9.121	−30.008	96.781	1.00	26.11		C
ATOM	5441	CG	PHE	D	72	−8.492	−30.051	95.425	1.00	30.35		C
ATOM	5442	CD1	PHE	D	72	−7.479	−30.982	95.144	1.00	29.20		C
ATOM	5443	CD2	PHE	D	72	−8.862	−29.139	94.444	1.00	27.20		C
ATOM	5444	CE1	PHE	D	72	−6.862	−31.014	93.898	1.00	31.22		C
ATOM	5445	CE2	PHE	D	72	−8.250	−29.161	93.189	1.00	30.03		C
ATOM	5446	CZ	PHE	D	72	−7.251	−30.105	92.913	1.00	29.83		C
ATOM	5447	N	THR	D	73	−9.842	−28.133	99.354	1.00	23.98		N
ATOM	5448	CA	THR	D	73	−10.593	−28.118	100.589	1.00	27.63		C
ATOM	5449	C	THR	D	73	−12.045	−27.791	100.275	1.00	28.02		C
ATOM	5450	O	THR	D	73	−12.363	−27.129	99.275	1.00	25.48		O
ATOM	5451	CB	THR	D	73	−9.993	−27.156	101.661	1.00	32.96		C
ATOM	5452	OG1	THR	D	73	−10.611	−25.872	101.585	1.00	38.47		O
ATOM	5453	CG2	THR	D	73	−8.473	−26.987	101.511	1.00	24.84		C
ATOM	5454	N	LEU	D	74	−12.926	−28.368	101.090	1.00	30.82		N
ATOM	5455	CA	LEU	D	74	−14.351	−28.062	101.114	1.00	26.16		C
ATOM	5456	C	LEU	D	74	−14.662	−27.367	102.433	1.00	27.40		C
ATOM	5457	O	LEU	D	74	−14.247	−27.843	103.499	1.00	27.12		O
ATOM	5458	CB	LEU	D	74	−15.184	−29.336	100.953	1.00	21.42		C
ATOM	5459	CG	LEU	D	74	−16.696	−29.239	101.152	1.00	21.05		C
ATOM	5460	CD1	LEU	D	74	−17.360	−28.535	100.013	1.00	24.58		C
ATOM	5461	CD2	LEU	D	74	−17.329	−30.584	101.345	1.00	20.48		C
ATOM	5462	N	THR	D	75	−15.378	−26.243	102.365	1.00	24.12		N
ATOM	5463	CA	THR	D	75	−15.762	−25.486	103.548	1.00	24.98		C
ATOM	5464	C	THR	D	75	−17.286	−25.435	103.651	1.00	28.91		C
ATOM	5465	O	THR	D	75	−17.971	−25.077	102.687	1.00	33.13		O
ATOM	5466	CB	THR	D	75	−15.167	−24.066	103.513	1.00	29.48		C
ATOM	5467	OG1	THR	D	75	−13.776	−24.123	103.842	1.00	31.85		O
ATOM	5468	CG2	THR	D	75	−15.840	−23.161	104.544	1.00	30.01		C
ATOM	5469	N	ILE	D	76	−17.820	−25.840	104.799	1.00	25.85		N
ATOM	5470	CA	ILE	D	76	−19.217	−25.616	105.141	1.00	25.76		C
ATOM	5471	C	ILE	D	76	−19.211	−24.568	106.232	1.00	30.23		C
ATOM	5472	O	ILE	D	76	−18.718	−24.829	107.337	1.00	34.43		O
ATOM	5473	CB	ILE	D	76	−19.922	−26.893	105.619	1.00	28.28		C
ATOM	5474	CG1	ILE	D	76	−19.619	−28.063	104.696	1.00	28.54		C
ATOM	5475	CG2	ILE	D	76	−21.443	−26.672	105.686	1.00	28.62		C
ATOM	5476	CD1	ILE	D	76	−20.092	−29.368	105.257	1.00	27.59		C
ATOM	5477	N	SER	D	77	−19.775	−23.395	105.945	1.00	30.77		N
ATOM	5478	CA	SER	D	77	−19.475	−22.251	106.803	1.00	33.53		C
ATOM	5479	C	SER	D	77	−20.286	−22.267	108.097	1.00	32.03		C
ATOM	5480	O	SER	D	77	−19.781	−21.840	109.141	1.00	35.78		O
ATOM	5481	CB	SER	D	77	−19.681	−20.943	106.038	1.00	25.30		C
ATOM	5482	OG	SER	D	77	−21.029	−20.795	105.672	1.00	30.61		O
ATOM	5483	N	ARG	D	78	−21.539	−22.727	108.051	1.00	34.30		N
ATOM	5484	CA	ARG	D	78	−22.346	−22.937	109.254	1.00	33.67		C
ATOM	5485	C	ARG	D	78	−23.026	−24.294	109.107	1.00	33.98		C
ATOM	5486	O	ARG	D	78	−23.982	−24.422	108.341	1.00	30.96		O
ATOM	5487	CB	ARG	D	78	−23.387	−21.830	109.423	1.00	34.14		C
ATOM	5488	CG	ARG	D	78	−24.425	−22.137	110.499	1.00	46.20		C
ATOM	5489	CD	ARG	D	78	−25.375	−20.962	110.761	1.00	46.68		C
ATOM	5490	NE	ARG	D	78	−25.737	−20.874	112.185	1.00	49.36		N
ATOM	5491	CZ	ARG	D	78	−26.801	−21.439	112.763	1.00	57.02		C
ATOM	5492	NH1	ARG	D	78	−27.008	−21.283	114.074	1.00	54.06		N1+
ATOM	5493	NH2	ARG	D	78	−27.666	−22.153	112.047	1.00	59.27		N
ATOM	5494	N	LEU	D	79	−22.616	−25.273	109.904	1.00	31.63		N
ATOM	5495	CA	LEU	D	79	−23.146	−26.627	109.772	1.00	29.40		C
ATOM	5496	C	LEU	D	79	−24.623	−26.674	110.172	1.00	34.83		C
ATOM	5497	O	LEU	D	79	−24.969	−26.417	111.328	1.00	36.97		O
ATOM	5498	CB	LEU	D	79	−22.333	−27.580	110.640	1.00	26.40		C
ATOM	5499	CG	LEU	D	79	−21.373	−28.630	110.107	1.00	26.42		C
ATOM	5500	CD1	LEU	D	79	−21.113	−28.496	108.643	1.00	29.85		C
ATOM	5501	CD2	LEU	D	79	−20.083	−28.535	110.868	1.00	29.71		C
ATOM	5502	N	GLU	D	80	−25.507	−26.990	109.211	1.00	35.29		N
ATOM	5503	CA	GLU	D	80	−26.911	−27.234	109.503	1.00	33.25		C
ATOM	5504	C	GLU	D	80	−27.130	−28.711	109.784	1.00	37.31		C
ATOM	5505	O	GLU	D	80	−26.269	−29.536	109.472	1.00	34.23		O
ATOM	5506	CB	GLU	D	80	−27.771	−26.790	108.334	1.00	37.10		C
ATOM	5507	CG	GLU	D	80	−27.822	−25.300	108.123	1.00	37.33		C
ATOM	5508	CD	GLU	D	80	−28.430	−24.559	109.292	1.00	45.25		C
ATOM	5509	OE1	GLU	D	80	−29.311	−25.110	109.996	1.00	48.39		O
ATOM	5510	OE2	GLU	D	80	−28.039	−23.395	109.496	1.00	54.67		O1−
ATOM	5511	N	PRO	D	81	−28.261	−29.088	110.403	1.00	43.56		N
ATOM	5512	CA	PRO	D	81	−28.458	−30.514	110.743	1.00	45.48		C
ATOM	5513	C	PRO	D	81	−28.252	−31.464	109.571	1.00	42.65		C
ATOM	5514	O	PRO	D	81	−27.600	−32.508	109.728	1.00	39.13		O
ATOM	5515	CB	PRO	D	81	−29.909	−30.547	111.254	1.00	44.07		C
ATOM	5516	CG	PRO	D	81	−30.130	−29.185	111.794	1.00	40.26		C
ATOM	5517	CD	PRO	D	81	−29.382	−28.259	110.884	1.00	41.88		C
ATOM	5518	N	GLU	D	82	−28.761	−31.107	108.389	1.00	40.42		N
ATOM	5519	CA	GLU	D	82	−28.620	−31.911	107.178	1.00	37.02		C
ATOM	5520	C	GLU	D	82	−27.222	−31.924	106.602	1.00	38.11		C
ATOM	5521	O	GLU	D	82	−27.053	−32.461	105.498	1.00	37.79		O
ATOM	5522	CB	GLU	D	82	−29.528	−31.396	106.079	1.00	34.91		C
ATOM	5523	CG	GLU	D	82	−29.092	−30.088	105.479	1.00	42.26		C
ATOM	5524	CD	GLU	D	82	−30.094	−28.977	105.612	1.00	49.69		C
ATOM	5525	OE1	GLU	D	82	−30.683	−28.801	106.716	1.00	59.37		O
ATOM	5526	OE2	GLU	D	82	−30.297	−28.286	104.582	1.00	55.07		O1−
ATOM	5527	N	ASP	D	83	−26.234	−31.314	107.246	1.00	31.73		N
ATOM	5528	CA	ASP	D	83	−24.893	−31.308	106.690	1.00	31.81		C
ATOM	5529	C	ASP	D	83	−24.033	−32.399	107.278	1.00	27.67		C
ATOM	5530	O	ASP	D	83	−22.905	−32.577	106.833	1.00	28.90		O
ATOM	5531	CB	ASP	D	83	−24.205	−29.949	106.911	1.00	35.00		C
ATOM	5532	CG	ASP	D	83	−24.923	−28.802	106.203	1.00	36.30		C
ATOM	5533	OD1	ASP	D	83	−25.767	−29.091	105.334	1.00	39.93		O
ATOM	5534	OD2	ASP	D	83	−24.663	−27.615	106.524	1.00	33.84		O1−
ATOM	5535	N	PHE	D	84	−24.531	−33.133	108.262	1.00	28.52		N
ATOM	5536	CA	PHE	D	84	−23.736	−34.160	108.921	1.00	27.69		C
ATOM	5537	C	PHE	D	84	−23.892	−35.469	108.164	1.00	27.68		C
ATOM	5538	O	PHE	D	84	−24.963	−36.083	108.176	1.00	27.12		O
ATOM	5539	CB	PHE	D	84	−24.127	−34.276	110.391	1.00	26.49		C
ATOM	5540	CG	PHE	D	84	−23.758	−33.065	111.194	1.00	27.03		C
ATOM	5541	CD1	PHE	D	84	−22.520	−32.992	111.822	1.00	27.26		C
ATOM	5542	CD2	PHE	D	84	−24.628	−31.981	111.289	1.00	30.67		C
ATOM	5543	CE1	PHE	D	84	−22.156	−31.865	112.562	1.00	31.27		C
ATOM	5544	CE2	PHE	D	84	−24.281	−30.849	112.016	1.00	29.02		C
ATOM	5545	CZ	PHE	D	84	−23.039	−30.794	112.667	1.00	32.36		C
ATOM	5546	N	ALA	D	85	−22.815	−35.890	107.516	1.00	25.77		N
ATOM	5547	CA	ALA	D	85	−22.859	−36.899	106.469	1.00	21.15		C
ATOM	5548	C	ALA	D	85	−21.420	−37.274	106.118	1.00	22.96		C
ATOM	5549	O	ALA	D	85	−20.472	−36.875	106.800	1.00	22.25		O
ATOM	5550	CB	ALA	D	85	−23.660	−36.381	105.275	1.00	25.38		C
ATOM	5551	N	VAL	D	86	−21.251	−38.069	105.059	1.00	25.06		N
ATOM	5552	CA	VAL	D	86	−19.939	−38.399	104.521	1.00	20.70		C
ATOM	5553	C	VAL	D	86	−19.708	−37.553	103.278	1.00	22.14		C
ATOM	5554	O	VAL	D	86	−20.628	−37.341	102.488	1.00	27.68		O
ATOM	5555	CB	VAL	D	86	−19.841	−39.901	104.217	1.00	19.64		C
ATOM	5556	CG1	VAL	D	86	−18.533	−40.230	103.523	1.00	22.34		C
ATOM	5557	CG2	VAL	D	86	−19.953	−40.660	105.485	1.00	16.64		C
ATOM	5558	N	TYR	D	87	−18.497	−37.033	103.120	1.00	21.19		N
ATOM	5559	CA	TYR	D	87	−18.151	−36.206	101.975	1.00	24.17		C
ATOM	5560	C	TYR	D	87	−17.024	−36.879	101.219	1.00	25.06		C
ATOM	5561	O	TYR	D	87	−16.084	−37.381	101.837	1.00	25.52		O
ATOM	5562	CB	TYR	D	87	−17.765	−34.766	102.410	1.00	25.82		C
ATOM	5563	CG	TYR	D	87	−18.963	−34.036	102.978	1.00	24.53		C
ATOM	5564	CD1	TYR	D	87	−19.368	−34.249	104.286	1.00	22.98		C
ATOM	5565	CD2	TYR	D	87	−19.735	−33.198	102.178	1.00	22.74		C
ATOM	5566	CE1	TYR	D	87	−20.502	−33.616	104.791	1.00	27.82		C
ATOM	5567	CE2	TYR	D	87	−20.857	−32.573	102.662	1.00	22.11		C
ATOM	5568	CZ	TYR	D	87	−21.244	−32.777	103.966	1.00	28.03		C
ATOM	5569	OH	TYR	D	87	−22.379	−32.154	104.449	1.00	29.25		O
ATOM	5570	N	PHE	D	88	−17.140	−36.897	99.885	1.00	22.99		N
ATOM	5571	CA	PHE	D	88	−16.222	−37.590	98.990	1.00	25.06		C
ATOM	5572	C	PHE	D	88	−15.653	−36.649	97.952	1.00	27.58		C
ATOM	5573	O	PHE	D	88	−16.403	−35.890	97.327	1.00	28.74		O
ATOM	5574	CB	PHE	D	88	−16.920	−38.715	98.216	1.00	29.50		C
ATOM	5575	CG	PHE	D	88	−17.173	−39.937	99.013	1.00	30.12		C
ATOM	5576	CD1	PHE	D	88	−16.133	−40.820	99.283	1.00	27.68		C
ATOM	5577	CD2	PHE	D	88	−18.442	−40.231	99.470	1.00	26.34		C
ATOM	5578	CE1	PHE	D	88	−16.354	−41.984	100.003	1.00	31.19		C
ATOM	5579	CE2	PHE	D	88	−18.664	−41.389	100.198	1.00	31.81		C
ATOM	5580	CZ	PHE	D	88	−17.614	−42.268	100.470	1.00	27.93		C
ATOM	5581	N	CYS	D	89	−14.350	−36.745	97.704	1.00	26.11		N
ATOM	5582	CA	CYS	D	89	−13.809	−36.023	96.567	1.00	24.60		C
ATOM	5583	C	CYS	D	89	−13.561	−36.988	95.406	1.00	25.26		C
ATOM	5584	O	CYS	D	89	−13.464	−38.206	95.575	1.00	23.50		O
ATOM	5585	CB	CYS	D	89	−12.537	−35.249	96.941	1.00	23.65		C
ATOM	5586	SG	CYS	D	89	−11.143	−36.170	97.584	1.00	38.72		S
ATOM	5587	N	GLN	D	90	−13.489	−36.424	94.208	1.00	21.35		N
ATOM	5588	CA	GLN	D	90	−13.364	−37.237	93.006	1.00	24.00		C
ATOM	5589	C	GLN	D	90	−12.697	−36.404	91.921	1.00	24.00		C
ATOM	5590	O	GLN	D	90	−13.073	−35.249	91.715	1.00	23.20		O
ATOM	5591	CB	GLN	D	90	−14.732	−37.733	92.536	1.00	21.84		C
ATOM	5592	CG	GLN	D	90	−14.703	−38.606	91.307	1.00	21.39		C
ATOM	5593	CD	GLN	D	90	−15.439	−37.976	90.144	1.00	26.00		C
ATOM	5594	OE1	GLN	D	90	−16.481	−37.331	90.333	1.00	29.02		O
ATOM	5595	NE2	GLN	D	90	−14.915	−38.158	88.933	1.00	21.45		N
ATOM	5596	N	GLN	D	91	−11.714	−36.984	91.236	1.00	22.32		N
ATOM	5597	CA	GLN	D	91	−11.051	−36.316	90.130	1.00	24.41		C
ATOM	5598	C	GLN	D	91	−11.459	−36.980	88.818	1.00	26.03		C
ATOM	5599	O	GLN	D	91	−11.628	−38.205	88.750	1.00	23.79		O
ATOM	5600	CB	GLN	D	91	−9.520	−36.329	90.308	1.00	21.11		C
ATOM	5601	CG	GLN	D	91	−8.866	−37.697	90.214	1.00	21.28		C
ATOM	5602	CD	GLN	D	91	−8.585	−38.091	88.785	1.00	26.27		C
ATOM	5603	OE1	GLN	D	91	−8.432	−37.231	87.917	1.00	28.92		O
ATOM	5604	NE2	GLN	D	91	−8.567	−39.384	88.514	1.00	26.42		N
ATOM	5605	N	TYR	D	92	−11.588	−36.162	87.776	1.00	22.58		N
ATOM	5606	CA	TYR	D	92	−11.946	−36.594	86.432	1.00	26.01		C
ATOM	5607	C	TYR	D	92	−11.013	−35.927	85.432	1.00	27.20		C
ATOM	5608	O	TYR	D	92	−11.409	−35.517	84.334	1.00	25.89		O
ATOM	5609	CB	TYR	D	92	−13.413	−36.300	86.093	1.00	22.29		C
ATOM	5610	CG	TYR	D	92	−13.889	−34.864	86.367	1.00	26.32		C
ATOM	5611	CD1	TYR	D	92	−14.320	−34.475	87.646	1.00	21.74		C
ATOM	5612	CD2	TYR	D	92	−13.903	−33.893	85.344	1.00	26.96		C
ATOM	5613	CE1	TYR	D	92	−14.755	−33.186	87.894	1.00	22.81		C
ATOM	5614	CE2	TYR	D	92	−14.347	−32.585	85.587	1.00	24.44		C
ATOM	5615	CZ	TYR	D	92	−14.764	−32.247	86.867	1.00	27.75		C
ATOM	5616	OH	TYR	D	92	−15.189	−30.972	87.141	1.00	29.35		O
ATOM	5617	N	GLU	D	93	−9.755	−35.782	85.826	1.00	27.70		N
ATOM	5618	CA	GLU	D	93	−8.729	−35.263	84.936	1.00	29.92		C
ATOM	5619	C	GLU	D	93	−8.055	−36.384	84.141	1.00	31.61		C
ATOM	5620	O	GLU	D	93	−7.883	−36.278	82.926	1.00	33.23		O
ATOM	5621	CB	GLU	D	93	−7.687	−34.482	85.744	1.00	25.29		C
ATOM	5622	CG	GLU	D	93	−6.386	−34.312	84.993	1.00	28.20		C
ATOM	5623	CD	GLU	D	93	−5.369	−33.447	85.700	1.00	32.11		C
ATOM	5624	OE1	GLU	D	93	−5.735	−32.389	86.285	1.00	26.85		O
ATOM	5625	OE2	GLU	D	93	−4.183	−33.828	85.637	1.00	36.40		O1−
ATOM	5626	N	SER	D	94	−7.694	−37.471	84.810	1.00	28.99		N
ATOM	5627	CA	SER	D	94	−6.939	−38.555	84.213	1.00	28.53		C
ATOM	5628	C	SER	D	94	−7.651	−39.859	84.514	1.00	28.50		C
ATOM	5629	O	SER	D	94	−8.040	−40.110	85.661	1.00	26.38		O
ATOM	5630	CB	SER	D	94	−5.499	−38.586	84.754	1.00	27.94		C
ATOM	5631	OG	SER	D	94	−4.912	−39.865	84.570	1.00	33.48		O
ATOM	5632	N	SER	D	95	−7.844	−40.669	83.487	1.00	25.22		N
ATOM	5633	CA	SER	D	95	−8.488	−41.943	83.683	1.00	29.13		C
ATOM	5634	C	SER	D	95	−7.512	−42.941	84.345	1.00	28.02		C
ATOM	5635	O	SER	D	95	−6.324	−42.923	84.083	1.00	28.38		O
ATOM	5636	CB	SER	D	95	−9.012	−42.479	82.363	1.00	30.42		C
ATOM	5637	OG	SER	D	95	−9.598	−43.754	82.570	1.00	42.60		O
ATOM	5638	N	PRO	D	96	−8.018	−43.796	85.228	1.00	25.83		N
ATOM	5639	CA	PRO	D	96	−9.421	−43.894	85.652	1.00	27.86		C
ATOM	5640	C	PRO	D	96	−9.883	−42.764	86.572	1.00	29.69		C
ATOM	5641	O	PRO	D	96	−9.078	−42.248	87.363	1.00	29.09		O
ATOM	5642	CB	PRO	D	96	−9.454	−45.229	86.397	1.00	32.44		C
ATOM	5643	CG	PRO	D	96	−8.081	−45.372	86.953	1.00	29.69		C
ATOM	5644	CD	PRO	D	96	−7.169	−44.788	85.901	1.00	25.85		C
ATOM	5645	N	TRP	D	97	−11.153	−42.369	86.470	1.00	27.79		N
ATOM	5646	CA	TRP	D	97	−11.727	−41.539	87.513	1.00	23.51		C
ATOM	5647	C	TRP	D	97	−11.541	−42.239	88.855	1.00	27.99		C
ATOM	5648	O	TRP	D	97	−11.697	−43.459	88.964	1.00	26.14		O
ATOM	5649	CB	TRP	D	97	−13.205	−41.292	87.265	1.00	26.18		C
ATOM	5650	CG	TRP	D	97	−13.628	−40.489	86.072	1.00	26.55		C
ATOM	5651	CD1	TRP	D	97	−14.907	−40.229	85.726	1.00	23.15		C
ATOM	5652	CD2	TRP	D	97	−12.804	−39.864	85.056	1.00	32.73		C
ATOM	5653	NE1	TRP	D	97	−14.953	−39.474	84.583	1.00	28.40		N
ATOM	5654	CE2	TRP	D	97	−13.683	−39.228	84.151	1.00	27.44		C
ATOM	5655	CE3	TRP	D	97	−11.419	−39.760	84.835	1.00	25.48		C
ATOM	5656	CZ2	TRP	D	97	−13.232	−38.510	83.046	1.00	28.49		C
ATOM	5657	CZ3	TRP	D	97	−10.975	−39.045	83.734	1.00	23.95		C
ATOM	5658	CH2	TRP	D	97	−11.876	−38.438	82.849	1.00	28.01		C
ATOM	5659	N	THR	D	98	−11.174	−41.469	89.877	1.00	28.12		N
ATOM	5660	CA	THR	D	98	−10.911	−42.018	91.196	1.00	28.04		C
ATOM	5661	C	THR	D	98	−11.606	−41.178	92.255	1.00	27.40		C
ATOM	5662	O	THR	D	98	−11.797	−39.972	92.089	1.00	24.69		O
ATOM	5663	CB	THR	D	98	−9.390	−42.067	91.493	1.00	30.50		C
ATOM	5664	OG1	THR	D	98	−8.813	−40.781	91.230	1.00	29.88		O
ATOM	5665	CG2	THR	D	98	−8.687	−43.122	90.648	1.00	24.32		C
ATOM	5666	N	PHE	D	99	−11.928	−41.821	93.372	1.00	28.87		N
ATOM	5667	CA	PHE	D	99	−12.603	−41.187	94.492	1.00	28.08		C
ATOM	5668	C	PHE	D	99	−11.686	−41.223	95.704	1.00	31.16		C
ATOM	5669	O	PHE	D	99	−10.854	−42.128	95.835	1.00	28.56		O
ATOM	5670	CB	PHE	D	99	−13.931	−41.891	94.859	1.00	22.78		C
ATOM	5671	CG	PHE	D	99	−15.028	−41.690	93.863	1.00	25.65		C
ATOM	5672	CD1	PHE	D	99	−15.156	−42.534	92.778	1.00	25.60		C
ATOM	5673	CD2	PHE	D	99	−15.945	−40.658	94.015	1.00	25.03		C
ATOM	5674	CE1	PHE	D	99	−16.171	−42.362	91.864	1.00	23.95		C
ATOM	5675	CE2	PHE	D	99	−16.957	−40.474	93.100	1.00	25.16		C
ATOM	5676	CZ	PHE	D	99	−17.066	−41.336	92.011	1.00	23.49		C
ATOM	5677	N	GLY	D	100	−11.852	−40.218	96.597	1.00	26.03		N
ATOM	5678	CA	GLY	D	100	−11.280	−40.302	97.918	1.00	25.35		C
ATOM	5679	C	GLY	D	100	−12.110	−41.227	98.769	1.00	29.26		C
ATOM	5680	O	GLY	D	100	−13.227	−41.602	98.411	1.00	31.89		O
ATOM	5681	N	GLN	D	101	−11.553	−41.623	99.901	1.00	26.91		N
ATOM	5682	CA	GLN	D	101	−12.213	−42.607	100.740	1.00	29.14		C
ATOM	5683	C	GLN	D	101	−13.218	−42.004	101.718	1.00	33.18		C
ATOM	5684	O	GLN	D	101	−13.871	−42.757	102.446	1.00	31.79		O
ATOM	5685	CB	GLN	D	101	−11.163	−43.426	101.480	1.00	37.07		C
ATOM	5686	CG	GLN	D	101	−10.254	−44.203	100.497	1.00	50.48		C
ATOM	5687	CD	GLN	D	101	−10.653	−45.667	100.316	1.00	57.12		C
ATOM	5688	OE1	GLN	D	101	−10.139	−46.549	101.022	1.00	66.11		O
ATOM	5689	NE2	GLN	D	101	−11.564	−45.935	99.371	1.00	48.92		N
ATOM	5690	N	GLY	D	102	−13.381	−40.691	101.740	1.00	27.41		N
ATOM	5691	CA	GLY	D	102	−14.489	−40.090	102.452	1.00	24.59		C
ATOM	5692	C	GLY	D	102	−14.084	−39.542	103.806	1.00	24.13		C
ATOM	5693	O	GLY	D	102	−13.158	−40.032	104.454	1.00	30.96		O
ATOM	5694	N	THR	D	103	−14.767	−38.478	104.226	1.00	26.72		N
ATOM	5695	CA	THR	D	103	−14.681	−37.929	105.577	1.00	25.89		C
ATOM	5696	C	THR	D	103	−16.080	−37.902	106.164	1.00	25.39		C
ATOM	5697	O	THR	D	103	−16.997	−37.334	105.560	1.00	19.85		O
ATOM	5698	CB	THR	D	103	−14.116	−36.500	105.626	1.00	28.14		C
ATOM	5699	OG1	THR	D	103	−12.740	−36.480	105.221	1.00	28.24		O
ATOM	5700	CG2	THR	D	103	−14.269	−35.913	107.044	1.00	26.41		C
ATOM	5701	N	LYS	D	104	−16.230	−38.501	107.344	1.00	27.38		N
ATOM	5702	CA	LYS	D	104	−17.489	−38.491	108.073	1.00	27.31		C
ATOM	5703	C	LYS	D	104	−17.515	−37.253	108.966	1.00	28.48		C
ATOM	5704	O	LYS	D	104	−16.604	−37.032	109.773	1.00	28.70		O
ATOM	5705	CB	LYS	D	104	−17.661	−39.787	108.875	1.00	25.02		C
ATOM	5706	CG	LYS	D	104	−19.009	−39.923	109.600	1.00	29.05		C
ATOM	5707	CD	LYS	D	104	−19.050	−41.169	110.488	1.00	32.39		C
ATOM	5708	CE	LYS	D	104	−20.386	−41.319	111.265	1.00	49.50		C
ATOM	5709	NZ	LYS	D	104	−20.557	−42.613	112.082	1.00	40.68		N1+
ATOM	5710	N	VAL	D	105	−18.520	−36.416	108.767	1.00	26.83		N
ATOM	5711	CA	VAL	D	105	−18.791	−35.267	109.621	1.00	27.60		C
ATOM	5712	C	VAL	D	105	−19.905	−35.666	110.574	1.00	25.51		C
ATOM	5713	O	VAL	D	105	−21.054	−35.808	110.157	1.00	24.45		O
ATOM	5714	CB	VAL	D	105	−19.176	−34.041	108.785	1.00	27.65		C
ATOM	5715	CG1	VAL	D	105	−19.528	−32.864	109.682	1.00	29.48		C
ATOM	5716	CG2	VAL	D	105	−18.026	−33.694	107.825	1.00	22.38		C
ATOM	5717	N	GLU	D	106	−19.579	−35.866	111.851	1.00	31.50		N
ATOM	5718	CA	GLU	D	106	−20.568	−36.309	112.826	1.00	28.01		C
ATOM	5719	C	GLU	D	106	−20.867	−35.198	113.826	1.00	31.26		C
ATOM	5720	O	GLU	D	106	−20.043	−34.311	114.068	1.00	29.59		O
ATOM	5721	CB	GLU	D	106	−20.137	−37.601	113.551	1.00	29.60		C
ATOM	5722	CG	GLU	D	106	−18.949	−37.531	114.521	1.00	33.75		C
ATOM	5723	CD	GLU	D	106	−19.264	−38.095	115.928	1.00	34.42		C
ATOM	5724	OE1	GLU	D	106	−19.053	−37.378	116.921	1.00	40.25		O
ATOM	5725	OE2	GLU	D	106	−19.688	−39.257	116.061	1.00	33.48		O1−
ATOM	5726	N	ILE	D	107	−22.075	−35.258	114.387	1.00	29.99		N
ATOM	5727	CA	ILE	D	107	−22.541	−34.269	115.347	1.00	27.29		C
ATOM	5728	C	ILE	D	107	−21.815	−34.467	116.668	1.00	32.55		C
ATOM	5729	O	ILE	D	107	−21.916	−35.529	117.291	1.00	29.14		O
ATOM	5730	CB	ILE	D	107	−24.048	−34.396	115.581	1.00	29.36		C
ATOM	5731	CG1	ILE	D	107	−24.859	−33.985	114.363	1.00	29.05		C
ATOM	5732	CG2	ILE	D	107	−24.428	−33.602	116.816	1.00	30.42		C
ATOM	5733	CD1	ILE	D	107	−26.308	−34.346	114.489	1.00	29.83		C
ATOM	5734	N	LYS	D	108	−21.120	−33.428	117.121	1.00	35.45		N
ATOM	5735	CA	LYS	D	108	−20.531	−33.410	118.452	1.00	32.78		C
ATOM	5736	C	LYS	D	108	−21.581	−32.996	119.483	1.00	36.07		C
ATOM	5737	O	LYS	D	108	−22.303	−32.011	119.282	1.00	36.02		O
ATOM	5738	CB	LYS	D	108	−19.355	−32.445	118.484	1.00	34.28		C
ATOM	5739	CG	LYS	D	108	−18.623	−32.454	119.791	1.00	36.31		C
ATOM	5740	CD	LYS	D	108	−17.705	−31.273	119.907	1.00	36.98		C
ATOM	5741	CE	LYS	D	108	−16.504	−31.728	120.659	1.00	44.81		C
ATOM	5742	NZ	LYS	D	108	−16.855	−33.094	121.165	1.00	40.45		N1+
ATOM	5743	N	ARG	D	109	−21.682	−33.760	120.572	1.00	31.47		N
ATOM	5744	CA	ARG	D	109	−22.636	−33.469	121.642	1.00	32.33		C
ATOM	5745	C	ARG	D	109	−22.004	−33.853	122.962	1.00	30.94		C
ATOM	5746	O	ARG	D	109	−20.848	−34.273	123.008	1.00	35.21		O
ATOM	5747	CB	ARG	D	109	−23.957	−34.203	121.464	1.00	26.67		C
ATOM	5748	CG	ARG	D	109	−23.826	−35.711	121.380	1.00	32.22		C
ATOM	5749	CD	ARG	D	109	−25.081	−36.397	121.890	1.00	28.47		C
ATOM	5750	NE	ARG	D	109	−25.123	−36.331	123.335	1.00	32.52		N
ATOM	5751	CZ	ARG	D	109	−26.235	−36.307	124.056	1.00	28.79		C
ATOM	5752	NH1	ARG	D	109	−26.159	−36.242	125.377	1.00	28.77		N1+
ATOM	5753	NH2	ARG	D	109	−27.406	−36.312	123.460	1.00	25.19		N
ATOM	5754	N	THR	D	110	−22.765	−33.713	124.040	1.00	27.95		N
ATOM	5755	CA	THR	D	110	−22.224	−34.032	125.356	1.00	33.38		C
ATOM	5756	C	THR	D	110	−22.147	−35.538	125.572	1.00	32.27		C
ATOM	5757	O	THR	D	110	−22.956	−36.306	125.044	1.00	32.94		O
ATOM	5758	CB	THR	D	110	−23.068	−33.429	126.468	1.00	32.63		C
ATOM	5759	OG1	THR	D	110	−24.415	−33.917	126.356	1.00	28.33		O
ATOM	5760	CG2	THR	D	110	−23.037	−31.936	126.370	1.00	31.15		C
ATOM	5761	N	VAL	D	111	−21.145	−35.946	126.354	1.00	29.24		N
ATOM	5762	CA	VAL	D	111	−20.999	−37.339	126.750	1.00	29.80		C
ATOM	5763	C	VAL	D	111	−22.298	−37.861	127.374	1.00	31.10		C
ATOM	5764	O	VAL	D	111	−22.978	−37.165	128.137	1.00	36.10		O
ATOM	5765	CB	VAL	D	111	−19.794	−37.464	127.699	1.00	29.10		C
ATOM	5766	CG1	VAL	D	111	−19.627	−38.899	128.181	1.00	32.56		C
ATOM	5767	CG2	VAL	D	111	−18.522	−36.988	126.978	1.00	24.86		C
ATOM	5768	N	ALA	D	112	−22.665	−39.086	127.004	1.00	30.83		N
ATOM	5769	CA	ALA	D	112	−23.886	−39.735	127.460	1.00	27.58		C
ATOM	5770	C	ALA	D	112	−23.597	−41.211	127.684	1.00	30.58		C
ATOM	5771	O	ALA	D	112	−23.169	−41.899	126.759	1.00	35.39		O
ATOM	5772	CB	ALA	D	112	−25.003	−39.561	126.435	1.00	26.61		C
ATOM	5773	N	ALA	D	113	−23.828	−41.703	128.896	1.00	32.52		N
ATOM	5774	CA	ALA	D	113	−23.548	−43.102	129.185	1.00	31.32		C
ATOM	5775	C	ALA	D	113	−24.588	−44.017	128.544	1.00	31.91		C
ATOM	5776	O	ALA	D	113	−25.757	−43.648	128.414	1.00	30.66		O
ATOM	5777	CB	ALA	D	113	−23.530	−43.351	130.685	1.00	26.64		C
ATOM	5778	N	PRO	D	114	−24.193	−45.222	128.150	1.00	29.42		N
ATOM	5779	CA	PRO	D	114	−25.182	−46.176	127.649	1.00	29.26		C
ATOM	5780	C	PRO	D	114	−26.021	−46.730	128.781	1.00	29.73		C
ATOM	5781	O	PRO	D	114	−25.589	−46.804	129.925	1.00	28.84		O
ATOM	5782	CB	PRO	D	114	−24.334	−47.277	127.005	1.00	27.37		C
ATOM	5783	CG	PRO	D	114	−23.042	−47.236	127.766	1.00	30.02		C
ATOM	5784	CD	PRO	D	114	−22.823	−45.773	128.131	1.00	29.01		C
ATOM	5785	N	SER	D	115	−27.255	−47.068	128.454	1.00	28.42		N
ATOM	5786	CA	SER	D	115	−28.020	−47.994	129.254	1.00	24.77		C
ATOM	5787	C	SER	D	115	−27.788	−49.394	128.706	1.00	27.46		C
ATOM	5788	O	SER	D	115	−27.741	−49.606	127.489	1.00	25.81		O
ATOM	5789	CB	SER	D	115	−29.502	−47.638	129.221	1.00	27.83		C
ATOM	5790	OG	SER	D	115	−29.644	−46.253	129.452	1.00	30.47		O
ATOM	5791	N	VAL	D	116	−27.612	−50.342	129.612	1.00	26.91		N
ATOM	5792	CA	VAL	D	116	−27.156	−51.679	129.275	1.00	27.26		C
ATOM	5793	C	VAL	D	116	−28.258	−52.657	129.636	1.00	26.73		C
ATOM	5794	O	VAL	D	116	−28.800	−52.605	130.742	1.00	33.45		O
ATOM	5795	CB	VAL	D	116	−25.850	−52.032	130.010	1.00	29.29		C
ATOM	5796	CG1	VAL	D	116	−25.339	−53.387	129.535	1.00	30.85		C
ATOM	5797	CG2	VAL	D	116	−24.814	−50.930	129.803	1.00	24.64		C
ATOM	5798	N	PHE	D	117	−28.591	−53.535	128.703	1.00	25.90		N
ATOM	5799	CA	PHE	D	117	−29.585	−54.573	128.907	1.00	25.96		C
ATOM	5800	C	PHE	D	117	−29.037	−55.838	128.293	1.00	27.24		C
ATOM	5801	O	PHE	D	117	−28.399	−55.788	127.240	1.00	29.01		O
ATOM	5802	CB	PHE	D	117	−30.930	−54.282	128.244	1.00	26.04		C
ATOM	5803	CG	PHE	D	117	−31.510	−52.943	128.560	1.00	29.45		C
ATOM	5804	CD1	PHE	D	117	−31.119	−51.810	127.851	1.00	28.96		C
ATOM	5805	CD2	PHE	D	117	−32.523	−52.826	129.497	1.00	27.92		C
ATOM	5806	CE1	PHE	D	117	−31.698	−50.590	128.119	1.00	31.67		C
ATOM	5807	CE2	PHE	D	117	−33.108	−51.607	129.767	1.00	28.75		C
ATOM	5808	CZ	PHE	D	117	−32.705	−50.490	129.086	1.00	31.59		C
ATOM	5809	N	ILE	D	118	−29.288	−56.966	128.938	1.00	28.76		N
ATOM	5810	CA	ILE	D	118	−28.835	−58.252	128.429	1.00	30.93		C
ATOM	5811	C	ILE	D	118	−30.053	−59.149	128.291	1.00	27.51		C
ATOM	5812	O	ILE	D	118	−30.949	−59.115	129.134	1.00	28.60		O
ATOM	5813	CB	ILE	D	118	−27.764	−58.872	129.348	1.00	29.79		C
ATOM	5814	CG1	ILE	D	118	−27.230	−60.167	128.757	1.00	33.20		C
ATOM	5815	CG2	ILE	D	118	−28.321	−59.122	130.738	1.00	28.76		C
ATOM	5816	CD1	ILE	D	118	−26.243	−60.873	129.679	1.00	35.26		C
ATOM	5817	N	PHE	D	119	−30.108	−59.909	127.204	1.00	28.10		N
ATOM	5818	CA	PHE	D	119	−31.241	−60.753	126.853	1.00	27.79		C
ATOM	5819	C	PHE	D	119	−30.812	−62.209	126.778	1.00	32.91		C
ATOM	5820	O	PHE	D	119	−29.869	−62.544	126.044	1.00	31.43		O
ATOM	5821	CB	PHE	D	119	−31.858	−60.343	125.507	1.00	29.66		C
ATOM	5822	CG	PHE	D	119	−32.413	−58.970	125.513	1.00	31.25		C
ATOM	5823	CD1	PHE	D	119	−33.683	−58.729	126.018	1.00	26.70		C
ATOM	5824	CD2	PHE	D	119	−31.659	−57.909	125.051	1.00	27.96		C
ATOM	5825	CE1	PHE	D	119	−34.198	−57.450	126.055	1.00	28.84		C
ATOM	5826	CE2	PHE	D	119	−32.165	−56.635	125.086	1.00	30.39		C
ATOM	5827	CZ	PHE	D	119	−33.445	−56.399	125.584	1.00	27.28		C
ATOM	5828	N	PRO	D	120	−31.482	−63.097	127.497	1.00	35.56		N
ATOM	5829	CA	PRO	D	120	−31.187	−64.530	127.394	1.00	36.54		C
ATOM	5830	C	PRO	D	120	−31.661	−65.088	126.065	1.00	34.90		C
ATOM	5831	O	PRO	D	120	−32.495	−64.470	125.387	1.00	33.38		O
ATOM	5832	CB	PRO	D	120	−31.987	−65.138	128.557	1.00	36.73		C
ATOM	5833	CG	PRO	D	120	−32.403	−63.956	129.408	1.00	42.07		C
ATOM	5834	CD	PRO	D	120	−32.546	−62.814	128.466	1.00	32.56		C
ATOM	5835	N	PRO	D	121	−31.155	−66.248	125.655	1.00	33.49		N
ATOM	5836	CA	PRO	D	121	−31.711	−66.900	124.463	1.00	35.36		C
ATOM	5837	C	PRO	D	121	−33.137	−67.359	124.718	1.00	32.32		C
ATOM	5838	O	PRO	D	121	−33.510	−67.738	125.829	1.00	33.72		O
ATOM	5839	CB	PRO	D	121	−30.772	−68.091	124.225	1.00	34.18		C
ATOM	5840	CG	PRO	D	121	−30.187	−68.357	125.588	1.00	34.16		C
ATOM	5841	CD	PRO	D	121	−30.062	−67.026	126.262	1.00	28.95		C
ATOM	5842	N	SER	D	122	−33.949	−67.282	123.672	1.00	37.30		N
ATOM	5843	CA	SER	D	122	−35.326	−67.733	123.761	1.00	35.72		C
ATOM	5844	C	SER	D	122	−35.386	−69.261	123.796	1.00	40.60		C
ATOM	5845	O	SER	D	122	−34.510	−69.961	123.264	1.00	37.13		O
ATOM	5846	CB	SER	D	122	−36.141	−67.176	122.589	1.00	30.63		C
ATOM	5847	OG	SER	D	122	−35.821	−67.837	121.384	1.00	34.59		O
ATOM	5848	N	ASP	D	123	−36.413	−69.776	124.481	1.00	44.14		N
ATOM	5849	CA	ASP	D	123	−36.631	−71.221	124.525	1.00	47.46		C
ATOM	5850	C	ASP	D	123	−36.913	−71.793	123.142	1.00	46.92		C
ATOM	5851	O	ASP	D	123	−36.606	−72.964	122.884	1.00	49.21		O
ATOM	5852	CB	ASP	D	123	−37.776	−71.541	125.478	1.00	54.79		C
ATOM	5853	CG	ASP	D	123	−37.352	−71.471	126.921	1.00	61.77		C
ATOM	5854	OD1	ASP	D	123	−36.195	−71.849	127.207	1.00	56.99		O
ATOM	5855	OD2	ASP	D	123	−38.161	−71.015	127.763	1.00	71.23		O1−
ATOM	5856	N	GLU	D	124	−37.480	−70.978	122.241	1.00	45.60		N
ATOM	5857	CA	GLU	D	124	−37.753	−71.411	120.869	1.00	49.64		C
ATOM	5858	C	GLU	D	124	−36.463	−71.644	120.084	1.00	50.62		C
ATOM	5859	O	GLU	D	124	−36.383	−72.565	119.259	1.00	49.45		O
ATOM	5860	CB	GLU	D	124	−38.613	−70.365	120.168	1.00	45.37		C
ATOM	5861	CG	GLU	D	124	−39.053	−70.740	118.759	1.00	60.55		C
ATOM	5862	CD	GLU	D	124	−39.635	−69.542	117.988	1.00	74.03		C
ATOM	5863	OE1	GLU	D	124	−39.948	−68.502	118.626	1.00	67.91		O
ATOM	5864	OE2	GLU	D	124	−39.760	−69.633	116.740	1.00	80.45		O1−
ATOM	5865	N	GLN	D	125	−35.452	−70.799	120.309	1.00	44.68		N
ATOM	5866	CA	GLN	D	125	−34.161	−70.979	119.660	1.00	44.38		C
ATOM	5867	C	GLN	D	125	−33.365	−72.110	120.296	1.00	44.17		C
ATOM	5868	O	GLN	D	125	−32.617	−72.803	119.596	1.00	44.30		O
ATOM	5869	CB	GLN	D	125	−33.353	−69.677	119.726	1.00	38.62		C
ATOM	5870	CG	GLN	D	125	−32.017	−69.721	118.987	1.00	34.83		C
ATOM	5871	CD	GLN	D	125	−31.067	−68.656	119.471	1.00	36.06		C
ATOM	5872	OE1	GLN	D	125	−31.232	−68.116	120.570	1.00	37.90		O
ATOM	5873	NE2	GLN	D	125	−30.080	−68.328	118.652	1.00	40.51		N
ATOM	5874	N	LEU	D	126	−33.515	−72.316	121.606	1.00	39.87		N
ATOM	5875	CA	LEU	D	126	−32.798	−73.405	122.254	1.00	43.24		C
ATOM	5876	C	LEU	D	126	−33.200	−74.756	121.683	1.00	49.92		C
ATOM	5877	O	LEU	D	126	−32.343	−75.623	121.467	1.00	50.55		O
ATOM	5878	CB	LEU	D	126	−33.035	−73.372	123.755	1.00	37.51		C
ATOM	5879	CG	LEU	D	126	−32.229	−72.275	124.411	1.00	38.73		C
ATOM	5880	CD1	LEU	D	126	−32.542	−72.240	125.881	1.00	34.97		C
ATOM	5881	CD2	LEU	D	126	−30.723	−72.461	124.145	1.00	38.73		C
ATOM	5882	N	LYS	D	127	−34.486	−74.933	121.365	1.00	50.02		N
ATOM	5883	CA	LYS	D	127	−34.931	−76.193	120.777	1.00	50.42		C
ATOM	5884	C	LYS	D	127	−34.041	−76.636	119.621	1.00	50.52		C
ATOM	5885	O	LYS	D	127	−33.827	−77.838	119.434	1.00	61.34		O
ATOM	5886	CB	LYS	D	127	−36.378	−76.066	120.287	1.00	54.82		C
ATOM	5887	CG	LYS	D	127	−37.364	−75.491	121.309	1.00	56.44		C
ATOM	5888	CD	LYS	D	127	−38.834	−75.811	120.959	1.00	64.32		C
ATOM	5889	CE	LYS	D	127	−39.297	−75.170	119.628	1.00	72.71		C
ATOM	5890	NZ	LYS	D	127	−39.699	−76.161	118.571	1.00	64.97		N1+
ATOM	5891	N	SER	D	128	−33.470	−75.687	118.880	1.00	50.62		N
ATOM	5892	CA	SER	D	128	−32.691	−75.949	117.674	1.00	48.62		C
ATOM	5893	C	SER	D	128	−31.181	−76.031	117.919	1.00	52.68		C
ATOM	5894	O	SER	D	128	−30.403	−76.019	116.957	1.00	53.36		O
ATOM	5895	CB	SER	D	128	−32.998	−74.877	116.626	1.00	51.45		C
ATOM	5896	OG	SER	D	128	−32.539	−73.605	117.065	1.00	54.76		O
ATOM	5897	N	GLY	D	129	−30.742	−76.074	119.169	1.00	49.90		N
ATOM	5898	CA	GLY	D	129	−29.355	−76.368	119.452	1.00	48.29		C
ATOM	5899	C	GLY	D	129	−28.416	−75.187	119.533	1.00	52.26		C
ATOM	5900	O	GLY	D	129	−27.243	−75.382	119.882	1.00	50.58		O
ATOM	5901	N	THR	D	130	−28.886	−73.969	119.259	1.00	49.43		N
ATOM	5902	CA	THR	D	130	−28.043	−72.784	119.302	1.00	44.36		C
ATOM	5903	C	THR	D	130	−28.614	−71.774	120.285	1.00	44.57		C
ATOM	5904	O	THR	D	130	−29.830	−71.596	120.369	1.00	45.91		O
ATOM	5905	CB	THR	D	130	−27.942	−72.142	117.926	1.00	49.85		C
ATOM	5906	OG1	THR	D	130	−27.337	−73.073	117.030	1.00	49.94		O
ATOM	5907	CG2	THR	D	130	−27.087	−70.871	117.975	1.00	47.05		C
ATOM	5908	N	ALA	D	131	−27.729	−71.098	121.008	1.00	40.05		N
ATOM	5909	CA	ALA	D	131	−28.104	−70.036	121.924	1.00	38.97		C
ATOM	5910	C	ALA	D	131	−27.432	−68.727	121.512	1.00	37.81		C
ATOM	5911	O	ALA	D	131	−26.209	−68.683	121.329	1.00	38.34		O
ATOM	5912	CB	ALA	D	131	−27.721	−70.421	123.347	1.00	38.52		C
ATOM	5913	N	SER	D	132	−28.224	−67.667	121.359	1.00	33.37		N
ATOM	5914	CA	SER	D	132	−27.707	−66.314	121.152	1.00	30.63		C
ATOM	5915	C	SER	D	132	−28.011	−65.482	122.392	1.00	31.31		C
ATOM	5916	O	SER	D	132	−29.166	−65.369	122.800	1.00	39.28		O
ATOM	5917	CB	SER	D	132	−28.321	−65.659	119.913	1.00	31.88		C
ATOM	5918	OG	SER	D	132	−27.968	−66.338	118.727	1.00	32.64		O
ATOM	5919	N	VAL	D	133	−26.999	−64.942	123.008	1.00	32.01		N
ATOM	5920	CA	VAL	D	133	−27.179	−63.987	124.097	1.00	34.18		C
ATOM	5921	C	VAL	D	133	−26.944	−62.601	123.519	1.00	32.77		C
ATOM	5922	O	VAL	D	133	−26.025	−62.421	122.706	1.00	31.33		O
ATOM	5923	CB	VAL	D	133	−26.213	−64.294	125.261	1.00	34.59		C
ATOM	5924	CG1	VAL	D	133	−26.610	−63.544	126.532	1.00	32.22		C
ATOM	5925	CG2	VAL	D	133	−26.180	−65.792	125.517	1.00	30.53		C
ATOM	5926	N	VAL	D	134	−27.781	−61.625	123.893	1.00	27.21		N
ATOM	5927	CA	VAL	D	134	−27.711	−60.290	123.295	1.00	28.33		C
ATOM	5928	C	VAL	D	134	−27.496	−59.226	124.365	1.00	28.83		C
ATOM	5929	O	VAL	D	134	−28.174	−59.214	125.397	1.00	27.78		O
ATOM	5930	CB	VAL	D	134	−28.950	−59.955	122.450	1.00	27.75		C
ATOM	5931	CG1	VAL	D	134	−28.794	−58.585	121.858	1.00	26.08		C
ATOM	5932	CG2	VAL	D	134	−29.096	−60.957	121.319	1.00	30.78		C
ATOM	5933	N	CYS	D	135	−26.565	−58.313	124.092	1.00	27.54		N
ATOM	5934	CA	CYS	D	135	−26.299	−57.155	124.928	1.00	31.96		C
ATOM	5935	C	CYS	D	135	−26.651	−55.895	124.141	1.00	32.81		C
ATOM	5936	O	CYS	D	135	−26.250	−55.760	122.979	1.00	27.82		O
ATOM	5937	CB	CYS	D	135	−24.827	−57.154	125.365	1.00	32.75		C
ATOM	5938	SG	CYS	D	135	−24.350	−56.013	126.697	1.00	40.27		S
ATOM	5939	N	LEU	D	136	−27.422	−54.996	124.762	1.00	26.44		N
ATOM	5940	CA	LEU	D	136	−27.826	−53.726	124.161	1.00	24.84		C
ATOM	5941	C	LEU	D	136	−27.168	−52.559	124.898	1.00	28.43		C
ATOM	5942	O	LEU	D	136	−27.375	−52.380	126.107	1.00	27.53		O
ATOM	5943	CB	LEU	D	136	−29.345	−53.566	124.191	1.00	26.69		C
ATOM	5944	CG	LEU	D	136	−29.908	−52.191	123.787	1.00	30.11		C
ATOM	5945	CD1	LEU	D	136	−29.570	−51.875	122.330	1.00	22.63		C
ATOM	5946	CD2	LEU	D	136	−31.439	−52.087	124.042	1.00	23.90		C
ATOM	5947	N	LEU	D	137	−26.403	−51.746	124.169	1.00	27.96		N
ATOM	5948	CA	LEU	D	137	−25.860	−50.492	124.687	1.00	24.59		C
ATOM	5949	C	LEU	D	137	−26.657	−49.367	124.027	1.00	28.90		C
ATOM	5950	O	LEU	D	137	−26.501	−49.096	122.830	1.00	28.52		O
ATOM	5951	CB	LEU	D	137	−24.364	−50.380	124.419	1.00	20.03		C
ATOM	5952	CG	LEU	D	137	−23.377	−51.186	125.271	1.00	24.15		C
ATOM	5953	CD1	LEU	D	137	−23.602	−52.697	125.252	1.00	20.47		C
ATOM	5954	CD2	LEU	D	137	−21.943	−50.875	124.827	1.00	21.46		C
ATOM	5955	N	ASN	D	138	−27.531	−48.732	124.806	1.00	30.48		N
ATOM	5956	CA	ASN	D	138	−28.551	−47.836	124.285	1.00	28.96		C
ATOM	5957	C	ASN	D	138	−28.215	−46.368	124.560	1.00	31.63		C
ATOM	5958	O	ASN	D	138	−27.933	−45.994	125.705	1.00	33.79		O
ATOM	5959	CB	ASN	D	138	−29.904	−48.179	124.900	1.00	27.28		C
ATOM	5960	CG	ASN	D	138	−31.052	−47.802	124.004	1.00	31.25		C
ATOM	5961	OD1	ASN	D	138	−31.153	−48.280	122.875	1.00	36.62		O
ATOM	5962	ND2	ASN	D	138	−31.880	−46.874	124.463	1.00	36.73		N
ATOM	5963	N	ASN	D	139	−28.258	−45.549	123.495	1.00	33.24		N
ATOM	5964	CA	ASN	D	139	−28.250	−44.074	123.524	1.00	28.78		C
ATOM	5965	C	ASN	D	139	−27.036	−43.490	124.238	1.00	27.30		C
ATOM	5966	O	ASN	D	139	−27.168	−42.799	125.238	1.00	35.75		O
ATOM	5967	CB	ASN	D	139	−29.520	−43.529	124.171	1.00	27.41		C
ATOM	5968	CG	ASN	D	139	−30.755	−43.820	123.364	1.00	34.79		C
ATOM	5969	OD1	ASN	D	139	−30.693	−44.255	122.215	1.00	31.67		O
ATOM	5970	ND2	ASN	D	139	−31.903	−43.606	123.985	1.00	49.31		N
ATOM	5971	N	PHE	D	140	−25.853	−43.720	123.683	1.00	28.66		N
ATOM	5972	CA	PHE	D	140	−24.631	−43.200	124.279	1.00	30.52		C
ATOM	5973	C	PHE	D	140	−23.895	−42.295	123.301	1.00	30.45		C
ATOM	5974	O	PHE	D	140	−24.127	−42.323	122.089	1.00	31.04		O
ATOM	5975	CB	PHE	D	140	−23.703	−44.333	124.760	1.00	27.13		C
ATOM	5976	CG	PHE	D	140	−23.324	−45.299	123.685	1.00	30.02		C
ATOM	5977	CD1	PHE	D	140	−24.068	−46.450	123.482	1.00	29.03		C
ATOM	5978	CD2	PHE	D	140	−22.224	−45.059	122.868	1.00	27.79		C
ATOM	5979	CE1	PHE	D	140	−23.724	−47.344	122.477	1.00	28.63		C
ATOM	5980	CE2	PHE	D	140	−21.869	−45.950	121.866	1.00	25.04		C
ATOM	5981	CZ	PHE	D	140	−22.619	−47.090	121.666	1.00	25.93		C
ATOM	5982	N	TYR	D	141	−23.033	−41.452	123.855	1.00	27.31		N
ATOM	5983	CA	TYR	D	141	−22.138	−40.640	123.059	1.00	29.62		C
ATOM	5984	C	TYR	D	141	−20.895	−40.416	123.882	1.00	30.14		C
ATOM	5985	O	TYR	D	141	−21.002	−40.131	125.060	1.00	31.98		O
ATOM	5986	CB	TYR	D	141	−22.777	−39.292	122.657	1.00	30.01		C
ATOM	5987	CG	TYR	D	141	−21.868	−38.536	121.719	1.00	28.91		C
ATOM	5988	CD1	TYR	D	141	−21.906	−38.764	120.356	1.00	24.75		C
ATOM	5989	CD2	TYR	D	141	−20.915	−37.652	122.207	1.00	33.08		C
ATOM	5990	CE1	TYR	D	141	−21.055	−38.124	119.505	1.00	27.43		C
ATOM	5991	CE2	TYR	D	141	−20.049	−36.991	121.353	1.00	32.86		C
ATOM	5992	CZ	TYR	D	141	−20.123	−37.233	119.999	1.00	31.49		C
ATOM	5993	OH	TYR	D	141	−19.254	−36.584	119.149	1.00	29.36		O
ATOM	5994	N	PRO	D	142	−19.704	−40.530	123.272	1.00	33.14		N
ATOM	5995	CA	PRO	D	142	−19.424	−40.777	121.853	1.00	31.33		C
ATOM	5996	C	PRO	D	142	−19.435	−42.241	121.404	1.00	31.01		C
ATOM	5997	O	PRO	D	142	−19.806	−43.143	122.140	1.00	30.96		O
ATOM	5998	CB	PRO	D	142	−18.028	−40.201	121.691	1.00	27.46		C
ATOM	5999	CG	PRO	D	142	−17.393	−40.495	123.007	1.00	28.61		C
ATOM	6000	CD	PRO	D	142	−18.464	−40.243	124.019	1.00	27.72		C
ATOM	6001	N	ARG	D	143	−18.974	−42.430	120.167	1.00	35.41		N
ATOM	6002	CA	ARG	D	143	−19.142	−43.686	119.441	1.00	32.43		C
ATOM	6003	C	ARG	D	143	−18.410	−44.842	120.111	1.00	35.51		C
ATOM	6004	O	ARG	D	143	−18.897	−45.974	120.120	1.00	39.91		O
ATOM	6005	CB	ARG	D	143	−18.633	−43.477	118.018	1.00	36.16		C
ATOM	6006	CG	ARG	D	143	−18.522	−44.686	117.126	1.00	44.24		C
ATOM	6007	CD	ARG	D	143	−19.818	−44.835	116.397	1.00	40.17		C
ATOM	6008	NE	ARG	D	143	−19.792	−45.523	115.101	1.00	38.57		N
ATOM	6009	CZ	ARG	D	143	−19.299	−46.736	114.883	1.00	38.79		C
ATOM	6010	NH1	ARG	D	143	−18.689	−47.407	115.852	1.00	42.03		N1+
ATOM	6011	NH2	ARG	D	143	−19.395	−47.265	113.675	1.00	43.44		N
ATOM	6012	N	GLU	D	144	−17.256	−44.580	120.697	1.00	31.31		N
ATOM	6013	CA	GLU	D	144	−16.406	−45.662	121.160	1.00	30.73		C
ATOM	6014	C	GLU	D	144	−16.975	−46.318	122.418	1.00	29.58		C
ATOM	6015	O	GLU	D	144	−17.308	−45.649	123.397	1.00	32.43		O
ATOM	6016	CB	GLU	D	144	−14.994	−45.126	121.391	1.00	28.89		C
ATOM	6017	CG	GLU	D	144	−14.361	−44.583	120.090	1.00	45.09		C
ATOM	6018	CD	GLU	D	144	−14.920	−43.198	119.638	1.00	55.20		C
ATOM	6019	OE1	GLU	D	144	−15.083	−42.301	120.513	1.00	49.33		O
ATOM	6020	OE2	GLU	D	144	−15.215	−43.020	118.417	1.00	49.10		O1−
ATOM	6021	N	ALA	D	145	−17.065	−47.640	122.396	1.00	25.69		N
ATOM	6022	CA	ALA	D	145	−17.552	−48.390	123.535	1.00	29.57		C
ATOM	6023	C	ALA	D	145	−16.972	−49.792	123.452	1.00	31.44		C
ATOM	6024	O	ALA	D	145	−16.702	−50.304	122.364	1.00	37.00		O
ATOM	6025	CB	ALA	D	145	−19.095	−48.415	123.584	1.00	25.18		C
ATOM	6026	N	LYS	D	146	−16.792	−50.416	124.607	1.00	31.28		N
ATOM	6027	CA	LYS	D	146	−16.278	−51.775	124.678	1.00	35.67		C
ATOM	6028	C	LYS	D	146	−17.308	−52.687	125.339	1.00	38.62		C
ATOM	6029	O	LYS	D	146	−17.790	−52.390	126.436	1.00	36.49		O
ATOM	6030	CB	LYS	D	146	−14.972	−51.810	125.466	1.00	33.50		C
ATOM	6031	CG	LYS	D	146	−14.242	−53.136	125.440	1.00	40.82		C
ATOM	6032	CD	LYS	D	146	−12.883	−53.049	126.167	1.00	52.07		C
ATOM	6033	CE	LYS	D	146	−12.130	−54.385	126.127	1.00	60.61		C
ATOM	6034	NZ	LYS	D	146	−10.663	−54.265	126.375	1.00	71.34		N1+
ATOM	6035	N	VAL	D	147	−17.649	−53.786	124.663	1.00	35.29		N
ATOM	6036	CA	VAL	D	147	−18.415	−54.883	125.242	1.00	37.00		C
ATOM	6037	C	VAL	D	147	−17.443	−56.024	125.497	1.00	36.93		C
ATOM	6038	O	VAL	D	147	−16.711	−56.436	124.593	1.00	43.76		O
ATOM	6039	CB	VAL	D	147	−19.568	−55.348	124.331	1.00	32.86		C
ATOM	6040	CG1	VAL	D	147	−20.166	−56.646	124.849	1.00	30.69		C
ATOM	6041	CG2	VAL	D	147	−20.638	−54.322	124.288	1.00	31.55		C
ATOM	6042	N	GLN	D	148	−17.443	−56.529	126.720	1.00	35.29		N
ATOM	6043	CA	GLN	D	148	−16.699	−57.714	127.106	1.00	36.02		C
ATOM	6044	C	GLN	D	148	−17.719	−58.707	127.647	1.00	37.18		C
ATOM	6045	O	GLN	D	148	−18.459	−58.386	128.579	1.00	35.76		O
ATOM	6046	CB	GLN	D	148	−15.637	−57.350	128.153	1.00	38.02		C
ATOM	6047	CG	GLN	D	148	−14.870	−58.512	128.744	1.00	45.95		C
ATOM	6048	CD	GLN	D	148	−13.798	−59.062	127.806	1.00	52.43		C
ATOM	6049	OE1	GLN	D	148	−13.806	−60.255	127.467	1.00	49.60		O
ATOM	6050	NE2	GLN	D	148	−12.857	−58.196	127.398	1.00	47.07		N
ATOM	6051	N	TRP	D	149	−17.787	−59.886	127.037	1.00	36.10		N
ATOM	6052	CA	TRP	D	149	−18.680	−60.955	127.473	1.00	37.96		C
ATOM	6053	C	TRP	D	149	−17.977	−61.861	128.481	1.00	35.95		C
ATOM	6054	O	TRP	D	149	−16.799	−62.191	128.318	1.00	37.64		O
ATOM	6055	CB	TRP	D	149	−19.142	−61.800	126.281	1.00	33.14		C
ATOM	6056	CG	TRP	D	149	−20.226	−61.240	125.409	1.00	34.49		C
ATOM	6057	CD1	TRP	D	149	−20.083	−60.721	124.147	1.00	33.46		C
ATOM	6058	CD2	TRP	D	149	−21.630	−61.200	125.697	1.00	36.39		C
ATOM	6059	NE1	TRP	D	149	−21.301	−60.343	123.643	1.00	29.56		N
ATOM	6060	CE2	TRP	D	149	−22.272	−60.620	124.571	1.00	33.79		C
ATOM	6061	CE3	TRP	D	149	−22.406	−61.584	126.795	1.00	31.81		C
ATOM	6062	CZ2	TRP	D	149	−23.653	−60.408	124.518	1.00	28.35		C
ATOM	6063	CZ3	TRP	D	149	−23.777	−61.367	126.741	1.00	37.34		C
ATOM	6064	CH2	TRP	D	149	−24.385	−60.787	125.607	1.00	31.64		C
ATOM	6065	N	LYS	D	150	−18.700	−62.265	129.526	1.00	35.84		N
ATOM	6066	CA	LYS	D	150	−18.195	−63.242	130.494	1.00	39.20		C
ATOM	6067	C	LYS	D	150	−19.214	−64.355	130.710	1.00	34.68		C
ATOM	6068	O	LYS	D	150	−20.391	−64.086	130.979	1.00	33.70		O
ATOM	6069	CB	LYS	D	150	−17.856	−62.579	131.831	1.00	29.07		C
ATOM	6070	CG	LYS	D	150	−16.601	−61.761	131.779	1.00	33.89		C
ATOM	6071	CD	LYS	D	150	−16.602	−60.781	132.911	1.00	41.07		C
ATOM	6072	CE	LYS	D	150	−15.607	−59.667	132.710	1.00	43.52		C
ATOM	6073	NZ	LYS	D	150	−15.402	−58.953	134.001	1.00	45.35		N1+
ATOM	6074	N	VAL	D	151	−18.756	−65.597	130.594	1.00	30.40		N
ATOM	6075	CA	VAL	D	151	−19.524	−66.777	130.977	1.00	36.11		C
ATOM	6076	C	VAL	D	151	−18.820	−67.400	132.176	1.00	36.89		C
ATOM	6077	O	VAL	D	151	−17.662	−67.816	132.061	1.00	34.20		O
ATOM	6078	CB	VAL	D	151	−19.637	−67.786	129.825	1.00	37.15		C
ATOM	6079	CG1	VAL	D	151	−20.568	−68.901	130.211	1.00	34.22		C
ATOM	6080	CG2	VAL	D	151	−20.111	−67.106	128.549	1.00	38.38		C
ATOM	6081	N	ASP	D	152	−19.508	−67.435	133.333	1.00	40.45		N
ATOM	6082	CA	ASP	D	152	−18.928	−67.863	134.626	1.00	35.46		C
ATOM	6083	C	ASP	D	152	−17.564	−67.218	134.854	1.00	37.61		C
ATOM	6084	O	ASP	D	152	−16.602	−67.868	135.265	1.00	40.92		O
ATOM	6085	CB	ASP	D	152	−18.833	−69.391	134.739	1.00	34.39		C
ATOM	6086	CG	ASP	D	152	−20.200	−70.051	134.992	1.00	43.58		C
ATOM	6087	OD1	ASP	D	152	−21.057	−69.424	135.659	1.00	44.13		O
ATOM	6088	OD2	ASP	D	152	−20.411	−71.206	134.549	1.00	44.21		O1−
ATOM	6089	N	ASN	D	153	−17.493	−65.920	134.560	1.00	36.04		N
ATOM	6090	CA	ASN	D	153	−16.305	−65.088	134.682	1.00	34.97		C
ATOM	6091	C	ASN	D	153	−15.188	−65.521	133.737	1.00	37.78		C
ATOM	6092	O	ASN	D	153	−14.015	−65.140	133.922	1.00	36.32		O
ATOM	6093	CB	ASN	D	153	−15.802	−65.009	136.126	1.00	33.76		C
ATOM	6094	CG	ASN	D	153	−15.114	−63.678	136.417	1.00	42.55		C
ATOM	6095	OD1	ASN	D	153	−15.704	−62.598	136.248	1.00	42.84		O
ATOM	6096	ND2	ASN	D	153	−13.853	−63.747	136.831	1.00	46.83		N
ATOM	6097	N	ALA	D	154	−15.521	−66.293	132.706	1.00	34.52		N
ATOM	6098	CA	ALA	D	154	−14.577	−66.555	131.629	1.00	35.50		C
ATOM	6099	C	ALA	D	154	−14.784	−65.526	130.521	1.00	38.64		C
ATOM	6100	O	ALA	D	154	−15.880	−65.417	129.954	1.00	35.76		O
ATOM	6101	CB	ALA	D	154	−14.727	−67.973	131.090	1.00	31.21		C
ATOM	6102	N	LEU	D	155	−13.725	−64.775	130.223	1.00	39.22		N
ATOM	6103	CA	LEU	D	155	−13.728	−63.839	129.108	1.00	34.49		C
ATOM	6104	C	LEU	D	155	−13.970	−64.578	127.815	1.00	31.95		C
ATOM	6105	O	LEU	D	155	−13.276	−65.550	127.518	1.00	33.49		O
ATOM	6106	CB	LEU	D	155	−12.391	−63.125	129.038	1.00	36.99		C
ATOM	6107	CG	LEU	D	155	−12.350	−61.800	129.779	1.00	48.06		C
ATOM	6108	CD1	LEU	D	155	−12.181	−62.015	131.301	1.00	43.48		C
ATOM	6109	CD2	LEU	D	155	−11.219	−60.978	129.190	1.00	51.82		C
ATOM	6110	N	GLN	D	156	−14.996	−64.166	127.080	1.00	36.40		N
ATOM	6111	CA	GLN	D	156	−15.212	−64.660	125.725	1.00	35.33		C
ATOM	6112	C	GLN	D	156	−14.505	−63.750	124.725	1.00	31.08		C
ATOM	6113	O	GLN	D	156	−14.665	−62.526	124.763	1.00	36.72		O
ATOM	6114	CB	GLN	D	156	−16.703	−64.738	125.398	1.00	32.10		C
ATOM	6115	CG	GLN	D	156	−17.523	−65.447	126.450	1.00	35.66		C
ATOM	6116	CD	GLN	D	156	−17.059	−66.878	126.701	1.00	36.63		C
ATOM	6117	OE1	GLN	D	156	−17.090	−67.722	125.804	1.00	31.49		O
ATOM	6118	NE2	GLN	D	156	−16.638	−67.153	127.929	1.00	35.80		N
ATOM	6119	N	SER	D	157	−13.790	−64.354	123.795	1.00	24.35		N
ATOM	6120	CA	SER	D	157	−13.068	−63.629	122.758	1.00	27.71		C
ATOM	6121	C	SER	D	157	−13.201	−64.434	121.474	1.00	29.57		C
ATOM	6122	O	SER	D	157	−12.715	−65.562	121.405	1.00	31.81		O
ATOM	6123	CB	SER	D	157	−11.607	−63.449	123.142	1.00	27.38		C
ATOM	6124	OG	SER	D	157	−10.897	−62.800	122.115	1.00	32.95		O
ATOM	6125	N	GLY	D	158	−13.880	−63.886	120.474	1.00	25.60		N
ATOM	6126	CA	GLY	D	158	−13.995	−64.518	119.171	1.00	23.02		C
ATOM	6127	C	GLY	D	158	−15.329	−65.156	118.862	1.00	31.71		C
ATOM	6128	O	GLY	D	158	−15.544	−65.567	117.710	1.00	30.83		O
ATOM	6129	N	ASN	D	159	−16.253	−65.223	119.824	1.00	28.19		N
ATOM	6130	CA	ASN	D	159	−17.529	−65.872	119.572	1.00	22.12		C
ATOM	6131	C	ASN	D	159	−18.686	−64.886	119.660	1.00	25.52		C
ATOM	6132	O	ASN	D	159	−19.803	−65.268	120.002	1.00	26.86		O
ATOM	6133	CB	ASN	D	159	−17.749	−67.054	120.516	1.00	25.99		C
ATOM	6134	CG	ASN	D	159	−17.495	−66.712	121.997	1.00	31.94		C
ATOM	6135	OD1	ASN	D	159	−17.103	−65.589	122.345	1.00	28.21		O
ATOM	6136	ND2	ASN	D	159	−17.712	−67.706	122.875	1.00	27.51		N
ATOM	6137	N	SER	D	160	−18.445	−63.625	119.295	1.00	27.33		N
ATOM	6138	CA	SER	D	160	−19.484	−62.606	119.297	1.00	26.68		C
ATOM	6139	C	SER	D	160	−19.310	−61.677	118.099	1.00	24.99		C
ATOM	6140	O	SER	D	160	−18.224	−61.571	117.525	1.00	29.23		O
ATOM	6141	CB	SER	D	160	−19.475	−61.812	120.614	1.00	27.08		C
ATOM	6142	OG	SER	D	160	−18.327	−61.009	120.707	1.00	26.36		O
ATOM	6143	N	GLN	D	161	−20.407	−61.024	117.708	1.00	24.70		N
ATOM	6144	CA	GLN	D	161	−20.404	−59.998	116.667	1.00	24.60		C
ATOM	6145	C	GLN	D	161	−21.192	−58.766	117.128	1.00	29.81		C
ATOM	6146	O	GLN	D	161	−21.972	−58.818	118.082	1.00	31.67		O
ATOM	6147	CB	GLN	D	161	−20.954	−60.560	115.380	1.00	22.23		C
ATOM	6148	CG	GLN	D	161	−20.025	−61.563	114.752	1.00	24.29		C
ATOM	6149	CD	GLN	D	161	−20.631	−62.200	113.532	1.00	27.64		C
ATOM	6150	OE1	GLN	D	161	−21.466	−63.098	113.629	1.00	32.76		O
ATOM	6151	NE2	GLN	D	161	−20.246	−61.717	112.372	1.00	23.06		N
ATOM	6152	N	GLU	D	162	−20.965	−57.641	116.458	1.00	30.47		N
ATOM	6153	CA	GLU	D	162	−21.462	−56.341	116.919	1.00	34.77		C
ATOM	6154	C	GLU	D	162	−21.983	−55.478	115.772	1.00	30.23		C
ATOM	6155	O	GLU	D	162	−21.425	−55.485	114.678	1.00	26.52		O
ATOM	6156	CB	GLU	D	162	−20.360	−55.528	117.568	1.00	32.41		C
ATOM	6157	CG	GLU	D	162	−20.266	−55.519	119.031	1.00	32.77		C
ATOM	6158	CD	GLU	D	162	−19.053	−54.695	119.437	1.00	41.06		C
ATOM	6159	OE1	GLU	D	162	−18.443	−54.075	118.530	1.00	38.20		O
ATOM	6160	OE2	GLU	D	162	−18.704	−54.667	120.637	1.00	50.77		O1−
ATOM	6161	N	SER	D	163	−22.953	−54.617	116.084	1.00	27.60		N
ATOM	6162	CA	SER	D	163	−23.426	−53.583	115.170	1.00	27.13		C
ATOM	6163	C	SER	D	163	−23.656	−52.284	115.923	1.00	25.97		C
ATOM	6164	O	SER	D	163	−24.105	−52.299	117.068	1.00	26.91		O
ATOM	6165	CB	SER	D	163	−24.781	−53.931	114.531	1.00	29.47		C
ATOM	6166	OG	SER	D	163	−24.662	−54.692	113.366	1.00	32.02		O
ATOM	6167	N	VAL	D	164	−23.422	−51.161	115.243	1.00	20.54		N
ATOM	6168	CA	VAL	D	164	−23.727	−49.843	115.781	1.00	23.87		C
ATOM	6169	C	VAL	D	164	−24.632	−49.109	114.794	1.00	25.79		C
ATOM	6170	O	VAL	D	164	−24.411	−49.146	113.580	1.00	28.96		O
ATOM	6171	CB	VAL	D	164	−22.451	−49.022	116.079	1.00	27.40		C
ATOM	6172	CG1	VAL	D	164	−22.804	−47.685	116.731	1.00	26.22		C
ATOM	6173	CG2	VAL	D	164	−21.543	−49.782	116.997	1.00	25.86		C
ATOM	6174	N	THR	D	165	−25.645	−48.432	115.318	1.00	22.06		N
ATOM	6175	CA	THR	D	165	−26.530	−47.661	114.471	1.00	26.12		C
ATOM	6176	C	THR	D	165	−25.845	−46.376	113.991	1.00	27.66		C
ATOM	6177	O	THR	D	165	−24.781	−45.984	114.468	1.00	24.77		O
ATOM	6178	CB	THR	D	165	−27.813	−47.311	115.216	1.00	27.08		C
ATOM	6179	OG1	THR	D	165	−27.482	−46.765	116.504	1.00	27.47		O
ATOM	6180	CG2	THR	D	165	−28.688	−48.544	115.355	1.00	26.44		C
ATOM	6181	N	GLU	D	166	−26.479	−45.719	113.023	1.00	27.00		N
ATOM	6182	CA	GLU	D	166	−26.079	−44.370	112.686	1.00	27.71		C
ATOM	6183	C	GLU	D	166	−26.495	−43.432	113.817	1.00	33.03		C
ATOM	6184	O	GLU	D	166	−27.359	−43.761	114.640	1.00	33.28		O
ATOM	6185	CB	GLU	D	166	−26.689	−43.951	111.339	1.00	30.38		C
ATOM	6186	CG	GLU	D	166	−26.119	−44.711	110.120	1.00	25.40		C
ATOM	6187	CD	GLU	D	166	−24.599	−44.606	110.040	1.00	38.65		C
ATOM	6188	OE1	GLU	D	166	−24.038	−43.552	110.423	1.00	46.73		O
ATOM	6189	OE2	GLU	D	166	−23.946	−45.597	109.652	1.00	40.23		O1−
ATOM	6190	N	GLN	D	167	−25.866	−42.254	113.856	1.00	29.35		N
ATOM	6191	CA	GLN	D	167	−26.181	−41.280	114.885	1.00	27.68		C
ATOM	6192	C	GLN	D	167	−27.675	−40.977	114.888	1.00	30.18		C
ATOM	6193	O	GLN	D	167	−28.273	−40.743	113.841	1.00	28.88		O
ATOM	6194	CB	GLN	D	167	−25.371	−40.014	114.663	1.00	26.86		C
ATOM	6195	CG	GLN	D	167	−25.050	−39.318	115.952	1.00	30.75		C
ATOM	6196	CD	GLN	D	167	−24.012	−38.230	115.810	1.00	30.88		C
ATOM	6197	OE1	GLN	D	167	−23.630	−37.851	114.707	1.00	26.28		O
ATOM	6198	NE2	GLN	D	167	−23.526	−37.741	116.942	1.00	31.17		N
ATOM	6199	N	ASP	D	168	−28.284	−40.993	116.073	1.00	32.93		N
ATOM	6200	CA	ASP	D	168	−29.740	−40.995	116.145	1.00	30.89		C
ATOM	6201	C	ASP	D	168	−30.322	−39.647	115.730	1.00	32.78		C
ATOM	6202	O	ASP	D	168	−29.864	−38.588	116.175	1.00	32.90		O
ATOM	6203	CB	ASP	D	168	−30.198	−41.372	117.553	1.00	31.28		C
ATOM	6204	CG	ASP	D	168	−31.716	−41.521	117.659	1.00	38.67		C
ATOM	6205	OD2	ASP	D	168	−32.352	−40.708	118.357	1.00	38.36		O
ATOM	6206	OD1	ASP	D	168	−32.272	−42.488	117.088	1.00	46.18		O1−
ATOM	6207	N	SER	D	169	−31.354	−39.697	114.883	1.00	39.01		N
ATOM	6208	CA	SER	D	169	−31.955	−38.482	114.346	1.00	32.75		C
ATOM	6209	C	SER	D	169	−32.582	−37.588	115.413	1.00	37.05		C
ATOM	6210	O	SER	D	169	−32.812	−36.404	115.145	1.00	38.37		O
ATOM	6211	CB	SER	D	169	−33.001	−38.845	113.284	1.00	39.20		C
ATOM	6212	OG	SER	D	169	−34.079	−39.588	113.824	1.00	50.23		O
ATOM	6213	N	LYS	D	170	−32.814	−38.077	116.629	1.00	34.51		N
ATOM	6214	CA	LYS	D	170	−33.421	−37.203	117.625	1.00	34.07		C
ATOM	6215	C	LYS	D	170	−32.468	−36.701	118.701	1.00	33.50		C
ATOM	6216	O	LYS	D	170	−32.589	−35.552	119.108	1.00	37.46		O
ATOM	6217	CB	LYS	D	170	−34.629	−37.888	118.275	1.00	37.63		C
ATOM	6218	CG	LYS	D	170	−35.389	−37.006	119.243	1.00	37.03		C
ATOM	6219	CD	LYS	D	170	−36.331	−37.786	120.178	1.00	38.46		C
ATOM	6220	CE	LYS	D	170	−37.575	−38.283	119.424	1.00	45.87		C
ATOM	6221	NZ	LYS	D	170	−38.639	−38.916	120.302	1.00	39.82		N1+
ATOM	6222	N	ASP	D	171	−31.531	−37.506	119.210	1.00	36.72		N
ATOM	6223	CA	ASP	D	171	−30.652	−37.034	120.285	1.00	30.44		C
ATOM	6224	C	ASP	D	171	−29.163	−37.175	119.956	1.00	31.83		C
ATOM	6225	O	ASP	D	171	−28.327	−37.027	120.864	1.00	24.40		O
ATOM	6226	CB	ASP	D	171	−30.977	−37.745	121.621	1.00	24.58		C
ATOM	6227	CG	ASP	D	171	−30.724	−39.290	121.598	1.00	37.38		C
ATOM	6228	OD1	ASP	D	171	−29.900	−39.800	120.803	1.00	38.28		O
ATOM	6229	OD2	ASP	D	171	−31.345	−40.026	122.402	1.00	44.17		O1−
ATOM	6230	N	SER	D	172	−28.814	−37.467	118.691	1.00	27.49		N
ATOM	6231	CA	SER	D	172	−27.433	−37.542	118.210	1.00	29.50		C
ATOM	6232	C	SER	D	172	−26.575	−38.575	118.954	1.00	33.88		C
ATOM	6233	O	SER	D	172	−25.339	−38.428	119.009	1.00	32.88		O
ATOM	6234	CB	SER	D	172	−26.756	−36.167	118.283	1.00	28.79		C
ATOM	6235	OG	SER	D	172	−27.503	−35.209	117.557	1.00	32.16		O
ATOM	6236	N	THR	D	173	−27.185	−39.602	119.550	1.00	25.27		N
ATOM	6237	CA	THR	D	173	−26.443	−40.663	120.214	1.00	26.81		C
ATOM	6238	C	THR	D	173	−26.265	−41.868	119.287	1.00	28.18		C
ATOM	6239	O	THR	D	173	−26.791	−41.932	118.163	1.00	26.72		O
ATOM	6240	CB	THR	D	173	−27.127	−41.101	121.529	1.00	29.20		C
ATOM	6241	OG1	THR	D	173	−28.454	−41.578	121.279	1.00	26.42		O
ATOM	6242	CG2	THR	D	173	−27.181	−39.948	122.547	1.00	27.06		C
ATOM	6243	N	TYR	D	174	−25.492	−42.824	119.787	1.00	24.11		N
ATOM	6244	CA	TYR	D	174	−25.252	−44.113	119.162	1.00	25.18		C
ATOM	6245	C	TYR	D	174	−25.858	−45.225	120.001	1.00	27.09		C
ATOM	6246	O	TYR	D	174	−25.925	−45.130	121.232	1.00	26.92		O
ATOM	6247	CB	TYR	D	174	−23.740	−44.371	118.993	1.00	24.71		C
ATOM	6248	CG	TYR	D	174	−23.145	−43.461	117.980	1.00	27.06		C
ATOM	6249	CD1	TYR	D	174	−23.212	−43.778	116.625	1.00	23.86		C
ATOM	6250	CD2	TYR	D	174	−22.587	−42.234	118.355	1.00	29.38		C
ATOM	6251	CE1	TYR	D	174	−22.697	−42.931	115.671	1.00	28.55		C
ATOM	6252	CE2	TYR	D	174	−22.060	−41.366	117.397	1.00	28.07		C
ATOM	6253	CZ	TYR	D	174	−22.125	−41.719	116.053	1.00	30.70		C
ATOM	6254	OH	TYR	D	174	−21.626	−40.882	115.081	1.00	29.66		O
ATOM	6255	N	SER	D	175	−26.220	−46.318	119.329	1.00	29.12		N
ATOM	6256	CA	SER	D	175	−26.623	−47.546	120.005	1.00	29.70		C
ATOM	6257	C	SER	D	175	−25.851	−48.723	119.437	1.00	27.77		C
ATOM	6258	O	SER	D	175	−25.515	−48.748	118.252	1.00	26.37		O
ATOM	6259	CB	SER	D	175	−28.127	−47.796	119.868	1.00	28.32		C
ATOM	6260	OG	SER	D	175	−28.822	−46.950	120.755	1.00	29.89		O
ATOM	6261	N	LEU	D	176	−25.615	−49.725	120.284	1.00	29.44		N
ATOM	6262	CA	LEU	D	176	−24.808	−50.884	119.918	1.00	26.61		C
ATOM	6263	C	LEU	D	176	−25.499	−52.174	120.346	1.00	25.01		C
ATOM	6264	O	LEU	D	176	−26.055	−52.255	121.444	1.00	25.06		O
ATOM	6265	CB	LEU	D	176	−23.412	−50.791	120.557	1.00	23.61		C
ATOM	6266	CG	LEU	D	176	−22.361	−51.831	120.176	1.00	26.86		C
ATOM	6267	CD1	LEU	D	176	−20.995	−51.225	120.278	1.00	28.36		C
ATOM	6268	CD2	LEU	D	176	−22.428	−53.052	121.099	1.00	25.35		C
ATOM	6269	N	SER	D	177	−25.405	−53.202	119.500	1.00	26.18		N
ATOM	6270	CA	SER	D	177	−25.932	−54.536	119.789	1.00	25.92		C
ATOM	6271	C	SER	D	177	−24.840	−55.587	119.589	1.00	25.55		C
ATOM	6272	O	SER	D	177	−24.136	−55.566	118.577	1.00	30.42		O
ATOM	6273	CB	SER	D	177	−27.142	−54.840	118.895	1.00	30.52		C
ATOM	6274	OG	SER	D	177	−27.570	−56.176	119.035	1.00	31.20		O
ATOM	6275	N	SER	D	178	−24.668	−56.474	120.574	1.00	28.18		N
ATOM	6276	CA	SER	D	178	−23.659	−57.527	120.542	1.00	25.27		C
ATOM	6277	C	SER	D	178	−24.288	−58.885	120.794	1.00	26.75		C
ATOM	6278	O	SER	D	178	−25.102	−59.040	121.705	1.00	31.18		O
ATOM	6279	CB	SER	D	178	−22.560	−57.312	121.568	1.00	30.71		C
ATOM	6280	OG	SER	D	178	−21.592	−58.348	121.447	1.00	32.24		O
ATOM	6281	N	THR	D	179	−23.888	−59.880	120.010	1.00	27.93		N
ATOM	6282	CA	THR	D	179	−24.458	−61.220	120.122	1.00	29.75		C
ATOM	6283	C	THR	D	179	−23.379	−62.248	120.444	1.00	31.38		C
ATOM	6284	O	THR	D	179	−22.529	−62.546	119.604	1.00	25.41		O
ATOM	6285	CB	THR	D	179	−25.160	−61.608	118.837	1.00	32.19		C
ATOM	6286	OG1	THR	D	179	−26.110	−60.586	118.488	1.00	42.39		O
ATOM	6287	CG2	THR	D	179	−25.841	−62.933	119.026	1.00	33.94		C
ATOM	6288	N	LEU	D	180	−23.448	−62.822	121.641	1.00	33.64		N
ATOM	6289	CA	LEU	D	180	−22.651	−63.988	121.989	1.00	26.84		C
ATOM	6290	C	LEU	D	180	−23.377	−65.233	121.509	1.00	28.96		C
ATOM	6291	O	LEU	D	180	−24.576	−65.383	121.759	1.00	33.24		O
ATOM	6292	CB	LEU	D	180	−22.446	−64.042	123.496	1.00	26.91		C
ATOM	6293	CG	LEU	D	180	−21.584	−65.169	124.035	1.00	32.83		C
ATOM	6294	CD1	LEU	D	180	−20.179	−64.954	123.541	1.00	32.39		C
ATOM	6295	CD2	LEU	D	180	−21.624	−65.196	125.566	1.00	35.83		C
ATOM	6296	N	THR	D	181	−22.683	−66.101	120.784	1.00	24.60		N
ATOM	6297	CA	THR	D	181	−23.289	−67.321	120.267	1.00	29.40		C
ATOM	6298	C	THR	D	181	−22.656	−68.546	120.928	1.00	35.38		C
ATOM	6299	O	THR	D	181	−21.430	−68.622	121.063	1.00	32.82		O
ATOM	6300	CB	THR	D	181	−23.162	−67.393	118.744	1.00	29.01		C
ATOM	6301	OG1	THR	D	181	−23.762	−66.235	118.169	1.00	36.58		O
ATOM	6302	CG2	THR	D	181	−23.943	−68.571	118.214	1.00	35.08		C
ATOM	6303	N	LEU	D	182	−23.499	−69.481	121.375	1.00	33.54		N
ATOM	6304	CA	LEU	D	182	−23.061	−70.743	121.957	1.00	31.73		C
ATOM	6305	C	LEU	D	182	−23.908	−71.860	121.379	1.00	38.06		C
ATOM	6306	O	LEU	D	182	−25.010	−71.638	120.866	1.00	39.76		O
ATOM	6307	CB	LEU	D	182	−23.242	−70.791	123.473	1.00	34.20		C
ATOM	6308	CG	LEU	D	182	−22.667	−69.731	124.395	1.00	37.93		C
ATOM	6309	CD1	LEU	D	182	−23.089	−70.021	125.827	1.00	39.29		C
ATOM	6310	CD2	LEU	D	182	−21.154	−69.692	124.276	1.00	41.23		C
ATOM	6311	N	SER	D	183	−23.401	−73.075	121.491	1.00	41.78		N
ATOM	6312	CA	SER	D	183	−24.276	−74.218	121.302	1.00	41.97		C
ATOM	6313	C	SER	D	183	−25.171	−74.354	122.533	1.00	40.93		C
ATOM	6314	O	SER	D	183	−24.832	−73.874	123.619	1.00	39.70		O
ATOM	6315	CB	SER	D	183	−23.449	−75.481	121.071	1.00	42.62		C
ATOM	6316	OG	SER	D	183	−22.677	−75.783	122.224	1.00	45.39		O
ATOM	6317	N	LYS	D	184	−26.323	−75.017	122.368	1.00	38.98		N
ATOM	6318	CA	LYS	D	184	−27.172	−75.267	123.536	1.00	46.77		C
ATOM	6319	C	LYS	D	184	−26.428	−76.067	124.602	1.00	45.69		C
ATOM	6320	O	LYS	D	184	−26.586	−75.820	125.806	1.00	44.13		O
ATOM	6321	CB	LYS	D	184	−28.465	−75.982	123.135	1.00	52.78		C
ATOM	6322	CG	LYS	D	184	−29.383	−76.279	124.334	1.00	45.82		C
ATOM	6323	CD	LYS	D	184	−30.721	−76.916	123.925	1.00	49.11		C
ATOM	6324	CE	LYS	D	184	−30.567	−78.342	123.414	1.00	56.53		C
ATOM	6325	NZ	LYS	D	184	−31.811	−78.834	122.761	1.00	58.33		N1+
ATOM	6326	N	ALA	D	185	−25.599	−77.019	124.172	1.00	44.49		N
ATOM	6327	CA	ALA	D	185	−24.835	−77.822	125.116	1.00	44.16		C
ATOM	6328	C	ALA	D	185	−23.903	−76.953	125.958	1.00	46.66		C
ATOM	6329	O	ALA	D	185	−23.932	−77.018	127.193	1.00	48.01		O
ATOM	6330	CB	ALA	D	185	−24.067	−78.902	124.363	1.00	43.48		C
ATOM	6331	N	ASP	D	186	−23.057	−76.142	125.307	1.00	47.56		N
ATOM	6332	CA	ASP	D	186	−22.203	−75.208	126.042	1.00	43.67		C
ATOM	6333	C	ASP	D	186	−23.040	−74.263	126.887	1.00	41.82		C
ATOM	6334	O	ASP	D	186	−22.744	−74.029	128.065	1.00	43.44		O
ATOM	6335	CB	ASP	D	186	−21.334	−74.400	125.079	1.00	47.25		C
ATOM	6336	CG	ASP	D	186	−20.218	−75.210	124.472	1.00	49.80		C
ATOM	6337	OD1	ASP	D	186	−19.524	−75.925	125.218	1.00	51.32		O
ATOM	6338	OD2	ASP	D	186	−20.038	−75.131	123.241	1.00	59.81		O1−
ATOM	6339	N	TYR	D	187	−24.100	−73.713	126.296	1.00	42.10		N
ATOM	6340	CA	TYR	D	187	−24.958	−72.799	127.030	1.00	42.00		C
ATOM	6341	C	TYR	D	187	−25.446	−73.439	128.322	1.00	40.74		C
ATOM	6342	O	TYR	D	187	−25.462	−72.797	129.381	1.00	36.12		O
ATOM	6343	CB	TYR	D	187	−26.148	−72.356	126.154	1.00	35.24		C
ATOM	6344	CG	TYR	D	187	−27.113	−71.482	126.924	1.00	36.73		C
ATOM	6345	CD1	TYR	D	187	−26.712	−70.236	127.403	1.00	33.83		C
ATOM	6346	CD2	TYR	D	187	−28.407	−71.905	127.202	1.00	37.83		C
ATOM	6347	CE1	TYR	D	187	−27.570	−69.443	128.137	1.00	35.37		C
ATOM	6348	CE2	TYR	D	187	−29.278	−71.112	127.932	1.00	36.87		C
ATOM	6349	CZ	TYR	D	187	−28.848	−69.883	128.404	1.00	34.37		C
ATOM	6350	OH	TYR	D	187	−29.704	−69.082	129.125	1.00	33.53		O
ATOM	6351	N	GLU	D	188	−25.818	−74.715	128.266	1.00	44.28		N
ATOM	6352	CA	GLU	D	188	−26.463	−75.311	129.426	1.00	48.57		C
ATOM	6353	C	GLU	D	188	−25.494	−75.827	130.473	1.00	44.50		C
ATOM	6354	O	GLU	D	188	−25.954	−76.294	131.513	1.00	43.86		O
ATOM	6355	CB	GLU	D	188	−27.384	−76.431	128.984	1.00	46.87		C
ATOM	6356	CG	GLU	D	188	−28.803	−75.966	128.881	1.00	52.89		C
ATOM	6357	CD	GLU	D	188	−29.586	−76.862	127.993	1.00	60.48		C
ATOM	6358	OE1	GLU	D	188	−28.963	−77.811	127.472	1.00	63.90		O
ATOM	6359	OE2	GLU	D	188	−30.800	−76.623	127.817	1.00	70.92		O1−
ATOM	6360	N	LYS	D	189	−24.184	−75.709	130.249	1.00	42.21		N
ATOM	6361	CA	LYS	D	189	−23.166	−76.082	131.214	1.00	34.10		C
ATOM	6362	C	LYS	D	189	−22.659	−74.905	132.027	1.00	41.19		C
ATOM	6363	O	LYS	D	189	−21.617	−75.025	132.675	1.00	43.76		O
ATOM	6364	CB	LYS	D	189	−21.981	−76.727	130.501	1.00	42.21		C
ATOM	6365	CG	LYS	D	189	−22.277	−78.025	129.749	1.00	49.04		C
ATOM	6366	CD	LYS	D	189	−21.065	−78.418	128.889	1.00	50.62		C
ATOM	6367	CE	LYS	D	189	−21.332	−79.669	128.071	1.00	61.29		C
ATOM	6368	NZ	LYS	D	189	−20.165	−79.960	127.197	1.00	67.56		N1+
ATOM	6369	N	HIS	D	190	−23.349	−73.768	132.011	1.00	40.38		N
ATOM	6370	CA	HIS	D	190	−22.850	−72.595	132.712	1.00	37.11		C
ATOM	6371	C	HIS	D	190	−24.018	−71.833	133.309	1.00	37.04		C
ATOM	6372	O	HIS	D	190	−25.167	−72.014	132.913	1.00	39.95		O
ATOM	6373	CB	HIS	D	190	−22.044	−71.702	131.782	1.00	41.03		C
ATOM	6374	CG	HIS	D	190	−20.840	−72.376	131.212	1.00	41.24		C
ATOM	6375	ND1	HIS	D	190	−19.759	−72.747	131.983	1.00	41.48		N
ATOM	6376	CD2	HIS	D	190	−20.560	−72.778	129.951	1.00	39.46		C
ATOM	6377	CE1	HIS	D	190	−18.856	−73.333	131.218	1.00	36.30		C
ATOM	6378	NE2	HIS	D	190	−19.320	−73.368	129.981	1.00	39.82		N
ATOM	6379	N	LYS	D	191	−23.719	−70.969	134.270	1.00	34.63		N
ATOM	6380	CA	LYS	D	191	−24.775	−70.340	135.046	1.00	45.76		C
ATOM	6381	C	LYS	D	191	−24.874	−68.842	134.790	1.00	46.36		C
ATOM	6382	O	LYS	D	191	−25.944	−68.357	134.407	1.00	46.07		O
ATOM	6383	CB	LYS	D	191	−24.566	−70.607	136.548	1.00	42.22		C
ATOM	6384	CG	LYS	D	191	−25.568	−69.875	137.451	1.00	49.74		C
ATOM	6385	CD	LYS	D	191	−25.227	−70.029	138.954	1.00	59.90		C
ATOM	6386	CE	LYS	D	191	−26.350	−69.510	139.853	1.00	60.67		C
ATOM	6387	NZ	LYS	D	191	−26.031	−69.671	141.293	1.00	66.07		N1+
ATOM	6388	N	VAL	D	192	−23.782	−68.100	134.968	1.00	39.06		N
ATOM	6389	CA	VAL	D	192	−23.809	−66.644	134.941	1.00	38.75		C
ATOM	6390	C	VAL	D	192	−23.378	−66.173	133.553	1.00	39.96		C
ATOM	6391	O	VAL	D	192	−22.277	−66.490	133.091	1.00	41.97		O
ATOM	6392	CB	VAL	D	192	−22.906	−66.063	136.039	1.00	36.31		C
ATOM	6393	CG1	VAL	D	192	−22.876	−64.544	135.989	1.00	34.38		C
ATOM	6394	CG2	VAL	D	192	−23.360	−66.548	137.380	1.00	41.02		C
ATOM	6395	N	TYR	D	193	−24.241	−65.414	132.886	1.00	38.30		N
ATOM	6396	CA	TYR	D	193	−23.924	−64.789	131.608	1.00	35.90		C
ATOM	6397	C	TYR	D	193	−23.862	−63.290	131.845	1.00	33.90		C
ATOM	6398	O	TYR	D	193	−24.747	−62.734	132.487	1.00	36.52		O
ATOM	6399	CB	TYR	D	193	−24.957	−65.165	130.534	1.00	31.33		C
ATOM	6400	CG	TYR	D	193	−24.828	−66.629	130.183	1.00	35.91		C
ATOM	6401	CD1	TYR	D	193	−25.458	−67.608	130.950	1.00	38.83		C
ATOM	6402	CD2	TYR	D	193	−23.971	−67.049	129.171	1.00	38.88		C
ATOM	6403	CE1	TYR	D	193	−25.297	−68.968	130.671	1.00	36.63		C
ATOM	6404	CE2	TYR	D	193	−23.799	−68.410	128.885	1.00	39.70		C
ATOM	6405	CZ	TYR	D	193	−24.461	−69.359	129.646	1.00	36.21		C
ATOM	6406	OH	TYR	D	193	−24.302	−70.691	129.360	1.00	37.29		O
ATOM	6407	N	ALA	D	194	−22.791	−62.646	131.400	1.00	33.30		N
ATOM	6408	CA	ALA	D	194	−22.654	−61.226	131.670	1.00	34.22		C
ATOM	6409	C	ALA	D	194	−22.000	−60.510	130.488	1.00	36.04		C
ATOM	6410	O	ALA	D	194	−21.164	−61.083	129.782	1.00	35.02		O
ATOM	6411	CB	ALA	D	194	−21.857	−61.026	132.952	1.00	29.25		C
ATOM	6412	N	CYS	D	195	−22.396	−59.254	130.263	1.00	32.88		N
ATOM	6413	CA	CYS	D	195	−21.638	−58.361	129.389	1.00	39.71		C
ATOM	6414	C	CYS	D	195	−21.246	−57.121	130.170	1.00	37.39		C
ATOM	6415	O	CYS	D	195	−22.084	−56.498	130.839	1.00	33.62		O
ATOM	6416	CB	CYS	D	195	−22.382	−57.939	128.108	1.00	39.73		C
ATOM	6417	SG	CYS	D	195	−23.983	−57.183	128.349	1.00	55.69		S
ATOM	6418	N	GLU	D	196	−19.981	−56.753	130.035	1.00	33.07		N
ATOM	6419	CA	GLU	D	196	−19.377	−55.641	130.742	1.00	38.70		C
ATOM	6420	C	GLU	D	196	−19.127	−54.523	129.734	1.00	35.02		C
ATOM	6421	O	GLU	D	196	−18.610	−54.777	128.639	1.00	28.28		O
ATOM	6422	CB	GLU	D	196	−18.078	−56.104	131.410	1.00	35.85		C
ATOM	6423	CG	GLU	D	196	−17.366	−55.070	132.220	1.00	39.77		C
ATOM	6424	CD	GLU	D	196	−15.962	−55.516	132.610	1.00	46.03		C
ATOM	6425	OE1	GLU	D	196	−15.435	−56.465	131.988	1.00	40.61		O
ATOM	6426	OE2	GLU	D	196	−15.373	−54.880	133.511	1.00	57.77		O1−
ATOM	6427	N	VAL	D	197	−19.512	−53.297	130.097	1.00	34.66		N
ATOM	6428	CA	VAL	D	197	−19.563	−52.169	129.169	1.00	35.82		C
ATOM	6429	C	VAL	D	197	−18.595	−51.112	129.680	1.00	34.18		C
ATOM	6430	O	VAL	D	197	−18.751	−50.610	130.797	1.00	35.27		O
ATOM	6431	CB	VAL	D	197	−20.993	−51.601	129.024	1.00	31.64		C
ATOM	6432	CG1	VAL	D	197	−21.014	−50.336	128.159	1.00	28.99		C
ATOM	6433	CG2	VAL	D	197	−21.944	−52.640	128.462	1.00	28.78		C
ATOM	6434	N	THR	D	198	−17.577	−50.805	128.883	1.00	33.99		N
ATOM	6435	CA	THR	D	198	−16.654	−49.718	129.164	1.00	32.70		C
ATOM	6436	C	THR	D	198	−16.983	−48.563	128.229	1.00	40.52		C
ATOM	6437	O	THR	D	198	−17.023	−48.743	127.005	1.00	37.25		O
ATOM	6438	CB	THR	D	198	−15.203	−50.146	128.950	1.00	33.81		C
ATOM	6439	OG1	THR	D	198	−14.907	−51.282	129.766	1.00	43.84		O
ATOM	6440	CG2	THR	D	198	−14.282	−49.029	129.347	1.00	29.60		C
ATOM	6441	N	HIS	D	199	−17.211	−47.384	128.805	1.00	37.58		N
ATOM	6442	CA	HIS	D	199	−17.528	−46.198	128.030	1.00	31.22		C
ATOM	6443	C	HIS	D	199	−17.075	−44.973	128.805	1.00	34.53		C
ATOM	6444	O	HIS	D	199	−17.002	−44.999	130.033	1.00	35.60		O
ATOM	6445	CB	HIS	D	199	−19.020	−46.115	127.723	1.00	33.40		C
ATOM	6446	CG	HIS	D	199	−19.383	−44.969	126.828	1.00	34.76		C
ATOM	6447	ND1	HIS	D	199	−19.824	−43.756	127.313	1.00	30.33		N
ATOM	6448	CD2	HIS	D	199	−19.360	−44.849	125.479	1.00	32.19		C
ATOM	6449	CE1	HIS	D	199	−20.061	−42.940	126.301	1.00	31.06		C
ATOM	6450	NE2	HIS	D	199	−19.778	−43.575	125.178	1.00	31.67		N
ATOM	6451	N	GLN	D	200	−16.786	−43.888	128.085	1.00	29.72		N
ATOM	6452	CA	GLN	D	200	−16.199	−42.738	128.754	1.00	31.37		C
ATOM	6453	C	GLU	D	200	−17.177	−42.022	129.684	1.00	35.36		C
ATOM	6454	O	GLN	D	200	−16.735	−41.248	130.541	1.00	42.18		O
ATOM	6455	CB	GLN	D	200	−15.629	−41.779	127.723	1.00	33.74		C
ATOM	6456	CG	GLN	D	200	−16.370	−40.476	127.548	1.00	35.08		C
ATOM	6457	CD	GLN	D	200	−15.538	−39.467	126.778	1.00	39.26		C
ATOM	6458	OE1	GLN	D	200	−15.357	−38.324	127.205	1.00	44.14		O
ATOM	6459	NE2	GLN	D	200	−15.015	−39.893	125.639	1.00	40.13		N
ATOM	6460	N	GLY	D	201	−18.482	−42.261	129.550	1.00	34.51		N
ATOM	6461	CA	GLY	D	201	−19.496	−41.749	130.451	1.00	32.88		C
ATOM	6462	C	GLY	D	201	−19.793	−42.624	131.658	1.00	34.93		C
ATOM	6463	O	GLY	D	201	−20.740	−42.333	132.397	1.00	30.85		O
ATOM	6464	N	LEU	D	202	−19.050	−43.719	131.838	1.00	30.30		N
ATOM	6465	CA	LEU	D	202	−19.137	−44.588	133.007	1.00	35.37		C
ATOM	6466	C	LEU	D	202	−17.845	−44.491	133.805	1.00	41.52		C
ATOM	6467	O	LEU	D	202	−16.751	−44.633	133.240	1.00	41.27		O
ATOM	6468	CB	LEU	D	202	−19.405	−46.046	132.624	1.00	36.42		C
ATOM	6469	CG	LEU	D	202	−20.723	−46.250	131.880	1.00	35.17		C
ATOM	6470	CD1	LEU	D	202	−20.916	−47.704	131.503	1.00	29.43		C
ATOM	6471	CD2	LEU	D	202	−21.865	−45.735	132.713	1.00	29.90		C
ATOM	6472	N	SER	D	203	−17.973	−44.219	135.113	1.00	44.01		N
ATOM	6473	CA	SER	D	203	−16.802	−44.095	135.978	1.00	39.30		C
ATOM	6474	C	SER	D	203	−16.068	−45.416	136.165	1.00	41.65		C
ATOM	6475	O	SER	D	203	−14.867	−45.408	136.460	1.00	49.60		O
ATOM	6476	CB	SER	D	203	−17.213	−43.537	137.323	1.00	34.65		C
ATOM	6477	OG	SER	D	203	−18.227	−44.369	137.839	1.00	55.55		O
ATOM	6478	N	SER	D	204	−16.749	−46.545	136.003	1.00	42.27		N
ATOM	6479	CA	SER	D	204	−16.084	−47.841	135.927	1.00	45.69		C
ATOM	6480	C	SER	D	204	−16.989	−48.788	135.149	1.00	36.06		C
ATOM	6481	O	SER	D	204	−18.181	−48.508	134.979	1.00	38.46		O
ATOM	6482	CB	SER	D	204	−15.755	−48.401	137.332	1.00	48.88		C
ATOM	6483	OG	SER	D	204	−16.914	−48.719	138.093	1.00	47.01		O
ATOM	6484	N	PRO	D	205	−16.453	−49.888	134.637	1.00	32.30		N
ATOM	6485	CA	PRO	D	205	−17.271	−50.768	133.791	1.00	36.16		C
ATOM	6486	C	PRO	D	205	−18.534	−51.253	134.498	1.00	37.49		C
ATOM	6487	O	PRO	D	205	−18.503	−51.695	135.642	1.00	46.01		O
ATOM	6488	CB	PRO	D	205	−16.313	−51.925	133.468	1.00	34.46		C
ATOM	6489	CG	PRO	D	205	−14.973	−51.268	133.442	1.00	33.52		C
ATOM	6490	CD	PRO	D	205	−15.013	−50.158	134.481	1.00	32.12		C
ATOM	6491	N	VAL	D	206	−19.629	−51.261	133.750	1.00	37.13		N
ATOM	6492	CA	VAL	D	206	−20.952	−51.648	134.217	1.00	32.96		C
ATOM	6493	C	VAL	D	206	−21.270	−53.027	133.650	1.00	35.67		C
ATOM	6494	O	VAL	D	206	−21.071	−53.272	132.456	1.00	33.93		O
ATOM	6495	CB	VAL	D	206	−21.984	−50.601	133.769	1.00	30.63		C
ATOM	6496	CG1	VAL	D	206	−23.390	−51.059	134.005	1.00	30.69		C
ATOM	6497	CG2	VAL	D	206	−21.703	−49.316	134.479	1.00	38.52		C
ATOM	6498	N	THR	D	207	−21.748	−53.932	134.503	1.00	40.16		N
ATOM	6499	CA	THR	D	207	−22.093	−55.285	134.087	1.00	33.00		C
ATOM	6500	C	THR	D	207	−23.587	−55.538	134.269	1.00	33.37		C
ATOM	6501	O	THR	D	207	−24.188	−55.112	135.255	1.00	34.36		O
ATOM	6502	CB	THR	D	207	−21.271	−56.317	134.871	1.00	32.59		C
ATOM	6503	OG1	THR	D	207	−19.872	−56.064	134.677	1.00	35.95		O
ATOM	6504	CG2	THR	D	207	−21.585	−57.744	134.412	1.00	31.54		C
ATOM	6505	N	LYS	D	208	−24.194	−56.172	133.277	1.00	38.08		N
ATOM	6506	CA	LYS	D	208	−25.529	−56.734	133.393	1.00	33.58		C
ATOM	6507	C	LYS	D	208	−25.435	−58.233	133.155	1.00	31.51		C
ATOM	6508	O	LYS	D	208	−24.797	−58.679	132.202	1.00	36.26		O
ATOM	6509	CB	LYS	D	208	−26.510	−56.072	132.395	1.00	32.49		C
ATOM	6510	CG	LYS	D	208	−26.633	−54.559	132.573	1.00	34.11		C
ATOM	6511	CD	LYS	D	208	−26.879	−54.180	134.030	1.00	32.10		C
ATOM	6512	CE	LYS	D	208	−27.135	−52.694	134.212	1.00	31.43		C
ATOM	6513	HZ	LYS	D	208	−28.595	−52.396	134.289	1.00	30.11		N1+
ATOM	6514	N	SER	D	209	−26.099	−59.013	133.995	1.00	40.89		N
ATOM	6515	CA	SER	D	209	−25.955	−60.457	133.950	1.00	34.12		C
ATOM	6516	C	SER	D	209	−27.289	−61.121	134.250	1.00	35.96		C
ATOM	6517	O	SER	D	209	−28.265	−60.469	134.620	1.00	35.44		O
ATOM	6518	CB	SER	D	209	−24.856	−60.923	134.926	1.00	34.50		C
ATOM	6519	OG	SER	D	209	−25.082	−60.438	136.238	1.00	29.12		O
ATOM	6520	N	PHE	D	210	−27.333	−62.431	134.025	1.00	39.78		N
ATOM	6521	CA	PHE	D	210	−28.424	−63.272	134.488	1.00	37.92		C
ATOM	6522	C	PHE	D	210	−27.883	−64.670	134.767	1.00	42.87		C
ATOM	6523	O	PHE	D	210	−26.994	−65.149	134.055	1.00	42.97		O
ATOM	6524	CB	PHE	D	210	−29.555	−63.296	133.464	1.00	34.40		C
ATOM	6525	CG	PHE	D	210	−29.193	−63.943	132.160	1.00	40.31		C
ATOM	6526	CD1	PHE	D	210	−29.365	−65.304	131.973	1.00	38.92		C
ATOM	6527	CD2	PHE	D	210	−28.702	−63.182	131.109	1.00	37.04		C
ATOM	6528	CE1	PHE	D	210	−29.055	−65.893	130.777	1.00	36.51		C
ATOM	6529	CE2	PHE	D	210	−28.393	−63.765	129.913	1.00	35.57		C
ATOM	6530	CZ	PHE	D	210	−28.568	−65.125	129.745	1.00	36.28		C
ATOM	6531	N	ASN	D	211	−28.433	−65.331	135.796	1.00	41.98		N
ATOM	6532	CA	ASN	D	211	−28.093	−66.720	136.076	1.00	44.07		C
ATOM	6533	C	ASN	D	211	−29.047	−67.583	135.273	1.00	45.82		C
ATOM	6534	O	ASN	D	211	−30.260	−67.386	135.349	1.00	49.01		O
ATOM	6535	CB	ASN	D	211	−28.194	−67.060	137.568	1.00	42.88		C
ATOM	6536	CG	ASN	D	211	−27.474	−66.058	138.456	1.00	48.18		C
ATOM	6537	OD1	ASN	D	211	−26.529	−65.407	138.034	1.00	55.66		O
ATOM	6538	ND2	ASN	D	211	−27.920	−65.934	139.701	1.00	53.20		N
ATOM	6539	N	ARG	D	212	−28.501	−68.538	134.512	1.00	42.56		N
ATOM	6540	CA	ARG	D	212	−29.339	−69.369	133.655	1.00	44.17		C
ATOM	6541	C	ARG	D	212	−30.389	−70.120	134.460	1.00	52.65		C
ATOM	6542	O	ARG	D	212	−30.117	−70.632	135.550	1.00	57.95		O
ATOM	6543	CB	ARG	D	212	−28.497	−70.365	132.870	1.00	44.08		C
ATOM	6544	CG	ARG	D	212	−29.313	−71.160	131.848	1.00	39.96		C
ATOM	6545	CD	ARG	D	212	−28.430	−72.092	131.021	1.00	41.55		C
ATOM	6546	NE	ARG	D	212	−27.681	−72.968	131.906	1.00	52.14		N
ATOM	6547	CZ	ARG	D	212	−28.121	−74.138	132.360	1.00	52.75		C
ATOM	6548	NH1	ARG	D	212	−29.310	−74.604	131.997	1.00	55.42		N1+
ATOM	6549	NH2	ARG	D	212	−27.365	−74.845	133.177	1.00	50.00		N
ATOM	6550	N	GLY	D	213	−31.606	−70.150	133.923	1.00	55.21		N
ATOM	6551	CA	GLY	D	213	−32.710	−70.874	134.521	1.00	61.80		C
ATOM	6552	C	GLY	D	213	−33.365	−70.219	135.716	1.00	69.36		C
ATOM	6553	O	GLY	D	213	−34.221	−70.844	136.350	1.00	78.60		O
ATOM	6554	N	GLU	D	214	−33.041	−68.971	136.017	1.00	64.22		N
ATOM	6555	CA	GLU	D	214	−33.596	−68.288	137.169	1.00	66.25		C
ATOM	6556	C	GLU	D	214	−34.131	−66.936	136.710	1.00	74.30		C
ATOM	6557	O	GLU	D	214	−34.125	−66.617	135.517	1.00	72.76		O
ATOM	6558	CB	GLU	D	214	−32.534	−68.153	138.268	1.00	68.20		C
ATOM	6559	CG	GLU	D	214	−31.925	−69.500	138.684	1.00	65.48		C
ATOM	6560	CD	GLU	D	214	−30.610	−69.356	139.461	1.00	70.80		C
ATOM	6561	OE1	GLU	D	214	−30.431	−68.335	140.180	1.00	56.20		O
ATOM	6562	OE2	GLU	D	214	−29.760	−70.276	139.354	1.00	68.01		O1−
ATOM	6563	N	CYS	D	215	−34.599	−66.138	137.668	1.00	83.83		N
ATOM	6564	CA	CYS	D	215	−35.238	−64.844	137.389	1.00	81.44		C
ATOM	6565	C	CYS	D	215	−34.229	−63.723	137.129	1.00	91.66		C
ATOM	6566	O	CYS	D	215	−33.764	−63.051	138.055	1.00	89.67		O
ATOM	6567	CB	CYS	D	215	−36.153	−64.449	138.554	1.00	87.78		C
ATOM	6568	SG	CYS	D	215	−35.402	−64.679	140.202	1.00	106.03		S
TER
ATOM	6569	N	THR	I	152	−42.630	−26.640	53.407	1.00	78.60	D000	N
ATOM	6570	CA	THR	I	152	−41.299	−26.066	53.631	1.00	90.61	D000	C
ATOM	6571	C	THR	I	152	−41.155	−25.639	55.096	1.00	90.48	D000	C
ATOM	6572	O	THR	I	152	−40.054	−25.653	55.660	1.00	85.79	D000	O
ATOM	6573	CB	THR	I	152	−41.001	−24.845	52.694	1.00	84.39	D000	C
ATOM	6574	OG1	THR	I	152	−42.169	−24.027	52.567	1.00	87.95	D000	O
ATOM	6575	CG2	THR	I	152	−40.569	−25.297	51.311	1.00	74.94	D000	C
ATOM	6576	N	CYS	I	153	−42.275	−25.254	55.707	1.00	89.21	D000	N
ATOM	6577	CA	CYS	I	153	−42.264	−24.807	57.092	1.00	81.53	D000	C
ATOM	6578	C	CYS	I	153	−43.556	−25.234	57.776	1.00	76.72	D000	C
ATOM	6579	O	CYS	I	153	−44.575	−25.496	57.128	1.00	77.13	D000	O
ATOM	6580	CB	CYS	I	153	−42.087	−23.284	57.178	1.00	79.48	D000	C
ATOM	6581	SG	CYS	I	153	−40.357	−22.736	57.167	1.00	91.46	D000	S
ATOM	6582	N	CYS	I	154	−43.494	−25.316	59.112	1.00	68.58	D000	N
ATOM	6583	CA	CYS	I	154	−44.632	−25.662	59.947	1.00	56.00	D000	C
ATOM	6584	C	CYS	I	154	−45.352	−24.407	60.411	1.00	54.60	D000	C
ATOM	6585	O	CYS	I	154	−44.726	−23.355	60.580	1.00	53.80	D000	O
ATOM	6586	CB	CYS	I	154	−44.181	−26.474	61.153	1.00	48.63	D000	C
ATOM	6587	SG	CYS	I	154	−43.645	−28.112	60.680	1.00	63.81	D000	S
ATOM	6588	N	PRO	I	155	−46.667	−24.480	60.621	1.00	47.88	D000	N
ATOM	6589	CA	PRO	I	155	−47.397	−23.284	61.039	1.00	41.43	D000	C
ATOM	6590	C	PRO	I	155	−46.878	−22.765	62.371	1.00	47.89	D000	C
ATOM	6591	O	PRO	I	155	−46.206	−23.471	63.130	1.00	43.34	D000	O
ATOM	6592	CB	PRO	I	155	−48.855	−23.757	61.137	1.00	38.59	D000	C
ATOM	6593	CG	PRO	I	155	−48.818	−25.245	61.066	1.00	40.42	D000	C
ATOM	6594	CD	PRO	I	155	−47.558	−25.631	60.385	1.00	47.80	D000	C
ATOM	6595	N	VAL	I	156	−47.223	−21.503	62.648	1.00	50.69	D000	N
ATOM	6596	CA	VAL	I	156	−46.805	−20.823	63.868	1.00	49.74	D000	C
ATOM	6597	C	VAL	I	156	−47.161	−21.667	65.084	1.00	50.63	D000	C
ATOM	6598	O	VAL	I	156	−48.294	−22.142	65.215	1.00	49.76	D000	O
ATOM	6599	CB	VAL	I	156	−47.471	−19.435	63.931	1.00	56.06	D000	C
ATOM	6600	CG1	VAL	I	156	−46.956	−18.628	65.112	1.00	48.56	D000	C
ATOM	6601	CG2	VAL	I	156	−47.275	−18.685	62.605	1.00	59.05	D000	C
ATOM	6602	N	ASN	I	157	−46.178	−21.872	65.968	1.00	51.11	D000	N
ATOM	6603	CA	ASN	I	157	−46.292	−22.645	67.205	1.00	44.19	D000	C
ATOM	6604	C	ASN	I	157	−46.372	−24.144	66.981	1.00	40.81	D000	C
ATOM	6605	O	ASN	I	157	−46.737	−24.864	67.902	1.00	42.83	D000	O
ATOM	6606	CB	ASN	I	157	−47.464	−22.193	68.081	1.00	45.04	D000	C
ATOM	6607	CG	ASN	I	157	−47.278	−20.791	68.601	1.00	50.02	D000	C
ATOM	6608	OD1	ASN	I	157	−46.197	−20.437	69.063	1.00	54.69	D000	O
ATOM	6609	ND2	ASN	I	157	−48.315	−19.979	68.513	1.00	59.66	D000	N
ATOM	6610	N	TRP	I	158	−46.085	−24.633	65.778	1.00	40.56	D000	N
ATOM	6611	CA	TRP	I	158	−45.839	−26.051	65.566	1.00	38.45	D000	C
ATOM	6612	C	TRP	I	158	−44.345	−26.293	65.371	1.00	40.31	D000	C
ATOM	6613	O	TRP	I	158	−43.584	−25.397	65.007	1.00	39.61	D000	O
ATOM	6614	CB	TRP	I	158	−46.629	−26.590	64.371	1.00	40.79	D000	C
ATOM	6615	CG	TRP	I	158	−48.118	−26.566	64.574	1.00	40.96	D000	C
ATOM	6616	CD1	TRP	I	158	−48.892	−25.473	64.883	1.00	39.11	D000	C
ATOM	6617	CD2	TRP	I	158	−49.025	−27.667	64.427	1.00	36.12	D000	C
ATOM	6618	NE1	TRP	I	158	−50.213	−25.840	64.971	1.00	35.50	D000	N
ATOM	6619	CE2	TRP	I	158	−50.325	−27.175	64.688	1.00	32.39	D000	C
ATOM	6620	CE3	TRP	I	158	−48.867	−29.017	64.101	1.00	36.76	D000	C
ATOM	6621	CZ2	TRP	I	158	−51.453	−27.985	64.636	1.00	33.44	D000	C
ATOM	6622	CZ3	TRP	I	158	−49.993	−29.826	64.048	1.00	36.91	D000	C
ATOM	6623	CH2	TRP	I	158	−51.271	−29.308	64.321	1.00	34.08	D000	C
ATOM	6624	N	VAL	I	159	−43.939	−27.531	65.615	1.00	42.08	D000	N
ATOM	6625	CA	VAL	I	159	−42.544	−27.931	65.687	1.00	36.72	D000	C
ATOM	6626	C	VAL	I	159	−42.284	−28.942	64.582	1.00	40.42	D000	C
ATOM	6627	O	VAL	I	159	−42.934	−29.992	64.529	1.00	34.21	D000	O
ATOM	6628	CB	VAL	I	159	−42.222	−28.551	67.060	1.00	40.12	D000	C
ATOM	6629	CG1	VAL	I	159	−40.793	−29.037	67.110	1.00	39.21	D000	C
ATOM	6630	CG2	VAL	I	159	−42.486	−27.563	68.171	1.00	43.22	D000	C
ATOM	6631	N	GLU	I	160	−41.300	−28.660	63.739	1.00	45.25	D000	N
ATOM	6632	CA	GLU	I	160	−40.975	−29.588	62.671	1.00	43.30	D000	C
ATOM	6633	C	GLU	I	160	−40.058	−30.686	63.184	1.00	41.09	D000	C
ATOM	6634	O	GLU	I	160	−39.201	−30.447	64.036	1.00	44.54	D000	O
ATOM	6635	CB	GLU	I	160	−40.309	−28.861	61.510	1.00	49.23	D000	C
ATOM	6636	CG	GLU	I	160	−40.396	−29.626	60.191	1.00	61.45	D000	C
ATOM	6637	CD	GLU	I	160	−39.556	−28.996	59.095	1.00	74.24	D000	C
ATOM	6638	OE1	GLU	I	160	−40.073	−28.128	58.350	1.00	75.44	D000	O
ATOM	6639	OE2	GLU	I	160	−38.365	−29.367	58.996	1.00	82.31	D000	O1−
ATOM	6640	N	HIS	I	161	−40.262	−31.899	62.675	1.00	34.25	D000	N
ATOM	6641	CA	HIS	I	161	−39.358	−33.005	62.927	1.00	35.38	D000	C
ATOM	6642	C	HIS	I	161	−39.634	−34.146	61.950	1.00	44.04	D000	C
ATOM	6643	O	HIS	I	161	−40.655	−34.832	62.063	1.00	44.75	D000	O
ATOM	6644	CB	HIS	I	161	−39.491	−33.493	64.372	1.00	34.41	D000	C
ATOM	6645	CG	HIS	I	161	−38.662	−34.709	64.679	1.00	42.31	D000	C
ATOM	6646	ND1	HIS	I	161	−37.356	−34.632	65.127	1.00	39.49	D000	N
ATOM	6647	CD2	HIS	I	161	−38.947	−36.031	64.578	1.00	37.68	D000	C
ATOM	6648	CE1	HIS	I	161	−36.884	−35.854	65.308	1.00	36.84	D000	C
ATOM	6649	NE2	HIS	I	161	−37.823	−36.720	64.970	1.00	37.93	D000	N
ATOM	6650	N	GLU	I	162	−38.726	−34.358	60.992	1.00	48.09	D000	N
ATOM	6651	CA	GLU	I	162	−38.750	−35.513	60.090	1.00	42.19	D000	C
ATOM	6652	C	GLU	I	162	−39.999	−35.567	59.225	1.00	46.13	D000	C
ATOM	6653	O	GLU	I	162	−40.676	−36.597	59.149	1.00	46.71	D000	O
ATOM	6654	CB	GLU	I	162	−38.576	−36.822	60.852	1.00	38.57	D000	C
ATOM	6655	CG	GLU	I	162	−37.232	−36.891	61.474	1.00	49.45	D000	C
ATOM	6656	CD	GLU	I	162	−36.178	−37.369	60.479	1.00	67.10	D000	C
ATOM	6657	OE1	GLU	I	162	−36.210	−38.565	60.098	1.00	74.81	D000	O
ATOM	6658	OE2	GLU	I	162	−35.341	−36.533	60.050	1.00	59.37	D000	O1−
ATOM	6659	N	ARG	I	163	−40.289	−34.453	58.547	1.00	48.14	D000	N
ATOM	6660	CA	ARG	I	163	−41.446	−34.362	57.648	1.00	57.33	D000	C
ATOM	6661	C	ARG	I	163	−42.768	−34.545	58.387	1.00	53.34	D000	C
ATOM	6662	O	ARG	I	163	−43.712	−35.129	57.854	1.00	56.97	D000	O
ATOM	6663	CB	ARG	I	163	−41.335	−35.388	56.509	1.00	65.00	D000	C
ATOM	6664	CG	ARG	I	163	−40.188	−35.176	55.528	1.00	68.66	D000	C
ATOM	6665	CD	ARG	I	163	−40.271	−36.202	54.398	1.00	80.19	D000	C
ATOM	6666	NE	ARG	I	163	−41.472	−36.074	53.577	1.00	89.56	D000	N
ATOM	6667	CZ	ARG	I	163	−41.971	−37.066	52.841	1.00	92.42	D000	C
ATOM	6668	NH1	ARG	I	163	−43.077	−36.881	52.123	1.00	78.10	D000	N1+
ATOM	6669	NH2	ARG	I	163	−41.362	−38.249	52.832	1.00	94.56	D000	N
ATOM	6670	N	SER	I	164	−42.822	−34.104	59.641	1.00	53.57	D000	N
ATOM	6671	CA	SER	I	164	−44.059	−33.988	60.400	1.00	46.49	D000	C
ATOM	6672	C	SER	I	164	−44.026	−32.697	61.203	1.00	51.04	D000	C
ATOM	6673	O	SER	I	164	−42.965	−32.279	61.679	1.00	50.06	D000	O
ATOM	6674	CB	SER	I	164	−44.270	−35.170	61.343	1.00	43.89	D000	C
ATOM	6675	OG	SER	I	164	−44.907	−36.249	60.692	1.00	50.01	D000	O
ATOM	6676	N	CYS	I	165	−45.194	−32.075	61.357	1.00	50.05	D000	N
ATOM	6677	CA	CYS	I	165	−45.370	−30.919	62.233	1.00	47.87	D000	C
ATOM	6678	C	CYS	I	165	−46.135	−31.340	63.489	1.00	43.11	0000	C
ATOM	6679	O	CYS	I	165	−47.190	−31.975	63.399	1.00	42.93	D000	O
ATOM	6680	CB	CYS	I	165	−46.116	−29.778	61.524	1.00	50.43	D000	C
ATOM	6681	SG	CYS	I	165	−45.326	−29.058	60.031	1.00	58.62	D000	S
ATOM	6682	N	TYR	I	166	−45.622	−30.957	64.656	1.00	43.41	D000	N
ATOM	6683	CA	TYR	I	166	−46.198	−31.350	65.934	1.00	35.17	D000	C
ATOM	6684	C	TYR	I	166	−46.617	−30.116	66.719	1.00	36.72	D000	C
ATOM	6685	O	TYR	I	166	−45.937	−29.084	66.683	1.00	35.81	D000	O
ATOM	6686	CB	TYR	I	166	−45.214	−32.158	66.761	1.00	28.42	D000	C
ATOM	6687	CG	TYR	I	166	−44.766	−33.439	66.120	1.00	35.36	D000	C
ATOM	6688	CD1	TYR	I	166	−43.703	−33.461	65.194	1.00	40.74	D000	C
ATOM	6689	CD2	TYR	I	166	−45.379	−34.629	66.435	1.00	28.15	D000	C
ATOM	6690	CE1	TYR	I	166	−43.280	−34.646	64.614	1.00	31.55	D000	C
ATOM	6691	CE2	TYR	I	166	−44.966	−35.813	65.864	1.00	35.33	D000	C
ATOM	6692	CZ	TYR	I	166	−43.926	−35.818	64.952	1.00	36.07	D000	C
ATOM	6693	OH	TYR	I	166	−43.557	−37.022	64.406	1.00	37.06	D000	O
ATOM	6694	N	TRP	I	167	−47.735	−30.235	67.438	1.00	33.78	D000	N
ATOM	6695	CA	TRP	I	167	−48.213	−29.191	68.335	1.00	33.91	D000	C
ATOM	6696	C	TRP	I	167	−48.485	−29.823	69.692	1.00	33.58	D000	C
ATOM	6697	O	TRP	I	167	−49.169	−30.848	69.776	1.00	37.11	D000	O
ATOM	6698	CB	TRP	I	167	−49.478	−28.509	67.776	1.00	37.58	D000	C
ATOM	6699	CG	TRP	I	167	−50.029	−27.432	68.678	1.00	36.19	D000	C
ATOM	6700	CD1	TRP	I	167	−49.648	−26.122	68.725	1.00	37.64	D000	C
ATOM	6701	CD2	TRP	I	167	−51.064	−27.580	69.657	1.00	33.12	D000	C
ATOM	6702	NE1	TRP	I	167	−50.365	−25.452	69.692	1.00	32.45	D000	N
ATOM	6703	CE2	TRP	I	167	−51.246	−26.325	70.269	1.00	31.52	D000	C
ATOM	6704	CE3	TRP	I	167	−51.846	−28.659	70.083	1.00	35.72	D000	C
ATOM	6705	CZ2	TRP	I	167	−52.183	−26.116	71.277	1.00	34.14	D000	C
ATOM	6706	CZ3	TRP	I	167	−52.782	−28.447	71.087	1.00	32.27	D000	C
ATOM	6707	CH2	TRP	I	167	−52.941	−27.185	71.669	1.00	31.51	D000	C
ATOM	6708	N	PHE	I	168	−47.934	−29.223	70.748	1.00	35.27	D000	N
ATOM	6709	CA	PHE	I	168	−47.963	−29.784	72.101	1.00	31.67	D000	C
ATOM	6710	C	PHE	I	168	−48.837	−28.898	72.975	1.00	31.00	D000	C
ATOM	6711	O	PHE	I	168	−48.468	−27.757	73.263	1.00	28.23	D000	O
ATOM	6712	CB	PHE	I	168	−46.555	−29.881	72.685	1.00	28.79	D000	C
ATOM	6713	CG	PHE	I	168	−45.609	−30.707	71.860	1.00	29.81	D000	C
ATOM	6714	CD1	PHE	I	168	−45.461	−32.067	72.099	1.00	30.76	D000	C
ATOM	6715	CD2	PHE	I	168	−44.881	−30.129	70.836	1.00	27.05	D000	C
ATOM	6716	CE1	PHE	I	168	−44.587	−32.824	71.329	1.00	29.28	D000	C
ATOM	6717	CE2	PHE	I	168	−44.009	−30.878	70.073	1.00	27.44	D000	C
ATOM	6718	CZ	PHE	I	168	−43.869	−32.224	70.310	1.00	26.73	D000	C
ATOM	6719	N	SER	I	169	−49.963	−29.437	73.440	1.00	31.45	D000	N
ATOM	6720	CA	SER	I	169	−50.883	−28.643	74.245	1.00	31.26	D000	C
ATOM	6721	C	SER	I	169	−50.266	−28.259	75.591	1.00	25.88	D000	C
ATOM	6722	O	SER	I	169	−49.376	−28.932	76.115	1.00	23.51	D000	O
ATOM	6723	CB	SER	I	169	−52.201	−29.404	74.471	1.00	30.30	D000	C
ATOM	6724	OG	SER	I	169	−52.074	−30.442	75.438	1.00	28.82	D000	O
ATOM	6725	N	ARG	I	170	−50.734	−27.135	76.129	1.00	27.95	D000	N
ATOM	6726	CA	ARG	I	170	−50.447	−26.722	77.495	1.00	34.22	D000	C
ATOM	6727	C	ARG	I	170	−51.671	−26.846	78.392	1.00	33.58	D000	C
ATOM	6728	O	ARG	I	170	−51.627	−26.414	79.546	1.00	31.86	D000	O
ATOM	6729	CB	ARG	I	170	−49.944	−25.282	77.529	1.00	25.51	D000	C
ATOM	6730	CG	ARG	I	170	−48.455	−25.122	77.693	1.00	33.77	D000	C
ATOM	6731	CD	ARG	I	170	−48.071	−25.130	79.130	1.00	32.63	D000	C
ATOM	6732	NE	ARG	I	170	−47.020	−26.113	79.328	1.00	38.28	D000	N
ATOM	6733	CZ	ARG	I	170	−46.005	−25.992	80.166	1.00	33.99	D000	C
ATOM	6734	NH1	ARG	I	170	−45.904	−24.932	80.960	1.00	29.65	D000	N1+
ATOM	6735	NH2	ARG	I	170	−45.123	−26.986	80.241	1.00	33.21	D000	N
ATOM	6736	N	SER	I	171	−52.760	−27.420	77.888	1.00	27.31	D000	N
ATOM	6737	CA	SER	I	171	−53.943	−27.684	78.682	1.00	24.95	D000	C
ATOM	6738	C	SER	I	171	−54.303	−29.138	78.489	1.00	29.34	D000	C
ATOM	6739	O	SER	I	171	−53.693	−29.847	77.682	1.00	31.49	D000	O
ATOM	6740	CB	SER	I	171	−55.119	−26.815	78.277	1.00	21.97	D000	C
ATOM	6741	OG	SER	I	171	−55.427	−27.085	76.932	1.00	35.69	D000	O
ATOM	6742	N	GLY	I	172	−55.301	−29.577	79.252	1.00	29.63	D000	N
ATOM	6743	CA	GLY	I	172	−55.700	−30.970	79.280	1.00	24.44	D000	C
ATOM	6744	C	GLY	I	172	−57.075	−31.181	78.703	1.00	25.61	D000	C
ATOM	6745	O	GLY	I	172	−57.864	−30.245	78.637	1.00	27.53	D000	O
ATOM	6746	N	LYS	I	173	−57.363	−32.400	78.273	1.00	25.19	D000	N
ATOM	6747	CA	LYS	I	173	−58.629	−32.726	77.650	1.00	27.09	D000	C
ATOM	6748	C	LYS	I	173	−58.823	−34.231	77.752	1.00	33.35	D000	C
ATOM	6749	O	LYS	I	173	−57.854	−34.995	77.672	1.00	29.52	D000	O
ATOM	6750	CB	LYS	I	173	−58.693	−32.295	76.172	1.00	27.91	D000	C
ATOM	6751	CG	LYS	I	173	−58.975	−30.805	75.865	1.00	25.52	D000	C
ATOM	6752	CD	LYS	I	173	−59.510	−30.671	74.410	1.00	26.32	D000	C
ATOM	6753	CE	LYS	I	173	−59.494	−29.257	73.861	1.00	19.84	D000	C
ATOM	6754	NZ	LYS	I	173	−60.449	−28.327	74.536	1.00	27.70	D000	N1+
ATOM	6755	N	ALA	I	174	−60.076	−34.643	77.956	1.00	29.60	D000	N
ATOM	6756	CA	ALA	I	174	−60.433	−36.038	77.791	1.00	32.67	D000	C
ATOM	6757	C	ALA	I	174	−60.003	−36.509	76.401	1.00	33.60	D000	C
ATOM	6758	O	ALA	I	174	−59.996	−35.730	75.441	1.00	31.75	D000	O
ATOM	6759	CB	ALA	I	174	−61.943	−36.202	77.997	1.00	28.75	D000	C
ATOM	6760	N	TRP	I	175	−59.641	−37.796	76.289	1.00	30.30	D000	N
ATOM	6761	CA	TRP	I	175	−59.069	−38.288	75.033	1.00	32.92	D000	C
ATOM	6762	C	TRP	I	175	−59.946	−37.956	73.824	1.00	35.10	D000	C
ATOM	6763	O	TRP	I	175	−59.441	−37.507	72.790	1.00	38.08	D000	O
ATOM	6764	CB	TRP	I	175	−58.822	−39.795	75.102	1.00	33.10	D000	C
ATOM	6765	CG	TRP	I	175	−58.056	−40.337	73.893	1.00	38.61	D000	C
ATOM	6766	CD1	TRP	I	175	−56.729	−40.615	73.835	1.00	38.20	D000	C
ATOM	6767	CD2	TRP	I	175	−58.584	−40.653	72.579	1.00	43.49	D000	C
ATOM	6768	NE1	TRP	I	175	−56.388	−41.079	72.580	1.00	35.04	D000	N
ATOM	6769	CE2	TRP	I	175	−57.505	−41.113	71.793	1.00	38.92	D000	C
ATOM	6770	CE3	TRP	I	175	−59.863	−40.593	71.996	1.00	43.77	D000	C
ATOM	6771	CZ2	TRP	I	175	−57.662	−41.517	70.456	1.00	44.27	D000	C
ATOM	6772	CZ3	TRP	I	175	−60.016	−40.989	70.650	1.00	43.79	D000	C
ATOM	6773	CH2	TRP	I	175	−58.925	−41.448	69.906	1.00	44.29	D000	C
ATOM	6774	N	ALA	I	176	−61.260	−38.156	73.936	1.00	33.82	D000	N
ATOM	6775	CA	ALA	I	176	−62.154	−37.894	72.815	1.00	28.11	D000	C
ATOM	6776	C	ALA	I	176	−62.108	−36.432	72.394	1.00	37.58	D000	C
ATOM	6777	O	ALA	I	176	−62.150	−36.111	71.196	1.00	36.74	D000	O
ATOM	6778	CB	ALA	I	176	−63.578	−38.275	73.199	1.00	27.93	D000	C
ATOM	6779	N	ASP	I	177	−62.043	−35.528	73.370	1.00	35.00	D000	N
ATOM	6780	CA	ASP	I	177	−62.036	−34.117	73.044	1.00	32.37	D000	C
ATOM	6781	C	ASP	I	177	−60.712	−33.703	72.435	1.00	34.46	D000	C
ATOM	6782	O	ASP	I	177	−60.672	−32.790	71.591	1.00	33.36	D000	O
ATOM	6783	CB	ASP	I	177	−62.355	−33.298	74.290	1.00	36.16	D000	C
ATOM	6784	CG	ASP	I	177	−63.729	−33.623	74.876	1.00	40.76	D000	C
ATOM	6785	OD1	ASP	I	177	−64.648	−33.982	74.097	1.00	35.33	D000	O
ATOM	6786	OD2	ASP	I	177	−63.888	−33.508	76.122	1.00	45.92	D000	O1−
ATOM	6787	N	ALA	I	178	−59.622	−34.340	72.869	1.00	33.13	D000	N
ATOM	6788	CA	ALA	I	178	−58.325	−34.082	72.255	1.00	34.80	D000	C
ATOM	6789	C	ALA	I	178	−58.313	−34.585	70.812	1.00	35.86	D000	C
ATOM	6790	O	ALA	I	178	−57.887	−33.873	69.898	1.00	30.16	D000	O
ATOM	6791	CB	ALA	I	178	−57.224	−34.734	73.085	1.00	29.11	D000	C
ATOM	6792	N	ASP	I	179	−58.825	−35.803	70.601	1.00	38.39	D000	N
ATOM	6793	CA	ASP	I	179	−59.085	−36.343	69.268	1.00	35.65	D000	C
ATOM	6794	C	ASP	I	179	−59.826	−35.347	68.401	1.00	37.02	D000	C
ATOM	6795	O	ASP	I	179	−59.397	−35.030	67.286	1.00	39.99	D000	O
ATOM	6796	CB	ASP	I	179	−59.886	−37.642	69.413	1.00	41.79	D000	C
ATOM	6797	CG	ASP	I	179	−60.149	−38.338	68.094	1.00	42.90	D000	C
ATOM	6798	OD1	ASP	I	179	−59.371	−38.120	67.149	1.00	43.83	D000	O
ATOM	6799	OD2	ASP	I	179	−61.096	−39.163	68.035	1.00	43.02	D000	O1−
ATOM	6800	N	ASN	I	180	−60.934	−34.820	68.911	1.00	39.12	D000	N
ATOM	6801	CA	ASN	I	180	−61.715	−33.882	68.117	1.00	39.76	D000	C
ATOM	6802	C	ASN	I	180	−60.945	−32.601	67.851	1.00	32.43	D000	C
ATOM	6803	O	ASN	I	180	−61.062	−32.026	66.768	1.00	38.63	D000	O
ATOM	6804	CB	ASN	I	180	−63.053	−33.580	68.801	1.00	34.44	D000	C
ATOM	6805	CG	ASN	I	180	−63.983	−34.773	68.793	1.00	38.43	D000	C
ATOM	6806	OD1	ASN	I	180	−63.692	−35.795	68.162	1.00	43.96	D000	O
ATOM	6807	ND2	ASN	I	180	−65.126	−34.642	69.458	1.00	38.70	D000	N
ATOM	6808	N	TYR	I	181	−60.142	−32.144	68.814	1.00	37.95	D000	N
ATOM	6809	CA	TYR	I	181	−59.388	−30.900	68.623	1.00	36.10	D000	C
ATOM	6810	C	TYR	I	181	−58.390	−31.012	67.470	1.00	36.90	D000	C
ATOM	6811	O	TYR	I	181	−58.240	−30.077	66.667	1.00	35.28	D000	O
ATOM	6812	CB	TYR	I	181	−58.660	−30.519	69.908	1.00	25.56	D000	C
ATOM	6813	CG	TYR	I	181	−57.826	−29.264	69.780	1.00	28.66	D000	C
ATOM	6814	CD1	TYR	I	181	−56.520	−29.301	69.277	1.00	31.67	D000	C
ATOM	6815	CD2	TYR	I	181	−58.336	−28.043	70.162	1.00	25.48	D000	C
ATOM	6816	CE1	TYR	I	181	−55.768	−28.154	69.148	1.00	29.47	D000	C
ATOM	6817	CE2	TYR	I	181	−57.579	−26.897	70.054	1.00	29.61	D000	C
ATOM	6818	CZ	TYR	I	181	−56.299	−26.952	69.546	1.00	33.58	D000	C
ATOM	6819	OH	TYR	I	181	−55.570	−25.786	69.431	1.00	36.52	D000	O
ATOM	6820	N	CYS	I	182	−57.668	−32.125	67.395	1.00	30.45	D000	N
ATOM	6821	CA	CYS	I	182	−56.669	−32.250	66.346	1.00	39.92	D000	C
ATOM	6822	C	CYS	I	182	−57.323	−32.304	64.964	1.00	42.48	D000	C
ATOM	6823	O	CYS	I	182	−56.879	−31.607	64.034	1.00	37.23	D000	O
ATOM	6824	CB	CYS	I	182	−55.793	−33.477	66.614	1.00	37.71	D000	C
ATOM	6825	SG	CYS	I	182	−54.685	−33.283	68.064	1.00	42.44	D000	S
ATOM	6826	N	ARG	I	183	−58.413	−33.073	64.832	1.00	33.83	D000	N
ATOM	6827	CA	ARG	I	183	−59.071	−33.213	63.538	1.00	34.20	D000	C
ATOM	6828	C	ARG	I	183	−59.478	−31.860	62.965	1.00	40.37	D000	C
ATOM	6829	O	ARG	I	183	−59.310	−31.617	61.764	1.00	43.30	D000	O
ATOM	6830	CB	ARG	I	183	−60.275	−34.128	63.670	1.00	36.10	D000	C
ATOM	6831	CG	ARG	I	183	−59.902	−35.562	63.991	1.00	34.06	D000	C
ATOM	6832	CD	ARG	I	183	−61.081	−36.236	64.587	1.00	39.52	D000	C
ATOM	6833	NE	ARG	I	183	−61.350	−37.531	63.997	1.00	57.45	D000	N
ATOM	6834	CZ	ARG	I	183	−62.574	−37.960	63.698	1.00	68.60	D000	C
ATOM	6835	NH1	ARG	I	183	−63.619	−37.172	63.920	1.00	55.03	D000	N1+
ATOM	6836	NH2	ARG	I	183	−62.754	−39.165	63.159	1.00	76.79	D000	N
ATOM	6837	N	LEU	I	184	−59.980	−30.952	63.805	1.00	34.08	D000	N
ATOM	6838	CA	LEU	I	184	−60.347	−29.625	63.319	1.00	36.10	D000	C
ATOM	6839	C	LEU	I	184	−59.159	−28.729	62.998	1.00	40.84	D000	C
ATOM	6840	O	LEU	I	184	−59.369	−27.647	62.436	1.00	43.24	D000	O
ATOM	6841	CB	LEU	I	184	−61.207	−28.901	64.344	1.00	42.44	D000	C
ATOM	6842	CG	LEU	I	184	−62.705	−29.142	64.369	1.00	44.30	D000	C
ATOM	6843	CD1	LEU	I	184	−62.982	−30.550	64.684	1.00	40.27	D000	C
ATOM	6844	CD2	LEU	I	184	−63.246	−28.314	65.458	1.00	44.72	D000	C
ATOM	6845	N	GLU	I	185	−57.938	−29.126	63.359	1.00	44.61	D000	N
ATOM	6846	CA	GLU	I	185	−56.714	−28.453	62.938	1.00	42.87	D000	C
ATOM	6847	C	GLU	I	185	−56.132	−29.068	61.664	1.00	45.96	D000	C
ATOM	6848	O	GLU	I	185	−55.000	−28.744	61.284	1.00	41.44	D000	O
ATOM	6849	CB	GLU	I	185	−55.678	−28.517	64.061	1.00	38.65	D000	C
ATOM	6850	CG	GLU	I	185	−56.035	−27.729	65.294	1.00	42.71	D000	C
ATOM	6851	CD	GLU	I	185	−55.905	−26.233	65.117	1.00	46.41	D000	C
ATOM	6852	OE1	GLU	I	185	−54.995	−25.799	64.379	1.00	49.20	D000	O
ATOM	6853	OE2	GLU	I	185	−56.701	−25.489	65.737	1.00	47.94	D000	O1−
ATOM	6854	N	ASP	I	186	−56.902	−29.923	60.992	1.00	46.15	D000	N
ATOM	6855	CA	ASP	I	186	−56.421	−30.765	59.904	1.00	46.32	D000	C
ATOM	6856	C	ASP	I	186	−55.202	−31.570	60.344	1.00	45.43	D000	C
ATOM	6857	O	ASP	I	186	−54.175	−31.625	59.670	1.00	47.14	D000	O
ATOM	6858	CB	ASP	I	186	−56.136	−29.951	58.642	1.00	54.37	D000	C
ATOM	6859	CG	ASP	I	186	−56.259	−30.795	57.356	1.00	66.46	D000	C
ATOM	6860	OD1	ASP	I	186	−56.408	−32.045	57.464	1.00	61.88	D000	O
ATOM	6861	OD2	ASP	I	186	−56.193	−30.206	56.242	1.00	69.65	D000	O1−
ATOM	6862	N	ALA	I	187	−55.318	−32.197	61.505	1.00	42.36	D000	N
ATOM	6863	CA	ALA	I	187	−54.205	−32.950	62.052	1.00	35.32	D000	C
ATOM	6864	C	ALA	I	187	−54.783	−34.150	62.787	1.00	33.26	D000	C
ATOM	6865	O	ALA	I	187	−55.966	−34.465	62.668	1.00	37.96	D000	O
ATOM	6866	CB	ALA	I	187	−53.337	−32.044	62.933	1.00	32.84	D000	C
ATOM	6867	N	HIS	I	188	−53.962	−34.816	63.567	1.00	30.88	D000	N
ATOM	6868	CA	HIS	I	188	−54.456	−35.987	64.253	1.00	32.32	D000	C
ATOM	6869	C	HIS	I	188	−53.593	−36.192	65.488	1.00	38.94	D000	C
ATOM	6870	O	HIS	I	188	−52.452	−35.723	65.547	1.00	41.15	D000	O
ATOM	6871	CB	HIS	I	188	−54.419	−37.199	63.331	1.00	28.57	D000	C
ATOM	6872	CG	HIS	I	188	−53.039	−37.551	62.871	1.00	39.86	D000	C
ATOM	6873	ND1	HIS	I	188	−52.317	−38.593	63.414	1.00	43.77	D000	N
ATOM	6874	CD2	HIS	I	188	−52.238	−36.986	61.935	1.00	40.63	D000	C
ATOM	6875	CE1	HIS	I	188	−51.136	−38.662	62.824	1.00	43.40	D000	C
ATOM	6876	NE2	HIS	I	188	−51.063	−37.697	61.925	1.00	44.73	D000	N
ATOM	6877	N	LEU	I	189	−54.155	−36.887	66.480	1.00	34.91	D000	N
ATOM	6878	CA	LEU	I	189	−53.389	−37.240	67.667	1.00	36.57	D000	C
ATOM	6879	C	LEU	I	189	−52.134	−38.003	67.269	1.00	36.22	D000	C
ATOM	6880	O	LEU	I	189	−52.181	−38.892	66.414	1.00	36.87	D000	O
ATOM	6881	CB	LEU	I	189	−54.227	−38.079	68.626	1.00	33.58	D000	C
ATOM	6882	CG	LEU	I	189	−55.332	−37.326	69.361	1.00	32.53	D000	C
ATOM	6883	CD1	LEU	I	189	−56.060	−38.310	70.251	1.00	31.98	D000	C
ATOM	6884	CD2	LEU	I	189	−54.785	−36.156	70.127	1.00	32.11	D000	C
ATOM	6885	N	VAL	I	190	−51.006	−37.639	67.889	1.00	34.36	D000	N
ATOM	6886	CA	VAL	I	190	−49.706	−38.113	67.426	1.00	36.90	D000	C
ATOM	6887	C	VAL	I	190	−49.705	−39.621	67.302	1.00	34.99	D000	C
ATOM	6888	O	VAL	I	190	−50.277	−40.340	68.126	1.00	38.49	D000	O
ATOM	6889	CB	VAL	I	190	−48.565	−37.658	68.355	1.00	40.36	D000	C
ATOM	6890	CG1	VAL	I	190	−48.720	−38.264	69.755	1.00	36.50	D000	C
ATOM	6891	CG2	VAL	I	190	−47.214	−38.026	67.743	1.00	36.89	D000	C
ATOM	6892	N	VAL	I	191	−49.097	−40.091	66.224	1.00	38.67	D000	N
ATOM	6893	CA	VAL	I	191	−48.933	−41.503	65.926	1.00	40.35	D000	C
ATOM	6894	C	VAL	I	191	−47.436	−41.758	65.901	1.00	37.87	D000	C
ATOM	6895	O	VAL	I	191	−46.719	−41.196	65.064	1.00	39.61	D000	O
ATOM	6896	CB	VAL	I	191	−49.589	−41.882	64.586	1.00	42.11	D000	C
ATOM	6897	CG1	VAL	I	191	−49.208	−43.319	64.164	1.00	36.05	D000	C
ATOM	6898	CG2	VAL	I	191	−51.109	−41.663	64.648	1.00	38.64	D000	C
ATOM	6899	N	VAL	I	192	−46.969	−42.599	66.805	1.00	36.01	D000	N
ATOM	6900	CA	VAL	I	192	−45.545	−42.767	67.055	1.00	41.63	D000	C
ATOM	6901	C	VAL	I	192	−45.088	−44.039	66.361	1.00	37.03	D000	C
ATOM	6902	O	VAL	I	192	−45.528	−45.138	66.718	1.00	40.05	D000	O
ATOM	6903	CB	VAL	I	192	−45.264	−42.808	68.565	1.00	40.06	D000	C
ATOM	6904	CG1	VAL	I	192	−43.805	−43.021	68.828	1.00	43.89	D000	C
ATOM	6905	CG2	VAL	I	192	−45.723	−41.516	69.199	1.00	30.23	D000	C
ATOM	6906	N	THR	I	193	−44.188	−43.897	65.377	1.00	40.22	D000	N
ATOM	6907	CA	THR	I	193	−43.828	−45.009	64.496	1.00	46.20	D000	C
ATOM	6908	C	THR	I	193	−42.371	−45.451	64.595	1.00	48.77	D000	C
ATOM	6909	O	THR	I	193	−42.009	−46.439	63.948	1.00	50.27	D000	O
ATOM	6910	CB	THR	I	193	−44.081	−44.649	63.021	1.00	37.88	D000	C
ATOM	6911	OG1	THR	I	193	−43.196	−43.588	62.655	1.00	46.69	D000	O
ATOM	6912	CG2	THR	I	193	−45.516	−44.167	62.808	1.00	35.86	D000	C
ATOM	6913	N	SER	I	194	−41.529	−44.758	65.364	1.00	47.04	D000	N
ATOM	6914	CA	SER	I	194	−40.107	−45.072	65.443	1.00	47.61	D000	C
ATOM	6915	C	SER	I	194	−39.578	−44.648	66.802	1.00	47.34	D000	C
ATOM	6916	O	SER	I	194	−40.228	−43.898	67.531	1.00	48.44	D000	O
ATOM	6917	CB	SER	I	194	−39.292	−44.369	64.357	1.00	44.10	D000	C
ATOM	6918	OG	SER	I	194	−39.457	−42.964	64.442	1.00	48.66	D000	O
ATOM	6919	N	TRP	I	195	−38.388	−45.147	67.143	1.00	44.89	D000	N
ATOM	6920	CA	TRP	I	195	−37.764	−44.738	68.392	1.00	43.95	D000	C
ATOM	6921	C	TRP	I	195	−37.376	−43.274	68.361	1.00	46.62	D000	C
ATOM	6922	O	TRP	I	195	−37.488	−42.577	69.379	1.00	43.24	D000	O
ATOM	6923	CB	TRP	I	195	−36.552	−45.605	68.717	1.00	48.92	D000	C
ATOM	6924	CG	TRP	I	195	−36.802	−46.281	70.004	1.00	55.85	D000	C
ATOM	6925	CD1	TRP	I	195	−37.056	−45.676	71.212	1.00	56.28	D000	C
ATOM	6926	CD2	TRP	I	195	−36.901	−47.690	70.230	1.00	56.55	D000	C
ATOM	6927	NE1	TRP	I	195	−37.292	−46.630	72.179	1.00	58.55	D000	N
ATOM	6928	CE2	TRP	I	195	−37.199	−47.874	71.605	1.00	65.39	D000	C
ATOM	6929	CE3	TRP	I	195	−36.755	−48.815	69.413	1.00	48.79	D000	C
ATOM	6930	CZ2	TRP	I	195	−37.353	−49.140	72.174	1.00	63.33	D000	C
ATOM	6931	CZ3	TRP	I	195	−36.904	−50.070	69.980	1.00	61.76	D000	C
ATOM	6932	CH2	TRP	I	195	−37.198	−50.223	71.349	1.00	69.03	D000	C
ATOM	6933	N	GLU	I	196	−36.914	−42.786	67.210	1.00	43.07	D000	N
ATOM	6934	CA	GLU	I	196	−36.579	−41.374	67.119	1.00	38.64	D000	C
ATOM	6935	C	GLU	I	196	−37.818	−40.526	67.331	1.00	38.66	D000	C
ATOM	6936	O	GLU	I	196	−37.782	−39.540	68.074	1.00	41.67	D000	O
ATOM	6937	CB	GLU	I	196	−35.919	−41.061	65.783	1.00	37.74	D000	C
ATOM	6938	CG	GLU	I	196	−36.000	−42.187	64.776	1.00	52.87	D000	C
ATOM	6939	CD	GLU	I	196	−35.141	−43.397	65.156	1.00	66.98	D000	C
ATOM	6940	OE1	GLU	I	196	−35.717	−44.504	65.378	1.00	59.55	D000	O
ATOM	6941	OE2	GLU	I	196	−33.899	−43.224	65.260	1.00	74.05	D000	O1−
ATOM	6942	N	GLU	I	197	−38.945	−40.923	66.737	1.00	39.39	D000	N
ATOM	6943	CA	GLU	I	197	−40.168	−40.155	66.948	1.00	42.64	D000	C
ATOM	6944	C	GLU	I	197	−40.599	−40.215	68.410	1.00	37.64	D000	C
ATOM	6945	O	GLU	I	197	−41.014	−39.205	68.981	1.00	32.92	D000	O
ATOM	6946	CB	GLU	I	197	−41.283	−40.664	66.038	1.00	40.56	D000	C
ATOM	6947	CG	GLU	I	197	−42.482	−39.748	66.042	1.00	37.27	D000	C
ATOM	6948	CD	GLU	I	197	−43.515	−40.096	64.990	1.00	42.36	D000	C
ATOM	6949	OE1	GLU	I	197	−43.544	−41.263	64.528	1.00	39.06	D000	O
ATOM	6950	OE2	GLU	I	197	−44.277	−39.173	64.601	1.00	44.17	D000	O1−
ATOM	6951	N	GLN	I	198	−40.485	−41.396	69.026	1.00	37.19	D000	N
ATOM	6952	CA	GLN	I	198	−40.810	−41.562	70.435	1.00	33.73	D000	C
ATOM	6953	C	GLN	I	198	−39.920	−40.689	71.301	1.00	39.61	D000	C
ATOM	6954	O	GLN	I	198	−40.401	−39.995	72.206	1.00	35.04	D000	O
ATOM	6955	CB	GLN	I	198	−40.659	−43.026	70.832	1.00	32.87	D000	C
ATOM	6956	CG	GLN	I	198	−40.502	−43.235	72.323	1.00	37.28	D000	C
ATOM	6957	CD	GLN	I	198	−41.830	−43.123	73.085	1.00	35.70	D000	C
ATOM	6958	OE1	GLN	I	198	−42.902	−43.371	72.539	1.00	30.32	D000	O
ATOM	6959	NE2	GLN	I	198	−41.749	−42.729	74.345	1.00	35.65	D000	N
ATOM	6960	N	LYS	I	199	−38.610	−40.700	71.014	1.00	44.77	D000	N
ATOM	6961	CA	LYS	I	199	−37.666	−39.882	71.765	1.00	39.06	D000	C
ATOM	6962	C	LYS	I	199	−37.934	−38.405	71.551	1.00	32.39	D000	C
ATOM	6963	O	LYS	I	199	−37.949	−37.629	72.509	1.00	31.60	D000	O
ATOM	6964	CB	LYS	I	199	−36.232	−40.241	71.380	1.00	36.82	D000	C
ATOM	6965	CG	LYS	I	199	−35.661	−41.318	72.265	1.00	38.84	D000	C
ATOM	6966	CD	LYS	I	199	−34.660	−42.196	71.578	1.00	46.27	D000	C
ATOM	6967	CE	LYS	I	199	−33.601	−41.398	70.901	1.00	41.73	D000	C
ATOM	6968	NZ	LYS	I	199	−32.530	−42.355	70.568	1.00	49.72	D000	N1+
ATOM	6969	N	PHE	I	200	−38.200	−38.011	70.309	1.00	34.30	D000	N
ATOM	6970	CA	PHE	I	200	−38.496	−36.613	70.030	1.00	32.36	D000	C
ATOM	6971	C	PHE	I	200	−39.712	−36.127	70.813	1.00	34.19	D000	C
ATOM	6972	O	PHE	I	200	−39.724	−34.995	71.313	1.00	32.22	D000	O
ATOM	6973	CB	PHE	I	200	−38.719	−36.408	68.539	1.00	28.30	D000	C
ATOM	6974	CG	PHE	I	200	−39.389	−35.123	68.221	1.00	29.58	D000	C
ATOM	6975	CD1	PHE	I	200	−38.661	−33.950	68.167	1.00	34.42	D000	C
ATOM	6976	CD2	PHE	I	200	−40.750	−35.070	67.988	1.00	32.89	D000	C
ATOM	6977	CE1	PHE	I	200	−39.278	−32.727	67.878	1.00	36.14	D000	C
ATOM	6978	CE2	PHE	I	200	−41.373	−33.852	67.708	1.00	32.23	D000	C
ATOM	6979	CZ	PHE	I	200	−40.628	−32.679	67.656	1.00	32.52	D000	C
ATOM	6980	N	VAL	I	201	−40.766	−36.949	70.896	1.00	34.21	D000	N
ATOM	6981	CA	VAL	I	201	−41.963	−36.512	71.604	1.00	32.09	D000	C
ATOM	6982	C	VAL	I	201	−41.691	−36.409	73.104	1.00	28.47	D000	C
ATOM	6983	O	VAL	I	201	−42.112	−35.445	73.745	1.00	29.67	D000	O
ATOM	6984	CB	VAL	I	201	−43.166	−37.423	71.280	1.00	33.84	D000	C
ATOM	6985	CG1	VAL	I	201	−44.371	−37.069	72.171	1.00	26.65	D000	C
ATOM	6986	CG2	VAL	I	201	−43.564	−37.259	69.826	1.00	29.93	D000	C
ATOM	6987	N	GLN	I	202	−40.948	−37.368	73.675	1.00	29.76	D000	N
ATOM	6988	CA	GLN	I	202	−40.625	−37.333	75.103	1.00	27.89	D000	C
ATOM	6989	C	GLN	I	202	−39.957	−36.027	75.500	1.00	30.88	D000	C
ATOM	6990	O	GLN	I	202	−40.371	−35.375	76.462	1.00	33.51	D000	O
ATOM	6991	CB	GLN	I	202	−39.692	−38.471	75.456	1.00	36.89	D000	C
ATOM	6992	CG	GLN	I	202	−40.291	−39.826	75.569	1.00	42.55	D000	C
ATOM	6993	CD	GLN	I	202	−39.269	−40.793	76.129	1.00	48.57	D000	C
ATOM	6994	OE1	GLN	I	202	−39.196	−41.954	75.707	1.00	49.10	D000	O
ATOM	6995	NE2	GLN	I	202	−38.440	−40.305	77.064	1.00	45.91	D000	N
ATOM	6996	N	HIS	I	203	−38.934	−35.620	74.748	1.00	28.33	D000	N
ATOM	6997	CA	HIS	I	203	−38.244	−34.367	74.998	1.00	28.20	D000	C
ATOM	6998	C	HIS	I	203	−39.221	−33.223	75.160	1.00	32.96	D000	C
ATOM	6999	O	HIS	I	203	−39.085	−32.395	76.066	1.00	38.66	D000	O
ATOM	7000	CB	HIS	I	203	−37.308	−34.053	73.837	1.00	38.51	D000	C
ATOM	7001	CG	HIS	I	203	−35.942	−34.622	73.991	1.00	45.00	D000	C
ATOM	7002	ND1	HIS	I	203	−35.086	−34.222	74.994	1.00	43.86	D000	N
ATOM	7003	CD2	HIS	I	203	−35.274	−35.544	73.260	1.00	44.53	D000	C
ATOM	7004	CE1	HIS	I	203	−33.951	−34.887	74.882	1.00	48.63	D000	C
ATOM	7005	NE2	HIS	I	203	−34.043	−35.701	73.843	1.00	52.83	D000	N
ATOM	7006	N	HIS	I	204	−40.192	−33.140	74.253	1.00	33.22	D000	N
ATOM	7007	CA	HIS	I	204	−41.092	−32.000	74.229	1.00	33.76	D000	C
ATOM	7008	C	HIS	I	204	−42.207	−32.107	75.257	1.00	30.31	D000	C
ATOM	7009	O	HIS	I	204	−42.651	−31.076	75.766	1.00	32.42	D000	O
ATOM	7010	CB	HIS	I	204	−41.680	−31.825	72.836	1.00	34.09	D000	C
ATOM	7011	CG	HIS	I	204	−40.730	−31.209	71.872	1.00	33.98	D000	C
ATOM	7012	ND1	HIS	I	204	−40.541	−29.847	71.793	1.00	36.56	D000	N
ATOM	7013	CD2	HIS	I	204	−39.894	−31.764	70.964	1.00	37.43	D000	C
ATOM	7014	CE1	HIS	I	204	−39.636	−29.587	70.865	1.00	42.50	D000	C
ATOM	7015	NE2	HIS	I	204	−39.224	−30.732	70.349	1.00	42.23	D000	N
ATOM	7016	N	ILE	I	205	−42.658	−33.313	75.609	1.00	27.51	D000	N
ATOM	7017	CA	ILE	I	205	−43.735	−33.386	76.587	1.00	30.86	D000	C
ATOM	7018	C	ILE	I	205	−43.220	−33.433	78.017	1.00	29.89	D000	C
ATOM	7019	O	ILE	I	205	−43.958	−33.056	78.934	1.00	35.65	D000	O
ATOM	7020	CB	ILE	I	205	−44.686	−34.591	76.395	1.00	31.24	D000	C
ATOM	7021	CG1	ILE	I	205	−43.981	−35.940	76.592	1.00	26.46	D000	C
ATOM	7022	CG2	ILE	I	205	−45.357	−34.529	75.064	1.00	28.37	D000	C
ATOM	7023	CD1	ILE	I	205	−44.943	−37.086	76.633	1.00	25.80	D000	C
ATOM	7024	N	GLY	I	206	−41.978	−33.852	78.238	1.00	28.95	D000	N
ATOM	7025	CA	GLY	I	206	−41.465	−33.985	79.584	1.00	29.61	D000	C
ATOM	7026	C	GLY	I	206	−42.122	−35.118	80.345	1.00	27.57	D000	C
ATOM	7027	O	GLY	I	206	−42.811	−35.956	79.766	1.00	29.14	D000	O
ATOM	7028	N	PRO	I	207	−41.941	−35.153	81.711	1.00	29.38	D000	N
ATOM	7029	CA	PRO	I	207	−42.433	−36.295	82.509	1.00	32.33	D000	C
ATOM	7030	C	PRO	I	207	−43.904	−36.143	82.896	1.00	35.00	D000	C
ATOM	7031	O	PRO	I	207	−44.262	−36.029	84.077	1.00	27.86	D000	O
ATOM	7032	CB	PRO	I	207	−41.492	−36.271	83.719	1.00	29.81	D000	C
ATOM	7033	CG	PRO	I	207	−41.194	−34.812	83.899	1.00	30.51	D000	C
ATOM	7034	CD	PRO	I	207	−41.260	−34.150	82.549	1.00	24.29	D000	C
ATOM	7035	N	VAL	I	208	−44.771	−36.126	81.879	1.00	31.78	D000	N
ATOM	7036	CA	VAL	I	208	−46.167	−35.726	81.999	1.00	26.40	D000	C
ATOM	7037	C	VAL	I	208	−47.040	−36.722	81.258	1.00	27.82	D000	C
ATOM	7038	O	VAL	I	208	−46.764	−37.034	80.098	1.00	30.68	D000	O
ATOM	7039	CB	VAL	I	208	−46.388	−34.323	81.425	1.00	25.92	D000	C
ATOM	7040	CG1	VAL	I	208	−47.832	−33.981	81.495	1.00	28.17	D000	C
ATOM	7041	CG2	VAL	I	208	−45.544	−33.320	82.172	1.00	26.96	D000	C
ATOM	7042	N	ASN	I	209	−48.080	−37.232	81.927	1.00	27.70	D000	N
ATOM	7043	CA	ASN	I	209	−49.054	−38.093	81.264	1.00	25.54	D000	C
ATOM	7044	C	ASN	I	209	−49.688	−37.350	80.096	1.00	29.53	D000	C
ATOM	7045	O	ASN	I	209	−50.263	−36.271	80.277	1.00	30.75	D000	O
ATOM	7046	CB	ASN	I	209	−50.119	−38.560	82.251	1.00	24.84	D000	C
ATOM	7047	CG	ASN	I	209	−49.588	−39.606	83.223	1.00	31.55	D000	C
ATOM	7048	OD1	ASN	I	209	−48.636	−40.343	82.922	1.00	29.18	D000	O
ATOM	7049	ND2	ASN	I	209	−50.193	−39.667	84.407	1.00	32.11	D000	N
ATOM	7050	N	THR	I	210	−49.543	−37.905	78.889	1.00	28.06	D000	N
ATOM	7051	CA	THR	I	210	−49.900	−37.194	77.666	1.00	29.54	D000	C
ATOM	7052	C	THR	I	210	−50.593	−38.164	76.716	1.00	30.18	D000	C
ATOM	7053	O	THR	I	210	−50.080	−39.257	76.474	1.00	31.78	D000	O
ATOM	7054	CB	THR	I	210	−48.635	−36.568	77.017	1.00	32.46	D000	C
ATOM	7055	OG1	THR	I	210	−48.068	−35.576	77.891	1.00	28.52	D000	O
ATOM	7056	CG2	THR	I	210	−48.955	−35.895	75.680	1.00	32.03	D000	C
ATOM	7057	N	TRP	I	211	−51.748	−37.771	76.178	1.00	28.21	D000	N
ATOM	7058	CA	TRP	I	211	−52.484	−38.637	75.257	1.00	30.26	D000	C
ATOM	7059	C	TRP	I	211	−51.777	−38.768	73.915	1.00	34.53	D000	C
ATOM	7060	O	TRP	I	211	−51.243	−37.784	73.388	1.00	36.53	D000	O
ATOM	7061	CB	TRP	I	211	−53.870	−38.078	74.986	1.00	27.00	D000	C
ATOM	7062	CG	TRP	I	211	−54.837	−38.105	76.098	1.00	29.16	D000	C
ATOM	7063	CD1	TRP	I	211	−55.575	−37.051	76.552	1.00	29.17	D000	C
ATOM	7064	CD2	TRP	I	211	−55.232	−39.235	76.871	1.00	27.40	D000	C
ATOM	7065	NE1	TRP	I	211	−56.401	−37.453	77.547	1.00	29.33	D000	N
ATOM	7066	CE2	TRP	I	211	−56.208	−38.791	77.777	1.00	31.18	D000	C
ATOM	7067	CE3	TRP	I	211	−54.849	−40.575	76.896	1.00	30.57	D000	C
ATOM	7068	CZ2	TRP	I	211	−56.804	−39.643	78.721	1.00	33.48	D000	C
ATOM	7069	CZ3	TRP	I	211	−55.442	−41.420	77.828	1.00	32.75	D000	C
ATOM	7070	CH2	TRP	I	211	−56.414	−40.952	78.721	1.00	31.65	D000	C
ATOM	7071	N	MET	I	212	−51.828	−39.969	73.332	1.00	30.71	D000	N
ATOM	7072	CA	MET	I	212	−51.425	−40.202	71.945	1.00	35.06	D000	C
ATOM	7073	C	MET	I	212	−52.588	−40.816	71.166	1.00	34.50	D000	C
ATOM	7074	O	MET	I	212	−53.536	−41.339	71.746	1.00	29.90	D000	O
ATOM	7075	CB	MET	I	212	−50.197	−41.126	71.870	1.00	33.98	D000	C
ATOM	7076	CG	MET	I	212	−50.532	−42.612	72.009	1.00	34.65	D000	C
ATOM	7077	SD	MET	I	212	−49.112	−43.701	72.320	1.00	36.95	D000	S
ATOM	7078	CE	MET	I	212	−48.665	−43.185	73.977	1.00	32.76	D000	C
ATOM	7079	N	GLY	I	213	−52.482	−40.824	69.836	1.00	31.69	D000	N
ATOM	7080	CA	GLY	I	213	−53.575	−41.340	69.027	1.00	34.66	D000	C
ATOM	7081	C	GLY	I	213	−53.764	−42.849	68.974	1.00	32.70	D000	C
ATOM	7082	O	GLY	I	213	−53.862	−43.424	67.900	1.00	36.23	D000	O
ATOM	7083	N	LEU	I	214	−53.871	−43.509	70.116	1.00	34.81	D000	N
ATOM	7084	CA	LEU	I	214	−53.951	−44.961	70.150	1.00	39.32	D000	C
ATOM	7085	C	LEU	I	214	−55.046	−45.365	71.132	1.00	45.03	D000	C
ATOM	7086	O	LEU	I	214	−54.950	−45.073	72.327	1.00	45.18	D000	O
ATOM	7087	CB	LEU	I	214	−52.589	−45.544	70.557	1.00	39.33	D000	C
ATOM	7088	CG	LEU	I	214	−52.388	−47.049	70.722	1.00	44.57	D000	C
ATOM	7089	CD1	LEU	I	214	−52.448	−47.717	69.369	1.00	42.58	D000	C
ATOM	7090	CD2	LEU	I	214	−51.059	−47.335	71.406	1.00	38.76	D000	C
ATOM	7091	N	HIS	I	215	−56.076	−46.053	70.639	1.00	50.99	D000	N
ATOM	7092	CA	HIS	I	215	−57.202	−46.449	71.479	1.00	54.24	D000	C
ATOM	7093	C	HIS	I	215	−57.809	−47.741	70.957	1.00	53.49	D000	C
ATOM	7094	O	HIS	I	215	−57.726	−48.039	69.766	1.00	59.77	D000	O
ATOM	7095	CB	HIS	I	215	−58.297	−45.381	71.525	1.00	51.69	D000	C
ATOM	7096	CG	HIS	I	215	−58.991	−45.169	70.220	1.00	53.16	D000	C
ATOM	7097	ND1	HIS	I	215	−60.319	−44.814	70.139	1.00	61.14	D000	N
ATOM	7098	CD2	HIS	I	215	−58.542	−45.241	68.946	1.00	52.42	D000	C
ATOM	7099	CE1	HIS	I	215	−60.664	−44.692	68.868	1.00	60.68	D000	C
ATOM	7100	NE2	HIS	I	215	−59.602	−44.938	68.124	1.00	56.57	D000	N
ATOM	7101	N	ASP	I	216	−58.446	−48.489	71.850	1.00	51.53	D000	N
ATOM	7102	CA	ASP	I	216	−59.163	−49.708	71.488	1.00	63.11	D000	C
ATOM	7103	C	ASP	I	216	−60.629	−49.629	71.897	1.00	70.32	D000	C
ATOM	7104	O	ASP	I	216	−61.218	−50.615	72.345	1.00	73.44	D000	O
ATOM	7105	CB	ASP	I	216	−58.504	−50.956	72.083	1.00	62.05	D000	C
ATOM	7106	CG	ASP	I	216	−58.816	−51.157	73.565	1.00	63.11	D000	C
ATOM	7107	OD1	ASP	I	216	−59.134	−50.177	74.265	1.00	66.02	D000	O
ATOM	7108	OD2	ASP	I	216	−58.783	−52.313	74.025	1.00	71.37	D000	O1−
ATOM	7109	N	GLN	I	217	−61.243	−48.448	71.761	1.00	68.81	D000	N
ATOM	7110	CA	GLN	I	217	−62.674	−48.330	72.036	1.00	79.13	D000	C
ATOM	7111	C	GLN	I	217	−63.497	−49.323	71.214	1.00	82.76	D000	C
ATOM	7112	O	GLN	I	217	−64.637	−49.629	71.584	1.00	81.10	D000	O
ATOM	7113	CB	GLN	I	217	−63.136	−46.885	71.804	1.00	78.37	D000	C
ATOM	7114	CG	GLN	I	217	−63.047	−46.020	73.089	1.00	75.77	D000	C
ATOM	7115	CD	GLN	I	217	−62.642	−44.570	72.825	1.00	67.80	D000	C
ATOM	7116	OE1	GLN	I	217	−61.796	−44.296	71.969	1.00	62.96	D000	O
ATOM	7117	NE2	GLN	I	217	−63.220	−43.637	73.591	1.00	56.15	D000	N
ATOM	7118	N	ASN	I	218	−62.934	−49.838	70.118	1.00	81.51	D000	N
ATOM	7119	CA	ASN	I	218	−63.546	−50.918	69.346	1.00	86.93	D000	C
ATOM	7120	C	ASN	I	218	−63.369	−52.279	70.037	1.00	84.87	D000	C
ATOM	7121	O	ASN	I	218	−64.349	−52.951	70.386	1.00	79.46	D000	O
ATOM	7122	CB	ASN	I	218	−62.928	−50.932	67.942	1.00	92.18	D000	C
ATOM	7123	CG	ASN	I	218	−63.905	−51.382	66.867	1.00	99.76	D000	C
ATOM	7124	OD1	ASN	I	218	−63.626	−51.249	65.669	1.00	98.33	D000	O
ATOM	7125	ND2	ASN	I	218	−65.059	−51.902	67.285	1.00	97.53	D000	N
ATOM	7126	N	GLY	I	219	−62.117	−52.679	70.279	1.00	81.16	D000	N
ATOM	7127	CA	GLY	I	219	−61.786	−54.004	70.763	1.00	72.74	D000	C
ATOM	7128	C	GLY	I	219	−60.286	−54.248	70.697	1.00	71.27	D000	C
ATOM	7129	O	GLY	I	219	−59.631	−54.504	71.715	1.00	64.68	D000	O
ATOM	7130	N	PRO	I	220	−59.712	−54.165	69.493	1.00	71.97	D000	N
ATOM	7131	CA	PRO	I	220	−58.254	−54.149	69.354	1.00	66.99	D000	C
ATOM	7132	C	PRO	I	220	−57.718	−52.723	69.288	1.00	65.66	D000	C
ATOM	7133	O	PRO	I	220	−58.435	−51.765	68.980	1.00	63.20	D000	O
ATOM	7134	CB	PRO	I	220	−58.025	−54.861	68.014	1.00	60.23	D000	C
ATOM	7135	CG	PRO	I	220	−59.311	−54.670	67.242	1.00	61.26	D000	C
ATOM	7136	CD	PRO	I	220	−60.369	−54.114	68.172	1.00	66.08	D000	C
ATOM	7137	N	TRP	I	221	−56.429	−52.596	69.586	1.00	55.14	D000	N
ATOM	7138	CA	TRP	I	221	−55.793	−51.292	69.545	1.00	47.35	D000	C
ATOM	7139	C	TRP	I	221	−55.622	−50.832	68.103	1.00	49.66	D000	C
ATOM	7140	O	TRP	I	221	−55.267	−51.614	67.218	1.00	47.87	D000	O
ATOM	7141	CB	TRP	I	221	−54.450	−51.345	70.262	1.00	52.11	D000	C
ATOM	7142	CG	TRP	I	221	−54.577	−51.541	71.768	1.00	58.06	D000	C
ATOM	7143	CD1	TRP	I	221	−54.489	−52.721	72.456	1.00	56.76	D000	C
ATOM	7144	CD2	TRP	I	221	−54.817	−50.524	72.754	1.00	56.97	D000	C
ATOM	7145	NE1	TRP	I	221	−54.650	−52.500	73.800	1.00	58.53	D000	N
ATOM	7146	CE2	TRP	I	221	−54.860	−51.163	74.012	1.00	57.57	D000	C
ATOM	7147	CE3	TRP	I	221	−54.999	−49.136	72.695	1.00	53.29	D000	C
ATOM	7148	CZ2	TRP	I	221	−55.078	−50.464	75.201	1.00	53.89	D000	C
ATOM	7149	CZ3	TRP	I	221	−55.211	−48.447	73.874	1.00	50.92	D000	C
ATOM	7150	CH2	TRP	I	221	−55.251	−49.113	75.110	1.00	52.06	D000	C
ATOM	7151	N	LYS	I	222	−55.888	−49.550	67.870	1.00	47.59	D000	N
ATOM	7152	CA	LYS	I	222	−55.833	−48.951	66.546	1.00	47.00	D000	C
ATOM	7153	C	LYS	I	222	−55.218	−47.565	66.654	1.00	47.01	D000	C
ATOM	7154	O	LYS	I	222	−55.421	−46.869	67.650	1.00	48.52	D000	O
ATOM	7155	CB	LYS	I	222	−57.240	−48.830	65.933	1.00	47.34	D000	C
ATOM	7156	CG	LYS	I	222	−58.076	−50.090	66.018	1.00	46.82	D000	C
ATOM	7157	CD	LYS	I	222	−59.483	−49.822	65.523	1.00	66.09	D000	C
ATOM	7158	CE	LYS	I	222	−60.297	−51.108	65.437	1.00	78.89	D000	C
ATOM	7159	NZ	LYS	I	222	−61.575	−50.950	64.682	1.00	75.65	D000	N1+
ATOM	7160	N	TRP	I	223	−54.475	−47.155	65.630	1.00	40.12	D000	N
ATOM	7161	CA	TRP	I	223	−54.033	−45.768	65.562	1.00	42.18	D000	C
ATOM	7162	C	TRP	I	223	−55.057	−44.910	64.815	1.00	40.82	D000	C
ATOM	7163	O	TRP	I	223	−55.674	−45.348	63.843	1.00	42.00	D000	O
ATOM	7164	CB	TRP	I	223	−52.654	−45.651	64.892	1.00	40.05	D000	C
ATOM	7165	CG	TRP	I	223	−51.497	−46.261	65.689	1.00	43.88	D000	C
ATOM	7166	CD1	TRP	I	223	−50.994	−47.529	65.568	1.00	43.26	D000	C
ATOM	7167	CD2	TRP	I	223	−50.711	−45.620	66.718	1.00	45.79	D000	C
ATOM	7168	NE1	TRP	I	223	−49.959	−47.722	66.455	1.00	40.92	D000	N
ATOM	7169	CE2	TRP	I	223	−49.761	−46.570	67.171	1.00	42.07	D000	C
ATOM	7170	CE3	TRP	I	223	−50.730	−44.341	67.310	1.00	40.91	D000	C
ATOM	7171	CZ2	TRP	I	223	−48.837	−46.284	68.182	1.00	38.74	D000	C
ATOM	7172	CZ3	TRP	I	223	−49.809	−44.054	68.305	1.00	37.29	D000	C
ATOM	7173	CH2	TRP	I	223	−48.872	−45.027	68.730	1.00	42.40	D000	C
ATOM	7174	N	VAL	I	224	−55.158	−43.642	65.220	1.00	35.57	D000	N
ATOM	7175	CA	VAL	I	224	−56.214	−42.782	64.710	1.00	38.56	D000	C
ATOM	7176	C	VAL	I	224	−56.046	−42.420	63.229	1.00	44.84	D000	C
ATOM	7177	O	VAL	I	224	−57.010	−41.965	62.593	1.00	41.50	D000	O
ATOM	7178	CB	VAL	I	224	−56.317	−41.511	65.574	1.00	38.88	D000	C
ATOM	7179	CG1	VAL	I	224	−56.643	−41.880	66.984	1.00	34.96	D000	C
ATOM	7180	CG2	VAL	I	224	−55.044	−40.664	65.498	1.00	36.68	D000	C
ATOM	7181	N	ASP	I	225	−54.854	−42.575	62.657	1.00	47.42	D000	N
ATOM	7182	CA	ASP	I	225	−54.634	−42.202	61.264	1.00	45.07	D000	C
ATOM	7183	C	ASP	I	225	−54.667	−43.405	60.323	1.00	47.81	D000	C
ATOM	7184	O	ASP	I	225	−54.433	−43.248	59.117	1.00	47.18	D000	O
ATOM	7185	CB	ASP	I	225	−53.316	−41.416	61.120	1.00	43.11	D000	C
ATOM	7186	CG	ASP	I	225	−52.062	−42.297	61.130	1.00	45.43	D000	C
ATOM	7187	OD1	ASP	I	225	−52.115	−43.489	61.519	1.00	41.39	D000	O
ATOM	7188	OD2	ASP	I	225	−50.996	−41.765	60.728	1.00	46.94	D000	O1−
ATOM	7189	N	GLY	I	226	−54.980	−44.593	60.847	1.00	47.45	D000	N
ATOM	7190	CA	GLY	I	226	−55.065	−45.811	60.081	1.00	41.79	D000	C
ATOM	7191	C	GLY	I	226	−53.833	−46.683	60.170	1.00	52.00	D000	C
ATOM	7192	O	GLY	I	226	−53.912	−47.876	59.850	1.00	56.10	D000	O
ATOM	7193	N	THR	I	227	−52.713	−46.128	60.647	1.00	51.85	D000	N
ATOM	7194	CA	THR	I	227	−51.473	−46.886	60.769	1.00	46.63	D000	C
ATOM	7195	C	THR	I	227	−51.717	−48.209	61.476	1.00	39.30	D000	C
ATOM	7196	O	THR	I	227	−52.498	−48.293	62.422	1.00	45.35	D000	O
ATOM	7197	CB	THR	I	227	−50.425	−46.078	61.535	1.00	41.84	D000	C
ATOM	7198	OG1	THR	I	227	−50.287	−44.782	60.931	1.00	39.58	D000	O
ATOM	7199	CG2	THR	I	227	−49.093	−46.792	61.502	1.00	32.58	D000	C
ATOM	7200	N	ASP	I	228	−51.097	−49.259	60.965	1.00	42.37	D000	N
ATOM	7201	CA	ASP	I	228	−51.312	−50.564	61.553	1.00	43.67	D000	C
ATOM	7202	C	ASP	I	228	−50.643	−50.637	62.911	1.00	47.41	D000	C
ATOM	7203	O	ASP	I	228	−49.510	−50.182	63.090	1.00	48.24	D000	O
ATOM	7204	CB	ASP	I	228	−50.780	−51.670	60.657	1.00	44.10	D000	C
ATOM	7205	CG	ASP	I	228	−50.886	−53.024	61.317	1.00	47.63	D000	C
ATOM	7206	OD1	ASP	I	228	−52.011	−53.436	61.652	1.00	48.15	D000	O
ATOM	7207	OD2	ASP	I	228	−49.842	−53.674	61.519	1.00	56.59	D000	O1−
ATOM	7208	N	TYR	I	229	−51.362	−51.196	63.878	1.00	48.84	D000	N
ATOM	7209	CA	TYR	I	229	−50.808	−51.333	65.220	1.00	52.99	D000	C
ATOM	7210	C	TYR	I	229	−49.895	−52.557	65.345	1.00	52.23	D000	C
ATOM	7211	O	TYR	I	229	−48.800	−52.471	65.919	1.00	51.49	D000	O
ATOM	7212	CB	TYR	I	229	−51.949	−51.395	66.243	1.00	46.59	D000	C
ATOM	7213	CG	TYR	I	229	−51.529	−51.806	67.625	1.00	44.81	D000	C
ATOM	7214	CD2	TYR	I	229	−51.533	−53.141	67.992	1.00	47.32	D000	C
ATOM	7215	CD1	TYR	I	229	−51.096	−50.875	68.549	1.00	47.52	D000	C
ATOM	7216	CE2	TYR	I	229	−51.138	−53.545	69.242	1.00	50.06	D000	C
ATOM	7217	CE1	TYR	I	229	−50.700	−51.268	69.830	1.00	49.62	D000	C
ATOM	7218	CZ	TYR	I	229	−50.723	−52.613	70.161	1.00	51.78	D000	C
ATOM	7219	OH	TYR	I	229	−50.341	−53.044	71.407	1.00	41.13	D000	O
ATOM	7220	N	GLU	I	230	−50.333	−53.705	64.828	1.00	53.05	D000	N
ATOM	7221	CA	GLU	I	230	−49.710	−54.967	65.221	1.00	54.20	D000	C
ATOM	7222	C	GLU	I	230	−48.276	−55.102	64.708	1.00	52.15	D000	C
ATOM	7223	O	GLU	I	230	−47.392	−55.578	65.430	1.00	54.02	D000	O
ATOM	7224	CB	GLU	I	230	−50.577	−56.134	64.766	1.00	60.03	D000	C
ATOM	7225	CG	GLU	I	230	−50.249	−57.386	65.539	1.00	67.01	D000	C
ATOM	7226	CD	GLU	I	230	−50.036	−57.099	67.016	1.00	66.61	D000	C
ATOM	7227	OE1	GLU	I	230	−51.027	−56.765	67.706	1.00	68.50	D000	O
ATOM	7228	OE2	GLU	I	230	−48.871	−57.189	67.479	1.00	67.23	D000	O1−
ATOM	7229	N	THR	I	231	−48.019	−54.721	63.470	1.00	52.10	D000	N
ATOM	7230	CA	THR	I	231	−46.651	−54.762	62.968	1.00	54.05	D000	C
ATOM	7231	C	THR	I	231	−45.864	−53.483	63.276	1.00	50.36	D000	C
ATOM	7232	O	THR	I	231	−44.664	−53.426	62.977	1.00	52.95	D000	O
ATOM	7233	CB	THR	I	231	−46.649	−55.055	61.450	1.00	52.18	D000	C
ATOM	7234	OG1	THR	I	231	−47.303	−53.996	60.732	1.00	44.52	D000	O
ATOM	7235	CG2	THR	I	231	−47.325	−56.388	61.140	1.00	44.56	D000	C
ATOM	7236	N	GLY	I	232	−46.494	−52.478	63.907	1.00	46.91	D000	N
ATOM	7237	CA	GLY	I	232	−45.878	−51.180	64.126	1.00	47.37	D000	C
ATOM	7238	C	GLY	I	232	−45.126	−51.024	65.460	1.00	47.60	D000	C
ATOM	7239	O	GLY	I	232	−45.082	−51.911	66.317	1.00	49.36	D000	O
ATOM	7240	N	PHE	I	233	−44.496	−49.860	65.599	1.00	41.36	D000	N
ATOM	7241	CA	PHE	I	233	−43.718	−49.535	66.789	1.00	43.90	D000	C
ATOM	7242	C	PHE	I	233	−44.583	−49.581	68.043	1.00	44.53	D000	C
ATOM	7243	O	PHE	I	233	−45.750	−49.180	68.019	1.00	48.88	D000	O
ATOM	7244	CB	PHE	I	233	−43.083	−48.144	66.644	1.00	46.48	D000	C
ATOM	7245	CG	PHE	I	233	−42.286	−47.729	67.846	1.00	53.61	D000	C
ATOM	7246	CD1	PHE	I	233	−40.995	−48.197	68.026	1.00	46.82	D000	C
ATOM	7247	CD2	PHE	I	233	−42.838	−46.911	68.820	1.00	52.29	D000	C
ATOM	7248	CE1	PHE	I	233	−40.276	−47.855	69.139	1.00	48.20	D000	C
ATOM	7249	CE2	PHE	I	233	−42.114	−46.558	69.940	1.00	45.86	D000	C
ATOM	7250	CZ	PHE	I	233	−40.831	−47.029	70.096	1.00	50.22	D000	C
ATOM	7251	N	LYS	I	234	−44.011	−50.083	69.143	1.00	41.34	D000	N
ATOM	7252	CA	LYS	I	234	−44.704	−50.159	70.428	1.00	44.31	D000	C
ATOM	7253	C	LYS	I	234	−43.739	−49.876	71.575	1.00	45.74	D000	C
ATOM	7254	O	LYS	I	234	−42.561	−50.223	71.499	1.00	52.26	D000	O
ATOM	7255	CB	LYS	I	234	−45.349	−51.532	70.647	1.00	50.12	D000	C
ATOM	7256	CG	LYS	I	234	−46.423	−51.935	69.649	1.00	46.91	D000	C
ATOM	7257	CD	LYS	I	234	−46.920	−53.333	69.980	1.00	41.34	D000	C
ATOM	7258	CE	LYS	I	234	−47.495	−53.986	68.756	1.00	52.95	D000	C
ATOM	7259	NZ	LYS	I	234	−46.449	−54.101	67.706	1.00	54.61	D000	N1+
ATOM	7260	N	ASN	I	235	−44.239	−49.255	72.646	1.00	46.61	D000	N
ATOM	7261	CA	ASN	I	235	−43.386	−48.905	73.785	1.00	40.27	D000	C
ATOM	7262	C	ASN	I	235	−44.180	−48.890	75.098	1.00	44.39	D000	C
ATOM	7263	O	ASN	I	235	−44.138	−47.925	75.865	1.00	45.23	D000	O
ATOM	7264	CB	ASN	I	235	−42.691	−47.564	73.545	1.00	38.53	D000	C
ATOM	7265	CG	ASN	I	235	−41.620	−47.270	74.577	1.00	40.11	D000	C
ATOM	7266	OD1	ASN	I	235	−40.990	−48.178	75.105	1.00	44.27	D000	O
ATOM	7267	ND2	ASN	I	235	−41.420	−46.000	74.879	1.00	41.29	D000	N
ATOM	7268	N	TRP	I	236	−44.905	−49.971	75.387	1.00	43.99	D000	N
ATOM	7269	CA	TRP	I	236	−45.720	−50.052	76.600	1.00	45.07	D000	C
ATOM	7270	C	TRP	I	236	−44.866	−50.125	77.866	1.00	46.24	D000	C
ATOM	7271	O	TRP	I	236	−43.739	−50.626	77.846	1.00	47.40	D000	O
ATOM	7272	CB	TRP	I	236	−46.614	−51.289	76.550	1.00	44.75	D000	C
ATOM	7273	CG	TRP	I	236	−47.647	−51.240	75.491	1.00	48.81	D000	C
ATOM	7274	CD1	TRP	I	236	−47.616	−51.876	74.288	1.00	46.27	D000	C
ATOM	7275	CD2	TRP	I	236	−48.878	−50.513	75.531	1.00	50.08	D000	C
ATOM	7276	NE1	TRP	I	236	−48.749	−51.591	73.573	1.00	46.50	D000	N
ATOM	7277	CE2	TRP	I	236	−49.543	−50.756	74.314	1.00	52.31	D000	C
ATOM	7278	CE3	TRP	I	236	−49.482	−49.680	76.480	1.00	48.48	D000	C
ATOM	7279	CZ2	TRP	I	236	−50.787	−50.195	74.018	1.00	53.44	D000	C
ATOM	7280	CZ3	TRP	I	236	−50.708	−49.126	76.192	1.00	49.54	D000	C
ATOM	7281	CH2	TRP	I	236	−51.354	−49.388	74.969	1.00	55.96	D000	C
ATOM	7282	N	ARG	I	237	−45.410	−49.600	78.981	1.00	46.86	D000	N
ATOM	7283	CA	ARG	I	237	−44.869	−49.924	80.304	1.00	52.81	D000	C
ATOM	7284	C	ARG	I	237	−45.128	−51.400	80.593	1.00	57.44	D000	C
ATOM	7285	O	ARG	I	237	−46.167	−51.926	80.193	1.00	65.84	D000	O
ATOM	7286	CB	ARG	I	237	−45.507	−49.082	81.421	1.00	48.92	D000	C
ATOM	7287	CG	ARG	I	237	−45.148	−47.579	81.479	1.00	52.62	D000	C
ATOM	7288	CD	ARG	I	237	−43.916	−47.207	82.346	1.00	51.01	D000	C
ATOM	7289	NE	ARG	I	237	−44.221	−47.118	83.786	1.00	55.72	D000	N
ATOM	7290	CZ	ARG	I	237	−44.309	−45.995	84.513	1.00	52.55	D000	C
ATOM	7291	NH1	ARG	I	237	−44.119	−44.796	83.979	1.00	44.43	D000	N1+
ATOM	7292	NH2	ARG	I	237	−44.588	−46.073	85.808	1.00	64.23	D000	N
ATOM	7293	N	PRO	I	238	−44.206	−52.094	81.259	1.00	64.01	D000	N
ATOM	7294	CA	PRO	I	238	−44.450	−53.500	81.615	1.00	65.03	D000	C
ATOM	7295	C	PRO	I	238	−45.771	−53.685	82.356	1.00	74.35	D000	C
ATOM	7296	O	PRO	I	238	−46.138	−52.874	83.210	1.00	79.19	D000	O
ATOM	7297	CB	PRO	I	238	−43.244	−53.846	82.493	1.00	66.34	D000	C
ATOM	7298	CG	PRO	I	238	−42.143	−53.019	81.911	1.00	66.55	D000	C
ATOM	7299	CD	PRO	I	238	−42.800	−51.710	81.488	1.00	66.32	D000	C
ATOM	7300	N	GLU	I	239	−46.483	−54.772	82.011	1.00	76.56	D000	N
ATOM	7301	CA	GLU	I	239	−47.850	−55.186	82.415	1.00	81.96	D000	C
ATOM	7302	C	GLU	I	239	−48.960	−54.622	81.521	1.00	85.73	D000	C
ATOM	7303	O	GLU	I	239	−50.134	−54.970	81.747	1.00	90.20	D000	O
ATOM	7304	CB	GLU	I	239	−48.223	−54.802	83.865	1.00	84.76	D000	C
ATOM	7305	CG	GLU	I	239	−48.026	−55.831	84.975	1.00	89.72	D000	C
ATOM	7306	CD	GLU	I	239	−49.063	−55.648	86.104	1.00	97.46	D000	C
ATOM	7307	OE1	GLU	I	239	−50.264	−55.495	85.787	1.00	95.00	D000	O
ATOM	7308	OE2	GLU	I	239	−48.689	−55.645	87.301	1.00	99.60	D000	O1−
ATOM	7309	N	GLN	I	240	−48.655	−53.809	80.513	1.00	78.77	D000	N
ATOM	7310	CA	GLN	I	240	−49.716	−53.126	79.762	1.00	74.65	D000	C
ATOM	7311	C	GLN	I	240	−49.744	−53.472	78.266	1.00	75.43	D000	C
ATOM	7312	O	GLN	I	240	−48.690	−53.736	77.678	1.00	70.27	D000	O
ATOM	7313	CB	GLN	I	240	−49.570	−51.610	79.956	1.00	69.99	D000	C
ATOM	7314	CG	GLN	I	240	−49.627	−51.179	81.421	1.00	73.64	D000	C
ATOM	7315	CD	GLN	I	240	−51.003	−51.423	82.047	1.00	79.48	D000	C
ATOM	7316	OE1	GLN	I	240	−51.278	−52.503	82.587	1.00	78.83	D000	O
ATOM	7317	NE2	GLN	I	240	−51.877	−50.413	81.968	1.00	68.96	D000	N
ATOM	7318	N	PRO	I	241	−50.945	−53.443	77.634	1.00	74.07	D000	N
ATOM	7319	CA	PRO	I	241	−52.250	−53.045	78.188	1.00	70.37	D000	C
ATOM	7320	C	PRO	I	241	−52.840	−54.061	79.178	1.00	75.66	D000	C
ATOM	7321	O	PRO	I	241	−53.904	−54.638	78.940	1.00	82.05	D000	O
ATOM	7322	CB	PRO	I	241	−53.129	−52.936	76.941	1.00	70.97	D000	C
ATOM	7323	CG	PRO	I	241	−52.543	−53.932	75.998	1.00	67.57	D000	C
ATOM	7324	CD	PRO	I	241	−51.061	−53.841	76.215	1.00	64.21	D000	C
ATOM	7325	N	GLY	I	252	−62.815	−49.790	79.716	1.00	70.62	D000	N
ATOM	7326	CA	GLY	I	252	−62.424	−49.267	81.017	1.00	74.95	D000	C
ATOM	7327	C	GLY	I	252	−61.035	−48.648	81.048	1.00	70.30	D000	C
ATOM	7328	O	GLY	I	252	−60.698	−47.871	81.940	1.00	66.65	D000	O
ATOM	7329	N	GLU	I	253	−60.214	−49.020	80.065	1.00	73.32	D000	N
ATOM	7330	CA	GLU	I	253	−58.880	−48.472	79.814	1.00	64.01	D000	C
ATOM	7331	C	GLU	I	253	−58.695	−48.525	78.298	1.00	60.63	D000	C
ATOM	7332	O	GLU	I	253	−57.927	−49.303	77.737	1.00	61.66	D000	O
ATOM	7333	CB	GLU	I	253	−57.775	−49.234	80.548	1.00	65.40	D000	C
ATOM	7334	CG	GLU	I	253	−57.837	−49.139	82.057	1.00	69.16	D000	C
ATOM	7335	CD	GLU	I	253	−57.007	−50.206	82.724	1.00	72.49	D000	C
ATOM	7336	OE1	GLU	I	253	−55.760	−50.161	82.597	1.00	66.87	D000	O
ATOM	7337	OE2	GLU	I	253	−57.610	−51.095	83.367	1.00	87.80	D000	O1−
ATOM	7338	N	ASP	I	254	−59.422	−47.662	77.607	1.00	59.36	D000	N
ATOM	7339	CA	ASP	I	254	−59.495	−47.720	76.163	1.00	59.89	D000	C
ATOM	7340	C	ASP	I	254	−58.603	−46.688	75.471	1.00	54.78	D000	C
ATOM	7341	O	ASP	I	254	−58.661	−46.575	74.247	1.00	56.31	D000	O
ATOM	7342	CB	ASP	I	254	−60.957	−47.546	75.721	1.00	67.74	D000	C
ATOM	7343	CG	ASP	I	254	−61.915	−48.563	76.378	1.00	69.29	D000	C
ATOM	7344	OD1	ASP	I	254	−61.449	−49.599	76.909	1.00	61.14	D000	O
ATOM	7345	OD2	ASP	I	254	−63.146	−48.308	76.361	1.00	69.38	D000	O1−
ATOM	7346	N	CYS	I	255	−57.789	−45.925	76.210	1.00	47.78	D000	N
ATOM	7347	CA	CYS	I	255	−56.967	−44.877	75.608	1.00	41.04	D000	C
ATOM	7348	C	CYS	I	255	−55.530	−44.924	76.117	1.00	39.20	D000	C
ATOM	7349	O	CYS	I	255	−55.295	−45.211	77.290	1.00	41.84	D000	O
ATOM	7350	CB	CYS	I	255	−57.559	−43.510	75.866	1.00	41.88	D000	C
ATOM	7351	SG	CYS	I	255	−59.123	−43.260	75.028	1.00	54.50	D000	S
ATOM	7352	N	ALA	I	256	−54.577	−44.614	75.230	1.00	35.83	D000	N
ATOM	7353	CA	ALA	I	256	−53.144	−44.757	75.487	1.00	36.99	D000	C
ATOM	7354	C	ALA	I	256	−52.466	−43.414	75.756	1.00	31.83	D000	C
ATOM	7355	O	ALA	I	256	−52.700	−42.427	75.047	1.00	30.75	D000	O
ATOM	7356	CB	ALA	I	256	−52.445	−45.428	74.300	1.00	37.73	D000	C
ATOM	7357	N	HIS	I	257	−51.584	−43.386	76.754	1.00	31.20	D000	N
ATOM	7358	CA	HIS	I	257	−50.871	−42.153	77.060	1.00	31.95	D000	C
ATOM	7359	C	HIS	I	257	−49.411	−42.453	77.347	1.00	31.16	D000	C
ATOM	7360	O	HIS	I	257	−49.056	−43.554	77.782	1.00	30.03	D000	O
ATOM	7361	CB	HIS	I	257	−51.523	−41.373	78.240	1.00	28.18	D000	C
ATOM	7362	CG	HIS	I	257	−51.545	−42.119	79.546	1.00	35.85	D000	C
ATOM	7363	ND1	HIS	I	257	−50.561	−41.985	80.501	1.00	32.60	D000	N
ATOM	7364	CD2	HIS	I	257	−52.433	−43.010	80.051	1.00	37.79	D000	C
ATOM	7365	CE1	HIS	I	257	−50.842	−42.756	81.535	1.00	33.70	D000	C
ATOM	7366	NE2	HIS	I	257	−51.975	−43.385	81.290	1.00	38.87	D000	N
ATOM	7367	N	PHE	I	258	−48.566	−41.458	77.069	1.00	32.31	D000	N
ATOM	7368	CA	PHE	I	258	−47.195	−41.470	77.550	1.00	29.99	D000	C
ATOM	7369	C	PHE	I	258	−47.186	−41.294	79.066	1.00	32.50	D000	C
ATOM	7370	O	PHE	I	258	−48.064	−40.659	79.648	1.00	28.89	D000	O
ATOM	7371	CB	PHE	I	258	−46.375	−40.346	76.926	1.00	31.38	D000	C
ATOM	7372	CG	PHE	I	258	−46.400	−40.303	75.434	1.00	30.17	D000	C
ATOM	7373	CD1	PHE	I	258	−45.501	−41.033	74.692	1.00	31.17	D000	C
ATOM	7374	CD2	PHE	I	258	−47.305	−39.487	74.769	1.00	35.10	D000	C
ATOM	7375	CE1	PHE	I	258	−45.522	−40.966	73.303	1.00	36.51	D000	C
ATOM	7376	CE2	PHE	I	258	−47.330	−39.415	73.380	1.00	33.32	D000	C
ATOM	7377	CZ	PHE	I	258	−46.440	−40.152	72.648	1.00	29.52	D000	C
ATOM	7378	N	THR	I	259	−46.212	−41.900	79.709	1.00	33.00	D000	N
ATOM	7379	CA	THR	I	259	−46.015	−41.713	81.132	1.00	34.18	D000	C
ATOM	7380	C	THR	I	259	−44.809	−40.809	81.341	1.00	36.61	D000	C
ATOM	7381	O	THR	I	259	−44.172	−40.339	80.389	1.00	38.23	D000	O
ATOM	7382	CB	THR	I	259	−45.834	−43.049	81.856	1.00	36.60	D000	C
ATOM	7383	OG1	THR	I	259	−44.598	−43.658	81.448	1.00	38.29	D000	O
ATOM	7384	CG2	THR	I	259	−47.006	−43.966	81.583	1.00	32.69	D000	C
ATOM	7385	N	ASP	I	260	−44.535	−40.524	82.610	1.00	36.88	D000	N
ATOM	7386	CA	ASP	I	260	−43.424	−39.664	82.983	1.00	36.02	D000	C
ATOM	7387	C	ASP	I	260	−42.065	−40.201	82.520	1.00	37.71	D000	C
ATOM	7388	O	ASP	I	260	−41.091	−39.443	82.545	1.00	42.78	D000	O
ATOM	7389	CB	ASP	I	260	−43.475	−39.440	84.501	1.00	38.98	D000	C
ATOM	7390	CG	ASP	I	260	−43.369	−40.730	85.292	1.00	40.08	D000	C
ATOM	7391	OD1	ASP	I	260	−43.567	−41.816	84.709	1.00	45.52	D000	O
ATOM	7392	OD2	ASP	I	260	−43.171	−40.658	86.518	1.00	38.74	D000	O1−
ATOM	7393	N	ASP	I	261	−41.964	−41.467	82.099	1.00	33.98	D000	N
ATOM	7394	CA	ASP	I	261	−40.713	−42.008	81.579	1.00	35.49	D000	C
ATOM	7395	C	ASP	I	261	−40.771	−42.320	80.090	1.00	41.58	D000	C
ATOM	7396	O	ASP	I	261	−39.833	−42.910	79.550	1.00	41.61	D000	O
ATOM	7397	CB	ASP	I	261	−40.289	−43.240	82.374	1.00	31.38	D000	C
ATOM	7398	CG	ASP	I	261	−41.194	−44.433	82.150	1.00	44.50	D000	C
ATOM	7399	OD1	ASP	I	261	−42.145	−44.348	81.338	1.00	49.19	D000	O
ATOM	7400	OD2	ASP	I	261	−40.992	−45.454	82.843	1.00	43.56	D000	O1−
ATOM	7401	N	GLY	I	262	−41.853	−41.954	79.414	1.00	43.44	D000	N
ATOM	7402	CA	GLY	I	262	−41.983	−42.127	77.991	1.00	39.17	D000	C
ATOM	7403	C	GLY	I	262	−42.711	−43.389	77.570	1.00	36.69	D000	C
ATOM	7404	O	GLY	I	262	−43.387	−43.377	76.537	1.00	31.77	D000	O
ATOM	7405	N	ARG	I	263	−42.625	−44.459	78.358	1.00	32.80	D000	N
ATOM	7406	CA	ARG	I	263	−43.300	−45.692	77.987	1.00	40.54	D000	C
ATOM	7407	C	ARG	I	263	−44.820	−45.549	78.138	1.00	42.34	D000	C
ATOM	7408	O	ARG	I	263	−45.332	−44.731	78.905	1.00	38.87	D000	O
ATOM	7409	CB	ARG	I	263	−42.773	−46.854	78.822	1.00	43.57	D000	C
ATOM	7410	CG	ARG	I	263	−41.309	−47.117	78.559	1.00	42.00	D000	C
ATOM	7411	CD	ARG	I	263	−40.789	−48.259	79.373	1.00	43.37	D000	C
ATOM	7412	NE	ARG	I	263	−41.000	−48.089	80.802	1.00	47.00	D000	N
ATOM	7413	CZ	ARG	I	263	−40.718	−49.024	81.706	1.00	54.61	D000	C
ATOM	7414	NH1	ARG	I	263	−40.206	−50.187	81.325	1.00	56.14	D000	N1+
ATOM	7415	NH2	ARG	I	263	−40.954	−48.806	82.995	1.00	57.34	D000	N
ATOM	7416	N	TRP	I	264	−45.545	−46.362	77.390	1.00	41.85	D000	N
ATOM	7417	CA	TRP	I	264	−46.964	−46.115	77.212	1.00	40.32	D000	C
ATOM	7418	C	TRP	I	264	−47.801	−46.797	78.282	1.00	39.94	D000	C
ATOM	7419	O	TRP	I	264	−47.377	−47.759	78.922	1.00	45.09	D000	O
ATOM	7420	CB	TRP	I	264	−47.427	−46.610	75.851	1.00	41.81	D000	C
ATOM	7421	CG	TRP	I	264	−46.709	−46.051	74.695	1.00	36.80	D000	C
ATOM	7422	CD1	TRP	I	264	−45.834	−45.016	74.688	1.00	37.17	D000	C
ATOM	7423	CD2	TRP	I	264	−46.807	−46.512	73.349	1.00	41.41	D000	C
ATOM	7424	NE1	TRP	I	264	−45.377	−44.795	73.417	1.00	37.55	D000	N
ATOM	7425	CE2	TRP	I	264	−45.957	−45.707	72.574	1.00	42.77	D000	C
ATOM	7426	CE3	TRP	I	264	−47.530	−47.534	72.724	1.00	37.74	D000	C
ATOM	7427	CZ2	TRP	I	264	−45.810	−45.888	71.205	1.00	40.50	D000	C
ATOM	7428	CZ3	TRP	I	264	−47.378	−47.716	71.383	1.00	38.97	D000	C
ATOM	7429	CH2	TRP	I	264	−46.536	−46.894	70.631	1.00	44.66	D000	C
ATOM	7430	N	ASN	I	265	−49.029	−46.309	78.432	1.00	37.04	D000	N
ATOM	7431	CA	ASN	I	265	−49.963	−46.923	79.356	1.00	37.46	D000	C
ATOM	7432	C	ASN	I	265	−51.387	−46.554	78.963	1.00	37.95	D000	C
ATOM	7433	O	ASN	I	265	−51.631	−45.512	78.353	1.00	36.28	D000	O
ATOM	7434	CB	ASN	I	265	−49.655	−46.518	80.791	1.00	40.53	D000	C
ATOM	7435	CG	ASN	I	265	−50.611	−47.123	81.765	1.00	49.10	D000	C
ATOM	7436	OD1	ASN	I	265	−50.635	−48.337	81.939	1.00	51.66	D000	O
ATOM	7437	ND2	ASN	I	265	−51.389	−46.281	82.440	1.00	49.67	D000	N
ATOM	7438	N	ASP	I	266	−52.314	−47.446	79.291	1.00	45.60	D000	N
ATOM	7439	CA	ASP	I	266	−53.738	−47.257	79.058	1.00	45.74	D000	C
ATOM	7440	C	ASP	I	266	−54.403	−46.761	80.331	1.00	47.12	D000	C
ATOM	7441	O	ASP	I	266	−54.070	−47.212	81.429	1.00	52.08	D000	O
ATOM	7442	CB	ASP	I	266	−54.413	−48.561	78.615	1.00	52.43	D000	C
ATOM	7443	CG	ASP	I	266	−54.095	−49.732	79.538	1.00	60.22	D000	C
ATOM	7444	OD1	ASP	I	266	−52.905	−49.973	79.827	1.00	64.14	D000	O
ATOM	7445	OD2	ASP	I	266	−55.035	−50.421	79.977	1.00	67.69	D000	O1−
ATOM	7446	N	ASP	I	267	−55.347	−45.838	80.176	1.00	44.83	D000	N
ATOM	7447	CA	ASP	I	267	−56.072	−45.253	81.295	1.00	49.89	D000	C
ATOM	7448	C	ASP	I	267	−57.475	−44.917	80.805	1.00	46.26	D000	C
ATOM	7449	O	ASP	I	267	−57.782	−45.069	79.623	1.00	47.12	D000	O
ATOM	7450	CB	ASP	I	267	−55.339	−44.020	81.860	1.00	46.24	D000	C
ATOM	7451	CG	ASP	I	267	−55.846	−43.631	83.228	1.00	48.24	D000	C
ATOM	7452	OD1	ASP	I	267	−56.671	−44.391	83.773	1.00	56.95	D000	O
ATOM	7453	OD2	ASP	I	267	−55.448	−42.573	83.754	1.00	49.05	D000	O1−
ATOM	7454	N	VAL	I	268	−58.347	−44.502	81.727	1.00	41.94	D000	N
ATOM	7455	CA	VAL	I	268	−59.707	−44.168	81.328	1.00	44.09	D000	C
ATOM	7456	C	VAL	I	268	−59.676	−42.946	80.419	1.00	44.94	D000	C
ATOM	7457	O	VAL	I	268	−58.896	−42.007	80.629	1.00	44.57	D000	O
ATOM	7458	CB	VAL	I	268	−60.606	−43.939	82.554	1.00	40.01	D000	C
ATOM	7459	CG1	VAL	I	268	−60.463	−45.079	83.506	1.00	42.61	D000	C
ATOM	7460	CG2	VAL	I	268	−60.274	−42.634	83.242	1.00	40.82	D000	C
ATOM	7461	N	CYS	I	269	−60.506	−42.962	79.379	1.00	38.74	D000	N
ATOM	7462	CA	CYS	I	269	−60.422	−41.901	78.385	1.00	41.24	D000	C
ATOM	7463	C	CYS	I	269	−60.908	−40.569	78.913	1.00	35.89	D000	C
ATOM	7464	O	CYS	I	269	−60.800	−39.554	78.219	1.00	40.53	D000	O
ATOM	7465	CB	CYS	I	269	−61.204	−42.298	77.127	1.00	43.34	D000	C
ATOM	7466	SG	CYS	I	269	−60.582	−43.835	76.370	1.00	57.52	D000	S
ATOM	7467	N	GLN	I	270	−61.422	−40.534	80.127	1.00	37.09	D000	N
ATOM	7468	CA	GLN	I	270	−61.959	−39.299	80.666	1.00	35.74	D000	C
ATOM	7469	C	GLN	I	270	−60.892	−38.406	81.284	1.00	33.91	D000	C
ATOM	7470	O	GLN	I	270	−61.156	−37.213	81.465	1.00	36.79	D000	O
ATOM	7471	CB	GLN	I	270	−63.029	−39.618	81.709	1.00	43.76	D000	C
ATOM	7472	CG	GLN	I	270	−64.394	−39.929	81.095	1.00	52.98	D000	C
ATOM	7473	CD	GLN	I	270	−64.451	−41.352	80.534	1.00	53.45	D000	C
ATOM	7474	OE1	GLN	I	270	−63.849	−42.272	81.106	1.00	52.07	D000	O
ATOM	7475	NE2	GLN	I	270	−65.156	−41.535	79.407	1.00	46.18	D000	N
ATOM	7476	N	ARG	I	271	−59.698	−38.940	81.589	1.00	33.55	D000	N
ATOM	7477	CA	ARG	I	271	−58.656	−38.139	82.228	1.00	34.17	D000	C
ATOM	7478	C	ARG	I	271	−58.333	−36.927	81.364	1.00	35.86	D000	C
ATOM	7479	O	ARG	I	271	−58.224	−37.058	80.136	1.00	34.42	D000	O
ATOM	7480	CB	ARG	I	271	−57.380	−38.947	82.464	1.00	36.48	D000	C
ATOM	7481	CG	ARG	I	271	−57.518	−40.084	83.447	1.00	39.60	D000	C
ATOM	7482	CD	ARG	I	271	−57.065	−39.699	84.838	1.00	45.14	D000	C
ATOM	7483	NE	ARG	I	271	−57.534	−40.662	85.844	1.00	59.73	D000	N
ATOM	7484	CZ	ARG	I	271	−58.422	−40.401	86.810	1.00	58.63	D000	C
ATOM	7485	NH1	ARG	I	271	−58.962	−39.185	86.947	1.00	54.22	D000	N1+
ATOM	7486	NH2	ARG	I	271	−58.758	−41.360	87.660	1.00	55.45	D000	N
ATOM	7487	N	PRO	I	272	−58.230	−35.749	81.936	1.00	32.00	D000	N
ATOM	7488	CA	PRO	I	272	−57.855	−34.553	81.148	1.00	29.00	D000	C
ATOM	7489	C	PRO	I	272	−56.342	−34.344	81.068	1.00	32.23	D000	C
ATOM	7490	O	PRO	I	272	−55.758	−33.416	81.633	1.00	31.22	D000	O
ATOM	7491	CB	PRO	I	272	−58.583	−33.433	81.892	1.00	26.05	D000	C
ATOM	7492	CG	PRO	I	272	−58.775	−33.959	83.324	1.00	28.86	D000	C
ATOM	7493	CD	PRO	I	272	−58.499	−35.435	83.347	1.00	27.78	D000	C
ATOM	7494	N	TYR	I	273	−55.680	−35.225	80.325	1.00	32.52	D000	N
ATOM	7495	CA	TYR	I	273	−54.251	−35.145	80.086	1.00	29.17	D000	C
ATOM	7496	C	TYR	I	273	−53.931	−34.170	78.946	1.00	28.33	D000	C
ATOM	7497	O	TYR	I	273	−54.790	−33.766	78.166	1.00	26.77	D000	O
ATOM	7498	CB	TYR	I	273	−53.689	−36.524	79.748	1.00	26.56	D000	C
ATOM	7499	CG	TYR	I	273	−53.687	−37.527	80.867	1.00	26.99	D000	C
ATOM	7500	CD1	TYR	I	273	−53.588	−37.129	82.194	1.00	29.63	D000	C
ATOM	7501	CD2	TYR	I	273	−53.757	−38.883	80.594	1.00	28.80	D000	C
ATOM	7502	CE1	TYR	I	273	−53.582	−38.057	83.212	1.00	28.90	D000	C
ATOM	7503	CE2	TYR	I	273	−53.737	−39.825	81.609	1.00	32.53	D000	C
ATOM	7504	CZ	TYR	I	273	−53.656	−39.404	82.911	1.00	29.59	D000	C
ATOM	7505	OH	TYR	I	273	−53.634	−40.338	83.910	1.00	29.82	D000	O
ATOM	7506	N	ARG	I	274	−52.672	−33.768	78.882	1.00	28.32	D000	N
ATOM	7507	CA	ARG	I	274	−52.212	−33.033	77.729	1.00	27.19	D000	C
ATOM	7508	C	ARG	I	274	−52.169	−33.971	76.536	1.00	26.48	D000	C
ATOM	7509	O	ARG	I	274	−52.280	−35.187	76.673	1.00	28.05	D000	O
ATOM	7510	CB	ARG	I	274	−50.857	−32.403	78.011	1.00	24.95	D000	C
ATOM	7511	CG	ARG	I	274	−50.926	−31.334	79.066	1.00	25.95	D000	C
ATOM	7512	CD	ARG	I	274	−49.541	−30.802	79.382	1.00	28.18	D000	C
ATOM	7513	NE	ARG	I	274	−49.548	−29.767	80.411	1.00	27.97	D000	N
ATOM	7514	CZ	ARG	I	274	−48.464	−29.347	81.063	1.00	29.49	D000	C
ATOM	7515	NH1	ARG	I	274	−47.274	−29.877	80.802	1.00	24.44	D000	N1+
ATOM	7516	NH2	ARG	I	274	−48.567	−28.400	81.992	1.00	28.37	D000	N
ATOM	7517	N	TRP	I	275	−52.038	−33.395	75.344	1.00	27.91	D000	N
ATOM	7518	CA	TRP	I	275	−52.039	−34.203	74.138	1.00	28.85	D000	C
ATOM	7519	C	TRP	I	275	−51.106	−33.568	73.105	1.00	30.78	D000	C
ATOM	7520	O	TRP	I	275	−50.671	−32.410	73.241	1.00	27.47	D000	O
ATOM	7521	CB	TRP	I	275	−53.473	−34.368	73.600	1.00	23.59	D000	C
ATOM	7522	CG	TRP	I	275	−54.009	−33.123	72.979	1.00	26.26	D000	C
ATOM	7523	CD1	TRP	I	275	−53.991	−32.808	71.648	1.00	26.24	D000	C
ATOM	7524	CD2	TRP	I	275	−54.629	−32.005	73.643	1.00	27.84	D000	C
ATOM	7525	NE1	TRP	I	275	−54.549	−31.571	71.442	1.00	27.63	D000	N
ATOM	7526	CE2	TRP	I	275	−54.959	−31.059	72.646	1.00	29.00	D000	C
ATOM	7527	CE3	TRP	I	275	−54.949	−31.718	74.971	1.00	27.22	D000	C
ATOM	7528	CZ2	TRP	I	275	−55.589	−29.850	72.941	1.00	23.11	D000	C
ATOM	7529	CZ3	TRP	I	275	−55.572	−30.511	75.258	1.00	26.94	D000	C
ATOM	7530	CH2	TRP	I	275	−55.876	−29.595	74.248	1.00	27.13	D000	C
ATOM	7531	N	VAL	I	276	−50.827	−34.338	72.051	1.00	26.77	D000	N
ATOM	7532	CA	VAL	I	276	−49.950	−33.930	70.959	1.00	29.58	D000	C
ATOM	7533	C	VAL	I	276	−50.723	−34.063	69.650	1.00	29.99	D000	C
ATOM	7534	O	VAL	I	276	−51.233	−35.146	69.335	1.00	32.34	D000	O
ATOM	7535	CB	VAL	I	276	−48.666	−34.790	70.916	1.00	34.01	D000	C
ATOM	7536	CG1	VAL	I	276	−47.726	−34.358	69.768	1.00	25.34	D000	C
ATOM	7537	CG2	VAL	I	276	−47.957	−34.821	72.259	1.00	22.27	D000	C
ATOM	7538	N	CYS	I	277	−50.815	−32.973	68.892	1.00	30.05	D000	N
ATOM	7539	CA	CYS	I	277	−51.289	−33.032	67.507	1.00	36.56	D000	C
ATOM	7540	C	CYS	I	277	−50.113	−33.216	66.544	1.00	39.90	D000	C
ATOM	7541	O	CYS	I	277	−49.037	−32.638	66.739	1.00	34.93	D000	O
ATOM	7542	CB	CYS	I	277	−52.054	−31.764	67.111	1.00	33.98	D000	C
ATOM	7543	SG	CYS	I	277	−53.711	−31.466	67.812	1.00	42.15	D000	S
ATOM	7544	N	GLU	I	278	−50.336	−34.004	65.486	1.00	37.84	D000	N
ATOM	7545	CA	GLU	I	278	−49.361	−34.207	64.419	1.00	38.01	D000	C
ATOM	7546	C	GLU	I	278	−49.980	−33.930	63.054	1.00	40.54	D000	C
ATOM	7547	O	GLU	I	278	−51.105	−34.354	62.766	1.00	41.44	D000	O
ATOM	7548	CB	GLU	I	278	−48.801	−35.646	64.430	1.00	36.62	D000	C
ATOM	7549	CG	GLU	I	278	−47.685	−35.926	63.414	1.00	36.43	D000	C
ATOM	7550	CD	GLU	I	278	−47.249	−37.379	63.472	1.00	44.33	D000	C
ATOM	7551	OE1	GLU	I	278	−47.852	−38.105	64.290	1.00	43.28	D000	O
ATOM	7552	OE2	GLU	I	278	−46.341	−37.806	62.708	1.00	44.12	D000	O1−
ATOM	7553	N	THR	I	279	−49.215	−33.280	62.187	1.00	40.86	D000	N
ATOM	7554	CA	THR	I	279	−49.596	−33.153	60.789	1.00	45.51	D000	C
ATOM	7555	C	THR	I	279	−48.349	−33.290	59.921	1.00	50.70	D000	C
ATOM	7556	O	THR	I	279	−47.274	−32.791	60.269	1.00	52.15	D000	O
ATOM	7557	CB	THR	I	279	−50.344	−31.830	60.515	1.00	40.68	D000	C
ATOM	7558	OG1	THR	I	279	−50.995	−31.916	59.247	1.00	46.37	D000	O
ATOM	7559	CG2	THR	I	279	−49.413	−30.622	60.530	1.00	40.76	D000	C
ATOM	7560	N	GLU	I	280	−48.502	−33.993	58.801	1.00	51.69	D000	N
ATOM	7561	CA	GLU	I	280	−47.419	−34.287	57.872	1.00	49.36	D000	C
ATOM	7562	C	GLU	I	280	−47.271	−33.158	56.860	1.00	56.06	D000	C
ATOM	7563	O	GLU	I	280	−48.253	−32.530	56.466	1.00	60.37	D000	O
ATOM	7564	CB	GLU	I	280	−47.687	−35.615	57.154	1.00	46.67	D000	C
ATOM	7565	CG	GLU	I	280	−47.603	−36.893	58.036	1.00	52.72	D000	C
ATOM	7566	CD	GLU	I	280	−48.756	−37.083	59.067	1.00	61.50	D000	C
ATOM	7567	OE1	GLU	I	280	−49.701	−36.259	59.124	1.00	55.57	D000	O
ATOM	7568	OE2	GLU	I	280	−48.724	−38.095	59.816	1.00	65.48	D000	O1−
ATOM	7569	N	LEU	I	281	−46.024	−32.894	56.450	1.00	68.28	D000	N
ATOM	7570	CA	LEU	I	281	−45.668	−31.688	55.705	1.00	66.92	D000	C
ATOM	7571	C	LEU	I	281	−45.742	−31.880	54.192	1.00	77.57	D000	C
ATOM	7572	O	LEU	I	281	−45.234	−31.029	53.454	1.00	82.51	D000	O
ATOM	7573	CB	LEU	I	281	−44.264	−31.217	56.095	1.00	62.30	D000	C
ATOM	7574	CG	LEU	I	281	−44.155	−29.845	56.772	1.00	72.01	D000	C
ATOM	7575	CD1	LEU	I	281	−42.720	−29.512	57.120	1.00	70.45	D000	C
ATOM	7576	CD2	LEU	I	281	−44.746	−28.748	55.893	1.00	76.75	D000	C
ATOM	7577	N	ASP	I	282	−46.399	−32.958	53.737	1.00	85.50	D000	N
ATOM	7578	CA	ASP	I	282	−46.623	−33.356	52.326	1.00	86.01	D000	C
ATOM	7579	C	ASP	I	282	−45.384	−34.002	51.715	1.00	79.75	D000	C
ATOM	7580	O	ASP	I	282	−45.258	−35.228	51.711	1.00	78.04	D000	O
ATOM	7581	CB	ASP	I	282	−47.092	−32.180	51.440	1.00	96.47	D000	C
ATOM	7582	CG	ASP	I	282	−48.461	−31.617	51.857	1.00	96.65	D000	C
ATOM	7583	OD1	ASP	I	282	−48.811	−31.701	53.055	1.00	90.88	D000	O
ATOM	7584	OD2	ASP	I	282	−49.190	−31.087	50.977	1.00	93.64	D000	O1−
TER
ATOM	7585	N	THR	P	152	−18.008	−35.866	53.223	1.00	83.74	D000	N
ATOM	7586	CA	THR	P	152	−19.403	−36.301	53.203	1.00	93.67	D000	C
ATOM	7587	C	THR	P	152	−19.882	−36.656	54.610	1.00	97.43	D000	C
ATOM	7588	O	THR	P	152	−21.055	−36.465	54.949	1.00	99.74	D000	O
ATOM	7589	CB	THR	P	152	−19.616	−37.526	52.274	1.00	95.00	D000	C
ATOM	7590	OG1	THR	P	152	−18.515	−38.434	52.412	1.00	96.24	D000	O
ATOM	7591	CG2	THR	P	152	−19.745	−37.100	50.820	1.00	89.07	D000	C
ATOM	7592	N	CYS	P	153	−18.962	−37.176	55.422	1.00	93.53	D000	N
ATOM	7593	CA	CYS	P	153	−19.248	−37.564	56.798	1.00	86.06	D000	C
ATOM	7594	C	CYS	P	153	−18.009	−37.320	57.642	1.00	73.09	D000	C
ATOM	7595	O	CYS	P	153	−16.902	−37.129	57.131	1.00	68.83	D000	O
ATOM	7596	CB	CYS	P	153	−19.718	−39.025	56.941	1.00	85.43	D000	C
ATOM	7597	SG	CYS	P	153	−21.535	−39.281	56.843	1.00	98.27	D000	S
ATOM	7598	N	CYS	P	154	−18.209	−37.292	58.847	1.00	71.85	D000	N
ATOM	7599	CA	CYS	P	154	−17.147	−37.059	59.803	1.00	58.19	D000	C
ATOM	7600	C	CYS	P	154	−16.521	−38.377	60.251	1.00	53.75	D000	C
ATOM	7601	O	CYS	P	154	−17.198	−39.409	60.291	1.00	57.74	D000	O
ATOM	7602	CB	CYS	P	154	−17.697	−36.308	61.010	1.00	51.76	D000	C
ATOM	7603	SG	CYS	P	154	−18.273	−34.615	60.600	1.00	60.05	D000	S
ATOM	7604	N	PRO	P	155	−15.231	−38.360	60.584	1.00	46.56	D000	N
ATOM	7605	CA	PRO	P	155	−14.547	−39.591	61.004	1.00	44.27	D000	C
ATOM	7606	C	PRO	P	155	−15.153	−40.210	62.258	1.00	48.95	D000	C
ATOM	7607	O	PRO	P	155	−15.934	−39.588	62.987	1.00	49.26	D000	O
ATOM	7608	CB	PRO	P	155	−13.109	−39.126	61.268	1.00	42.58	D000	C
ATOM	7609	CG	PRO	P	155	−12.971	−37.842	60.535	1.00	40.45	D000	C
ATOM	7610	CD	PRO	P	155	−14.317	−37.209	60.522	1.00	44.50	D000	C
ATOM	7611	N	VAL	P	156	−14.786	−41.475	62.492	1.00	50.73	D000	N
ATOM	7612	CA	VAL	P	156	−15.268	−42.191	63.670	1.00	48.55	D000	C
ATOM	7613	C	VAL	P	156	−14.926	−41.390	64.914	1.00	49.57	D000	C
ATOM	7614	O	VAL	P	156	−13.791	−40.923	65.071	1.00	49.11	D000	O
ATOM	7615	CB	VAL	P	156	−14.658	−43.599	63.733	1.00	49.04	D000	C
ATOM	7616	CG1	VAL	P	156	−15.733	−44.639	63.993	1.00	37.71	D000	C
ATOM	7617	CG2	VAL	P	156	−13.879	−43.914	62.449	1.00	56.31	D000	C
ATOM	7618	N	ASN	P	157	−15.919	−41.205	65.791	1.00	49.29	D000	N
ATOM	7619	CA	ASN	P	157	−15.831	−40.490	67.074	1.00	45.69	D000	C
ATOM	7620	C	ASN	P	157	−15.791	−38.976	66.917	1.00	42.84	D000	C
ATOM	7621	O	ASN	P	157	−15.571	−38.265	67.913	1.00	42.59	D000	O
ATOM	7622	CB	ASN	P	157	−14.592	−40.896	67.878	1.00	46.95	D000	C
ATOM	7623	CG	ASN	P	157	−14.548	−42.372	68.177	1.00	48.62	D000	C
ATOM	7624	OD1	ASN	P	157	−15.544	−42.976	68.582	1.00	51.67	D000	O
ATOM	7625	ND2	ASN	P	157	−13.396	−42.973	67.937	1.00	38.36	D000	N
ATOM	7626	N	TRP	P	158	−16.009	−38.453	65.719	1.00	42.42	D000	N
ATOM	7627	CA	TRP	P	158	−16.226	−37.030	65.523	1.00	41.39	D000	C
ATOM	7628	C	TRP	P	158	−17.714	−36.789	65.274	1.00	42.54	D000	C
ATOM	7629	O	TRP	P	158	−18.454	−37.697	64.895	1.00	47.35	D000	O
ATOM	7630	CB	TRP	P	158	−15.395	−36.490	64.348	1.00	38.79	D000	C
ATOM	7631	CG	TRP	P	158	−13.877	−36.545	64.488	1.00	37.39	D000	C
ATOM	7632	CD1	TRP	P	158	−13.107	−37.655	64.704	1.00	39.44	D000	C
ATOM	7633	CD2	TRP	P	158	−12.955	−35.444	64.366	1.00	35.99	D000	C
ATOM	7634	NE1	TRP	P	158	−11.763	−37.316	64.728	1.00	31.69	D000	N
ATOM	7635	CE2	TRP	P	158	−11.644	−35.969	64.524	1.00	34.45	D000	C
ATOM	7636	CE3	TRP	P	158	−13.107	−34.070	64.140	1.00	35.66	D000	C
ATOM	7637	CZ2	TRP	P	158	−10.501	−35.165	64.471	1.00	30.75	D000	C
ATOM	7638	CZ3	TRP	P	158	−11.970	−33.273	64.083	1.00	35.96	D000	C
ATOM	7639	CH2	TRP	P	158	−10.681	−33.827	64.247	1.00	31.46	D000	C
ATOM	7640	N	VAL	P	159	−18.149	−35.554	65.509	1.00	37.16	D000	N
ATOM	7641	CA	VAL	P	159	−19.556	−35.188	65.499	1.00	34.88	D000	C
ATOM	7642	C	VAL	P	159	−19.788	−34.115	64.443	1.00	38.07	D000	C
ATOM	7643	O	VAL	P	159	−19.116	−33.083	64.447	1.00	39.78	D000	O
ATOM	7644	CB	VAL	P	159	−19.996	−34.693	66.885	1.00	37.29	D000	C
ATOM	7645	CG1	VAL	P	159	−21.462	−34.286	66.872	1.00	33.76	D000	C
ATOM	7646	CG2	VAL	P	159	−19.717	−35.762	67.920	1.00	35.15	D000	C
ATOM	7647	N	GLU	P	160	−20.747	−34.346	63.548	1.00	44.59	D000	N
ATOM	7648	CA	GLU	P	160	−21.060	−33.351	62.529	1.00	41.41	D000	C
ATOM	7649	C	GLU	P	160	−22.016	−32.294	63.071	1.00	42.80	D000	C
ATOM	7650	O	GLU	P	160	−22.890	−32.577	63.894	1.00	40.17	D000	O
ATOM	7651	CB	GLU	P	160	−21.661	−34.005	61.284	1.00	46.52	D000	C
ATOM	7652	CG	GLU	P	160	−21.512	−33.122	60.047	1.00	56.68	D000	C
ATOM	7653	CD	GLU	P	160	−22.207	−33.644	58.800	1.00	66.43	D000	C
ATOM	7654	OE1	GLU	P	160	−22.148	−34.876	58.533	1.00	67.75	D000	O
ATOM	7655	OE2	GLU	P	160	−22.785	−32.796	58.074	1.00	67.82	D000	O1−
ATOM	7656	N	HIS	P	161	−21.824	−31.060	62.622	1.00	42.59	D000	N
ATOM	7657	CA	HIS	P	161	−22.738	−29.980	62.952	1.00	40.24	D000	C
ATOM	7658	C	HIS	P	161	−22.456	−28.824	62.011	1.00	43.60	D000	C
ATOM	7659	O	HIS	P	161	−21.382	−28.220	62.096	1.00	45.56	D000	O
ATOM	7660	CB	HIS	P	161	−22.588	−29.557	64.413	1.00	35.89	D000	C
ATOM	7661	CG	HIS	P	161	−23.438	−28.383	64.790	1.00	44.75	D000	C
ATOM	7662	ND1	HIS	P	161	−24.736	−28.521	65.238	1.00	41.80	D000	N
ATOM	7663	CD2	HIS	P	161	−23.178	−27.050	64.788	1.00	44.31	D000	C
ATOM	7664	CE1	HIS	P	161	−25.239	−27.324	65.496	1.00	44.21	D000	C
ATOM	7665	NE2	HIS	P	161	−24.315	−26.415	65.231	1.00	47.45	D000	N
ATOM	7666	N	GLU	P	162	−23.391	−28.535	61.098	1.00	46.24	D000	N
ATOM	7667	CA	GLU	P	162	−23.294	−27.382	60.201	1.00	47.89	D000	C
ATOM	7668	C	GLU	P	162	−22.059	−27.512	59.301	1.00	50.82	D000	C
ATOM	7669	O	GLU	P	162	−21.272	−26.573	59.127	1.00	44.74	D000	O
ATOM	7670	CB	GLU	P	162	−23.249	−26.082	61.009	1.00	53.01	D000	C
ATOM	7671	CG	GLU	P	162	−24.485	−25.787	61.849	1.00	58.08	D000	C
ATOM	7672	CD	GLU	P	162	−25.529	−24.958	61.127	1.00	70.25	D000	C
ATOM	7673	OE1	GLU	P	162	−25.288	−23.740	60.921	1.00	71.49	D000	O
ATOM	7674	OE2	GLU	P	162	−26.575	−25.529	60.746	1.00	76.35	D000	O1−
ATOM	7675	N	ARG	P	163	−21.884	−28.714	58.744	1.00	48.09	D000	N
ATOM	7676	CA	ARG	P	163	−20.780	−29.023	57.836	1.00	57.37	D000	C
ATOM	7677	C	ARG	P	163	−19.428	−28.733	58.490	1.00	57.98	D000	C
ATOM	7678	O	ARG	P	163	−18.464	−28.324	57.834	1.00	57.75	D000	O
ATOM	7679	CB	ARG	P	163	−20.918	−28.307	56.486	1.00	60.45	D000	C
ATOM	7680	CG	ARG	P	163	−22.191	−28.694	55.747	1.00	58.49	D000	C
ATOM	7681	CD	ARG	P	163	−22.201	−28.270	54.296	1.00	71.93	D000	C
ATOM	7682	NE	ARG	P	163	−21.240	−29.050	53.518	1.00	71.00	D000	N
ATOM	7683	CZ	ARG	P	163	−20.116	−28.576	52.983	1.00	75.19	D000	C
ATOM	7684	NH1	ARG	P	163	−19.331	−29.398	52.298	1.00	77.55	D000	N1+
ATOM	7685	NH2	ARG	P	163	−19.773	−27.296	53.117	1.00	67.90	D000	N
ATOM	7686	N	SER	P	164	−19.350	−28.961	59.794	1.00	55.73	D000	N
ATOM	7687	CA	SER	P	164	−18.096	−28.955	60.520	1.00	45.84	D000	C
ATOM	7688	C	SER	P	164	−18.058	−30.235	61.329	1.00	47.92	D000	C
ATOM	7689	O	SER	P	164	−19.103	−30.761	61.727	1.00	45.64	D000	O
ATOM	7690	CB	SER	P	164	−17.950	−27.732	61.415	1.00	45.00	D000	C
ATOM	7691	OG	SER	P	164	−17.414	−26.645	60.673	1.00	53.08	D000	O
ATOM	7692	N	CYS	P	165	−16.854	−30.786	61.464	1.00	44.78	D000	N
ATOM	7693	CA	CYS	P	165	−16.607	−31.976	62.262	1.00	41.69	D000	C
ATOM	7694	C	CYS	P	165	−15.855	−31.593	63.523	1.00	41.12	D000	C
ATOM	7695	O	CYS	P	165	−14.843	−30.886	63.464	1.00	42.93	D000	O
ATOM	7696	CB	CYS	P	165	−15.813	−33.009	61.472	1.00	49.43	D000	C
ATOM	7697	SG	CYS	P	165	−16.607	−33.584	59.964	1.00	54.63	D000	S
ATOM	7698	N	TYR	P	166	−16.342	−32.073	64.651	1.00	38.95	D000	N
ATOM	7699	CA	TYR	P	166	−15.815	−31.709	65.949	1.00	35.52	D000	C
ATOM	7700	C	TYR	P	166	−15.385	−32.965	66.674	1.00	36.03	D000	C
ATOM	7701	O	TYR	P	166	−16.004	−34.021	66.524	1.00	35.78	D000	O
ATOM	7702	CB	TYR	P	166	−16.857	−30.955	66.776	1.00	34.96	D000	C
ATOM	7703	CG	TYR	P	166	−17.320	−29.668	66.153	1.00	36.68	D000	C
ATOM	7704	CD1	TYR	P	166	−18.334	−29.650	65.195	1.00	32.91	D000	C
ATOM	7705	CD2	TYR	P	166	−16.732	−28.461	66.513	1.00	33.68	D000	C
ATOM	7706	CE1	TYR	P	166	−18.753	−28.447	64.630	1.00	36.09	D000	C
ATOM	7707	CE2	TYR	P	166	−17.141	−27.259	65.953	1.00	30.23	D000	C
ATOM	7708	CZ	TYR	P	166	−18.149	−27.251	65.019	1.00	35.59	D000	C
ATOM	7709	OH	TYR	P	166	−18.541	−26.044	64.482	1.00	35.19	D000	O
ATOM	7710	N	TRP	P	167	−14.307	−32.851	67.435	1.00	34.48	D000	N
ATOM	7711	CA	TRP	P	167	−13.853	−33.934	68.284	1.00	32.86	D000	C
ATOM	7712	C	TRP	P	167	−13.586	−33.377	69.678	1.00	34.10	D000	C
ATOM	7713	O	TRP	P	167	−12.924	−32.339	69.820	1.00	34.23	D000	O
ATOM	7714	CB	TRP	P	167	−12.613	−34.593	67.695	1.00	31.80	D000	C
ATOM	7715	CG	TRP	P	167	−12.104	−35.731	68.511	1.00	33.09	D000	C
ATOM	7716	CD1	TRP	P	167	−12.489	−37.025	68.430	1.00	33.37	D000	C
ATOM	7717	CD2	TRP	P	167	−11.128	−35.664	69.554	1.00	28.44	D000	C
ATOM	7718	NE1	TRP	P	167	−11.793	−37.780	69.336	1.00	29.92	D000	N
ATOM	7719	CE2	TRP	P	167	−10.948	−36.966	70.036	1.00	29.30	D000	C
ATOM	7720	CE3	TRP	P	167	−10.351	−34.629	70.091	1.00	31.68	D000	C
ATOM	7721	CZ2	TRP	P	167	−10.034	−37.270	71.048	1.00	34.20	D000	C
ATOM	7722	CZ3	TRP	P	167	−9.442	−34.929	71.100	1.00	32.44	D000	C
ATOM	7723	CH2	TRP	P	167	−9.294	−36.236	71.570	1.00	30.38	D000	C
ATOM	7724	N	PHE	P	168	−14.102	−34.066	70.699	1.00	30.71	D000	N
ATOM	7725	CA	PHE	P	168	−14.055	−33.612	72.088	1.00	32.96	D000	C
ATOM	7726	C	PHE	P	168	−13.115	−34.503	72.884	1.00	29.97	D000	C
ATOM	7727	O	PHE	P	168	−13.354	−35.706	73.001	1.00	33.55	D000	O
ATOM	7728	CB	PHE	P	168	−15.460	−33.603	72.691	1.00	26.93	D000	C
ATOM	7729	CG	PHE	P	168	−16.381	−32.711	71.950	1.00	26.93	D000	C
ATOM	7730	CD1	PHE	P	168	−16.509	−31.381	72.314	1.00	25.66	D000	C
ATOM	7731	CD2	PHE	P	168	−17.057	−33.170	70.831	1.00	28.28	D000	C
ATOM	7732	CE1	PHE	P	168	−17.335	−30.515	71.594	1.00	29.79	D000	C
ATOM	7733	CE2	PHE	P	168	−17.877	−32.328	70.108	1.00	30.00	D000	C
ATOM	7734	CZ	PHE	P	168	−18.025	−30.988	70.490	1.00	26.93	D000	C
ATOM	7735	N	SER	P	169	−12.026	−33.922	73.385	1.00	30.64	D000	N
ATOM	7736	CA	SER	P	169	−11.061	−34.707	74.145	1.00	34.97	D000	C
ATOM	7737	C	SER	P	169	−11.675	−35.155	75.471	1.00	27.83	D000	C
ATOM	7738	O	SER	P	169	−12.547	−34.495	76.036	1.00	28.09	D000	O
ATOM	7739	CB	SER	P	169	−9.761	−33.908	74.389	1.00	29.33	D000	C
ATOM	7740	OG	SER	P	169	−9.906	−32.926	75.407	1.00	28.03	D000	O
ATOM	7741	N	ARG	P	170	−11.219	−36.298	75.960	1.00	26.00	D000	N
ATOM	7742	CA	ARG	P	170	−11.564	−36.758	77.295	1.00	31.89	D000	C
ATOM	7743	C	ARG	P	170	−10.359	−36.735	78.233	1.00	33.73	D000	C
ATOM	7744	O	ARG	P	170	−10.416	−37.279	79.337	1.00	35.93	D000	O
ATOM	7745	CB	ARG	P	170	−12.183	−38.148	77.207	1.00	26.68	D000	C
ATOM	7746	CG	ARG	P	170	−12.874	−38.607	78.430	1.00	33.68	D000	C
ATOM	7747	CD	ARG	P	170	−14.298	−38.263	78.356	1.00	32.40	D000	C
ATOM	7748	NE	ARG	P	170	−15.029	−38.782	79.492	1.00	28.94	D000	N
ATOM	7749	CZ	ARG	P	170	−15.923	−38.060	80.155	1.00	29.78	D000	C
ATOM	7750	NH1	ARG	P	170	−16.586	−38.582	81.182	1.00	24.35	D000	N1+
ATOM	7751	NH2	ARG	P	170	−16.137	−36.805	79.779	1.00	23.51	D000	N
ATOM	7752	N	SER	P	171	−9.256	−36.149	77.801	1.00	29.68	D000	N
ATOM	7753	CA	SER	P	171	−8.088	−35.943	78.633	1.00	26.30	D000	C
ATOM	7754	C	SER	P	171	−7.684	−34.481	78.520	1.00	31.62	D000	C
ATOM	7755	O	SER	P	171	−8.299	−33.707	77.774	1.00	33.43	D000	O
ATOM	7756	CB	SER	P	171	−6.959	−36.886	78.220	1.00	26.16	D000	C
ATOM	7757	OG	SER	P	171	−6.679	−36.700	76.857	1.00	32.31	D000	O
ATOM	7758	N	GLY	P	172	−6.662	−34.095	79.290	1.00	28.87	D000	N
ATOM	7759	CA	GLY	P	172	−6.215	−32.713	79.329	1.00	27.34	D000	C
ATOM	7760	C	GLY	P	172	−4.841	−32.482	78.725	1.00	28.11	D000	C
ATOM	7761	O	GLY	P	172	−4.034	−33.407	78.627	1.00	29.36	D000	O
ATOM	7762	N	LYS	P	173	−4.567	−31.249	78.312	1.00	26.28	D000	N
ATOM	7763	CA	LYS	P	173	−3.311	−30.891	77.669	1.00	28.99	D000	C
ATOM	7764	C	LYS	P	173	−3.133	−29.390	77.801	1.00	31.16	D000	C
ATOM	7765	O	LYS	P	173	−4.101	−28.640	77.686	1.00	26.89	D000	O
ATOM	7766	CB	LYS	P	173	−3.274	−31.249	76.168	1.00	29.64	D000	C
ATOM	7767	CG	LYS	P	173	−3.023	−32.712	75.792	1.00	25.52	D000	C
ATOM	7768	CD	LYS	P	173	−2.577	−32.794	74.349	1.00	26.55	D000	C
ATOM	7769	CE	LYS	P	173	−2.684	−34.206	73.811	1.00	33.01	D000	C
ATOM	7770	NZ	LYS	P	173	−1.755	−35.154	74.459	1.00	35.05	D000	N1+
ATOM	7771	N	ALA	P	174	−1.890	−28.962	78.015	1.00	32.75	D000	N
ATOM	7772	CA	ALA	P	174	−1.556	−27.556	77.874	1.00	30.91	D000	C
ATOM	7773	C	ALA	P	174	−1.960	−27.069	76.483	1.00	32.66	D000	C
ATOM	7774	O	ALA	P	174	−1.967	−27.838	75.511	1.00	28.87	D000	O
ATOM	7775	CB	ALA	P	174	−0.062	−27.349	78.113	1.00	32.92	D000	C
ATOM	7776	N	TRP	P	175	−2.308	−25.777	76.396	1.00	31.13	D000	N
ATOM	7777	CA	TRP	P	175	−2.873	−25.232	75.157	1.00	35.20	D000	C
ATOM	7778	C	TRP	P	175	−1.991	−25.526	73.942	1.00	35.94	D000	C
ATOM	7779	O	TRP	P	175	−2.491	−25.919	72.884	1.00	31.80	D000	O
ATOM	7780	CB	TRP	P	175	−3.105	−23.719	75.294	1.00	35.59	D000	C
ATOM	7781	CG	TRP	P	175	−3.896	−23.089	74.131	1.00	42.77	D000	C
ATOM	7782	CD1	TRP	P	175	−5.235	−22.812	74.113	1.00	41.04	D000	C
ATOM	7783	CD2	TRP	P	175	−3.387	−22.650	72.846	1.00	48.23	D000	C
ATOM	7784	NE1	TRP	P	175	−5.594	−22.244	72.908	1.00	42.82	D000	N
ATOM	7785	CE2	TRP	P	175	−4.483	−22.130	72.115	1.00	46.08	D000	C
ATOM	7786	CE3	TRP	P	175	−2.117	−22.651	72.244	1.00	45.34	D000	C
ATOM	7787	CZ2	TRP	P	175	−4.348	−21.616	70.816	1.00	42.61	D000	C
ATOM	7788	CZ3	TRP	P	175	−1.988	−22.133	70.948	1.00	42.70	D000	C
ATOM	7789	CH2	TRP	P	175	−3.095	−21.626	70.256	1.00	41.85	D000	C
ATOM	7790	N	ALA	P	176	−0.677	−25.331	74.076	1.00	34.88	D000	N
ATOM	7791	CA	ALA	P	176	0.226	−25.561	72.957	1.00	30.60	D000	C
ATOM	7792	C	ALA	P	176	0.226	−27.022	72.528	1.00	36.67	D000	C
ATOM	7793	O	ALA	P	176	0.291	−27.325	71.328	1.00	33.09	D000	O
ATOM	7794	CB	ALA	P	176	1.632	−25.111	73.326	1.00	30.07	D000	C
ATOM	7795	N	ASP	P	177	0.176	−27.949	73.490	1.00	34.27	D000	N
ATOM	7796	CA	ASP	P	177	0.168	−29.353	73.103	1.00	30.80	D000	C
ATOM	7797	C	ASP	P	177	−1.161	−29.738	72.466	1.00	29.53	D000	C
ATOM	7798	O	ASP	P	177	−1.190	−30.546	71.540	1.00	28.69	D000	O
ATOM	7799	CB	ASP	P	177	0.466	−30.238	74.315	1.00	33.82	D000	C
ATOM	7800	CG	ASP	P	177	1.804	−29.908	74.967	1.00	40.40	D000	C
ATOM	7801	OD1	ASP	P	177	2.724	−29.448	74.243	1.00	40.31	D000	O
ATOM	7802	OD2	ASP	P	177	1.934	−30.111	76.206	1.00	43.49	D000	O1−
ATOM	7803	N	ALA	P	178	−2.267	−29.156	72.931	1.00	33.12	D000	N
ATOM	7804	CA	ALA	P	178	−3.558	−29.421	72.307	1.00	31.89	D000	C
ATOM	7805	C	ALA	P	178	−3.617	−28.832	70.899	1.00	35.82	D000	C
ATOM	7806	O	ALA	P	178	−4.104	−29.487	69.969	1.00	35.46	D000	O
ATOM	7807	CB	ALA	P	178	−4.690	−28.874	73.178	1.00	25.57	D000	C
ATOM	7808	N	ASP	P	179	−3.149	−27.588	70.741	1.00	33.89	D000	N
ATOM	7809	CA	ASP	P	179	−2.957	−26.971	69.429	1.00	35.32	D000	C
ATOM	7810	C	ASP	P	179	−2.204	−27.905	68.481	1.00	38.70	D000	C
ATOM	7811	O	ASP	P	179	−2.660	−28.182	67.365	1.00	37.15	D000	O
ATOM	7812	CB	ASP	P	179	−2.188	−25.656	69.607	1.00	36.39	D000	C
ATOM	7813	CG	ASP	P	179	−2.089	−24.840	68.331	1.00	45.78	D000	C
ATOM	7814	OD1	ASP	P	179	−2.995	−24.936	67.468	1.00	47.95	D000	O
ATOM	7815	OD2	ASP	P	179	−1.093	−24.096	68.191	1.00	50.66	D000	O1−
ATOM	7816	N	ASN	P	180	−1.049	−28.410	68.918	1.00	32.54	D000	N
ATOM	7817	CA	ASN	P	180	−0.271	−29.285	68.052	1.00	37.32	D000	C
ATOM	7818	C	ASN	P	180	−1.019	−30.582	67.794	1.00	38.98	D000	C
ATOM	7819	O	ASN	P	180	−0.911	−31.163	66.707	1.00	43.91	D000	O
ATOM	7820	CB	ASN	P	180	1.118	−29.563	68.660	1.00	33.88	D000	C
ATOM	7821	CG	ASN	P	180	2.023	−28.309	68.713	1.00	36.32	D000	C
ATOM	7822	OD1	ASN	P	180	1.696	−27.243	68.174	1.00	45.19	D000	O
ATOM	7823	ND2	ASN	P	180	3.160	−28.445	69.372	1.00	35.02	D000	N
ATOM	7824	N	TYR	P	181	−1.771	−31.060	68.782	1.00	39.97	D000	N
ATOM	7825	CA	TYR	P	181	−2.544	−32.280	68.589	1.00	39.12	D000	C
ATOM	7826	C	TYR	P	181	−3.578	−32.097	67.471	1.00	38.18	D000	C
ATOM	7827	O	TYR	P	181	−3.740	−32.963	66.601	1.00	35.54	D000	O
ATOM	7828	CB	TYR	P	181	−3.216	−32.680	69.908	1.00	26.15	D000	C
ATOM	7829	CG	TYR	P	181	−4.103	−33.884	69.760	1.00	30.23	D000	C
ATOM	7830	CD1	TYR	P	181	−5.415	−33.752	69.303	1.00	32.63	D000	C
ATOM	7831	CD2	TYR	P	181	−3.642	−35.158	70.052	1.00	31.11	D000	C
ATOM	7832	CE1	TYR	P	181	−6.223	−34.846	69.131	1.00	29.23	D000	C
ATOM	7833	CE2	TYR	P	181	−4.463	−36.267	69.898	1.00	26.83	D000	C
ATOM	7834	CZ	TYR	P	181	−5.750	−36.093	69.433	1.00	27.61	D000	C
ATOM	7835	OH	TYR	P	181	−6.587	−37.157	69.283	1.00	34.40	D000	O
ATOM	7836	N	CYS	P	182	−4.291	−30.973	67.476	1.00	34.18	D000	N
ATOM	7837	CA	CYS	P	182	−5.297	−30.784	66.443	1.00	40.39	D000	C
ATOM	7838	C	CYS	P	182	−4.643	−30.653	65.076	1.00	39.40	D000	C
ATOM	7839	O	CYS	P	182	−5.119	−31.245	64.098	1.00	36.09	D000	O
ATOM	7840	CB	CYS	P	182	−6.178	−29.570	66.756	1.00	38.38	D000	C
ATOM	7841	SG	CYS	P	182	−7.302	−29.774	68.185	1.00	41.03	D000	S
ATOM	7842	N	ARG	P	183	−3.541	−29.899	64.997	1.00	38.60	D000	N
ATOM	7843	CA	ARG	P	183	−2.855	−29.714	63.724	1.00	36.47	D000	C
ATOM	7844	C	ARG	P	183	−2.442	−31.048	63.106	1.00	35.85	D000	C
ATOM	7845	O	ARG	P	183	−2.647	−31.265	61.908	1.00	36.71	D000	O
ATOM	7846	CB	ARG	P	183	−1.648	−28.802	63.900	1.00	36.20	D000	C
ATOM	7847	CG	ARG	P	183	−1.953	−27.334	64.191	1.00	35.03	D000	C
ATOM	7848	CD	ARG	P	183	−0.707	−26.729	64.791	1.00	45.48	D000	C
ATOM	7849	NE	ARG	P	183	−0.297	−25.461	64.189	1.00	63.54	D000	N
ATOM	7850	CZ	ARG	P	183	0.971	−25.139	63.900	1.00	64.81	D000	C
ATOM	7851	NH1	ARG	P	183	1.957	−25.996	64.123	1.00	42.00	D000	N1+
ATOM	7852	NH2	ARG	P	183	1.259	−23.956	63.368	1.00	73.94	D000	N
ATOM	7853	N	LEU	P	184	−1.906	−31.972	63.906	1.00	34.56	D000	N
ATOM	7854	CA	LEU	P	184	−1.585	−33.295	63.377	1.00	34.47	D000	C
ATOM	7855	C	LEU	P	184	−2.812	−34.158	63.104	1.00	43.39	D000	C
ATOM	7856	O	LEU	P	184	−2.648	−35.287	62.629	1.00	48.31	D000	O
ATOM	7857	CB	LEU	P	184	−0.669	−34.073	64.311	1.00	40.32	D000	C
ATOM	7858	CG	LEU	P	184	0.849	−33.962	64.235	1.00	47.86	D000	C
ATOM	7859	CD1	LEU	P	184	1.306	−33.127	63.057	1.00	34.57	D000	C
ATOM	7860	CD2	LEU	P	184	1.398	−33.477	65.565	1.00	40.91	D000	C
ATOM	7861	N	GLU	P	185	−4.016	−33.714	63.463	1.00	43.99	D000	N
ATOM	7862	CA	GLU	P	185	−5.220	−34.401	63.011	1.00	42.68	D000	C
ATOM	7863	C	GLU	P	185	−5.746	−33.822	61.714	1.00	42.10	D000	C
ATOM	7864	O	GLU	P	185	−6.877	−34.117	61.325	1.00	41.36	D000	O
ATOM	7865	CB	GLU	P	185	−6.314	−34.365	64.076	1.00	40.55	D000	C
ATOM	7866	CG	GLU	P	185	−5.941	−35.182	65.257	1.00	41.11	D000	C
ATOM	7867	CD	GLU	P	185	−5.903	−36.635	64.898	1.00	46.25	D000	C
ATOM	7868	OE1	GLU	P	185	−6.722	−37.051	64.048	1.00	49.14	D000	O
ATOM	7869	OE2	GLU	P	185	−5.032	−37.350	65.434	1.00	47.23	D000	O1−
ATOM	7870	N	ASP	P	186	−4.940	−33.010	61.039	1.00	47.67	D000	N
ATOM	7871	CA	ASP	P	186	−5.390	−32.232	59.896	1.00	45.07	D000	C
ATOM	7872	C	ASP	P	186	−6.621	−31.416	60.279	1.00	43.94	D000	C
ATOM	7873	O	ASP	P	186	−7.601	−31.332	59.539	1.00	49.84	D000	O
ATOM	7874	CB	ASP	P	186	−5.656	−33.149	58.700	1.00	47.50	D000	C
ATOM	7875	CG	ASP	P	186	−5.429	−32.459	57.365	1.00	55.72	D000	C
ATOM	7876	OD1	ASP	P	186	−5.209	−31.227	57.346	1.00	54.34	D000	O
ATOM	7877	OD2	ASP	P	186	−5.476	−33.160	56.329	1.00	65.88	D000	O1−
ATOM	7878	N	ALA	P	187	−6.558	−30.797	61.453	1.00	43.57	D000	N
ATOM	7879	CA	ALA	P	187	−7.683	−30.054	62.009	1.00	40.06	D000	C
ATOM	7880	C	ALA	P	187	−7.136	−28.872	62.799	1.00	39.06	D000	C
ATOM	7881	O	ALA	P	187	−5.965	−28.502	62.673	1.00	41.54	D000	O
ATOM	7882	CB	ALA	P	187	−8.559	−30.971	62.871	1.00	37.26	D000	C
ATOM	7883	N	HIS	P	188	−7.984	−28.270	63.620	1.00	38.84	D000	N
ATOM	7884	CA	HIS	P	188	−7.523	−27.141	64.411	1.00	42.15	D000	C
ATOM	7885	C	HIS	P	188	−8.399	−26.992	65.655	1.00	44.84	D000	C
ATOM	7886	O	HIS	P	188	−9.536	−27.477	65.704	1.00	37.93	D000	O
ATOM	7887	CB	HIS	P	188	−7.528	−25.863	63.577	1.00	38.38	D000	C
ATOM	7888	CG	HIS	P	188	−8.885	−25.488	63.084	1.00	39.56	D000	C
ATOM	7889	ND1	HIS	P	188	−9.637	−24.489	63.663	1.00	42.56	D000	N
ATOM	7890	CD2	HIS	P	188	−9.644	−26.008	62.092	1.00	38.88	D000	C
ATOM	7891	CE1	HIS	P	188	−10.793	−24.394	63.034	1.00	45.45	D000	C
ATOM	7892	NE2	HIS	P	188	−10.822	−25.305	62.075	1.00	47.23	D000	N
ATOM	7893	N	LEU	P	189	−7.834	−26.338	66.673	1.00	39.67	D000	N
ATOM	7894	CA	LEU	P	189	−8.599	−26.011	67.860	1.00	36.17	D000	C
ATOM	7895	C	LEU	P	189	−9.829	−25.215	67.464	1.00	35.83	D000	C
ATOM	7896	O	LEU	P	189	−9.731	−24.279	66.669	1.00	34.94	D000	O
ATOM	7897	CB	LEU	P	189	−7.733	−25.219	68.832	1.00	37.51	D000	C
ATOM	7898	CG	LEU	P	189	−6.682	−25.973	69.637	1.00	36.68	D000	C
ATOM	7899	CD1	LEU	P	189	−5.830	−25.001	70.439	1.00	36.06	D000	C
ATOM	7900	CD2	LEU	P	189	−7.377	−26.952	70.569	1.00	34.22	D000	C
ATOM	7901	N	VAL	P	190	−10.979	−25.590	68.040	1.00	34.05	D000	N
ATOM	7902	CA	VAL	P	190	−12.274	−25.094	67.585	1.00	34.93	D000	C
ATOM	7903	C	VAL	P	190	−12.304	−23.565	67.518	1.00	35.33	D000	C
ATOM	7904	O	VAL	P	190	−11.823	−22.852	68.410	1.00	34.50	D000	O
ATOM	7905	CB	VAL	P	190	−13.400	−25.641	68.486	1.00	34.45	D000	C
ATOM	7906	CG1	VAL	P	190	−13.221	−25.185	69.924	1.00	32.88	D000	C
ATOM	7907	CG2	VAL	P	190	−14.740	−25.157	67.990	1.00	33.98	D000	C
ATOM	7908	N	VAL	P	191	−12.889	−23.066	66.438	1.00	34.01	D000	N
ATOM	7909	CA	VAL	P	191	−13.051	−21.643	66.182	1.00	35.07	D000	C
ATOM	7910	C	VAL	P	191	−14.544	−21.382	66.161	1.00	36.61	D000	C
ATOM	7911	O	VAL	P	191	−15.256	−21.923	65.306	1.00	41.56	D000	O
ATOM	7912	CB	VAL	P	191	−12.385	−21.225	64.856	1.00	35.46	D000	C
ATOM	7913	CG1	VAL	P	191	−12.817	−19.830	64.431	1.00	35.96	D000	C
ATOM	7914	CG2	VAL	P	191	−10.875	−21.295	64.981	1.00	36.37	D000	C
ATOM	7915	N	VAL	P	192	−15.021	−20.581	67.111	1.00	35.79	D000	N
ATOM	7916	CA	VAL	P	192	−16.450	−20.417	67.355	1.00	37.67	D000	C
ATOM	7917	C	VAL	P	192	−16.893	−19.094	66.754	1.00	37.75	D000	C
ATOM	7918	O	VAL	P	192	−16.442	−18.024	67.186	1.00	38.75	D000	O
ATOM	7919	CB	VAL	P	192	−16.776	−20.473	68.854	1.00	38.25	D000	C
ATOM	7920	CG1	VAL	P	192	−18.267	−20.314	69.053	1.00	35.90	D000	C
ATOM	7921	CG2	VAL	P	192	−16.282	−21.774	69.455	1.00	37.22	D000	C
ATOM	7922	N	THR	P	193	−17.795	−19.159	65.778	1.00	36.90	D000	N
ATOM	7923	CA	THR	P	193	−18.151	−17.982	64.995	1.00	42.26	D000	C
ATOM	7924	C	THR	P	193	−19.600	−17.530	65.148	1.00	41.06	D000	C
ATOM	7925	O	THR	P	193	−19.950	−16.480	64.605	1.00	46.91	D000	O
ATOM	7926	CB	THR	P	193	−17.813	−18.204	63.503	1.00	40.10	D000	C
ATOM	7927	OG1	THR	P	193	−18.471	−19.382	63.012	1.00	45.59	D000	O
ATOM	7928	CG2	THR	P	193	−16.302	−18.323	63.286	1.00	36.33	D000	C
ATOM	7929	N	SER	P	194	−20.440	−18.252	65.892	1.00	39.77	D000	N
ATOM	7930	CA	SER	P	194	−21.849	−17.898	66.016	1.00	36.24	D000	C
ATOM	7931	C	SER	P	194	−22.416	−18.395	67.342	1.00	40.36	D000	C
ATOM	7932	O	SER	P	194	−21.829	−19.244	68.013	1.00	39.43	D000	O
ATOM	7933	CB	SER	P	194	−22.666	−18.470	64.855	1.00	32.78	D000	C
ATOM	7934	OG	SER	P	194	−22.508	−19.875	64.777	1.00	40.86	D000	O
ATOM	7935	N	TRP	P	195	−23.589	−17.862	67.714	1.00	44.41	D000	N
ATOM	7936	CA	TRP	P	195	−24.275	−18.381	68.894	1.00	41.04	D000	C
ATOM	7937	C	TRP	P	195	−24.665	−19.830	68.684	1.00	37.41	D000	C
ATOM	7938	O	TRP	P	195	−24.633	−20.639	69.618	1.00	38.72	D000	O
ATOM	7939	CB	TRP	P	195	−25.519	−17.557	69.216	1.00	44.82	D000	C
ATOM	7940	CG	TRP	P	195	−25.243	−16.309	70.020	1.00	51.32	D000	C
ATOM	7941	CD1	TRP	P	195	−25.307	−15.008	69.586	1.00	46.03	D000	C
ATOM	7942	CD2	TRP	P	195	−24.854	−16.251	71.395	1.00	47.53	D000	C
ATOM	7943	NE1	TRP	P	195	−24.987	−14.148	70.610	1.00	47.20	D000	N
ATOM	7944	CE2	TRP	P	195	−24.706	−14.885	71.733	1.00	51.18	D000	C
ATOM	7945	CE3	TRP	P	195	−24.614	−17.221	72.375	1.00	46.44	D000	C
ATOM	7946	CZ2	TRP	P	195	−24.331	−14.464	73.016	1.00	55.85	D000	C
ATOM	7947	CZ3	TRP	P	195	−24.241	−16.801	73.654	1.00	53.40	D000	C
ATOM	7948	CH2	TRP	P	195	−24.105	−15.435	73.961	1.00	52.97	D000	C
ATOM	7949	N	GLU	P	196	−25.024	−20.181	67.458	1.00	34.05	D000	N
ATOM	7950	CA	GLU	P	196	−25.384	−21.557	67.174	1.00	36.55	D000	C
ATOM	7951	C	GLU	P	196	−24.200	−22.484	67.430	1.00	37.31	D000	C
ATOM	7952	O	GLU	P	196	−24.343	−23.528	68.078	1.00	36.90	D000	O
ATOM	7953	CB	GLU	P	196	−25.899	−21.650	65.740	1.00	37.33	D000	C
ATOM	7954	CG	GLU	P	196	−25.908	−23.036	65.156	1.00	54.30	D000	C
ATOM	7955	CD	GLU	P	196	−27.254	−23.709	65.306	1.00	67.53	D000	C
ATOM	7956	OE1	GLU	P	196	−28.111	−23.139	66.025	1.00	74.43	D000	O
ATOM	7957	OE2	GLU	P	196	−27.453	−24.799	64.704	1.00	66.20	D000	O1−
ATOM	7958	N	GLU	P	197	−23.008	−22.101	66.961	1.00	37.44	D000	N
ATOM	7959	CA	GLU	P	197	−21.837	−22.949	67.173	1.00	37.15	D000	C
ATOM	7960	C	GLU	P	197	−21.448	−23.002	68.652	1.00	36.59	D000	C
ATOM	7961	O	GLU	P	197	−21.077	−24.064	69.166	1.00	34.20	D000	O
ATOM	7962	CB	GLU	P	197	−20.674	−22.458	66.315	1.00	32.94	D000	C
ATOM	7963	CG	GLU	P	197	−19.417	−23.347	66.343	1.00	35.50	D000	C
ATOM	7964	CD	GLU	P	197	−18.383	−22.948	65.292	1.00	41.89	D000	C
ATOM	7965	OE1	GLU	P	197	−18.466	−21.807	64.772	1.00	45.12	D000	O
ATOM	7966	OE2	GLU	P	197	−17.486	−23.771	64.985	1.00	41.03	D000	O1−
ATOM	7967	N	GLN	P	198	−21.538	−21.865	69.345	1.00	32.12	D000	N
ATOM	7968	CA	GLN	P	198	−21.193	−21.792	70.759	1.00	31.52	D000	C
ATOM	7969	C	GLN	P	198	−22.083	−22.703	71.598	1.00	35.74	D000	C
ATOM	7970	O	GLN	P	198	−21.600	−23.403	72.501	1.00	30.28	D000	O
ATOM	7971	CB	GLN	P	198	−21.298	−20.334	71.226	1.00	33.50	D000	C
ATOM	7972	CG	GLN	P	198	−21.391	−20.126	72.734	1.00	33.84	D000	C
ATOM	7973	CD	GLN	P	198	−20.055	−20.173	73.450	1.00	33.31	D000	C
ATOM	7974	OE1	GLN	P	198	−19.009	−19.859	72.878	1.00	30.27	D000	O
ATOM	7975	NE2	GLN	P	198	−20.085	−20.563	74.713	1.00	33.30	D000	N
ATOM	7976	N	LYS	P	199	−23.393	−22.694	71.320	1.00	35.11	D000	N
ATOM	7977	CA	LYS	P	199	−24.328	−23.523	72.070	1.00	32.09	D000	C
ATOM	7978	C	LYS	P	199	−24.070	−25.009	71.828	1.00	32.10	D000	C
ATOM	7979	O	LYS	P	199	−24.103	−25.811	72.767	1.00	31.39	D000	O
ATOM	7980	CB	LYS	P	199	−25.753	−23.142	71.692	1.00	31.90	D000	C
ATOM	7981	CG	LYS	P	199	−26.283	−21.993	72.497	1.00	34.02	D000	C
ATOM	7982	CD	LYS	P	199	−27.260	−21.182	71.709	1.00	36.65	D000	C
ATOM	7983	CE	LYS	P	199	−28.314	−22.071	71.096	1.00	40.59	D000	C
ATOM	7984	NZ	LYS	P	199	−29.444	−21.249	70.594	1.00	48.36	D000	N1+
ATOM	7985	N	PHE	P	200	−23.806	−25.392	70.581	1.00	28.05	D000	N
ATOM	7986	CA	PHE	P	200	−23.515	−26.788	70.283	1.00	28.75	D000	C
ATOM	7987	C	PHE	P	200	−22.286	−27.284	71.036	1.00	32.43	D000	C
ATOM	7988	O	PHE	P	200	−22.287	−28.399	71.568	1.00	30.79	D000	O
ATOM	7989	CB	PHE	P	200	−23.318	−26.956	68.787	1.00	27.58	D000	C
ATOM	7990	CG	PHE	P	200	−22.644	−28.222	68.417	1.00	29.26	D000	C
ATOM	7991	CD1	PHE	P	200	−23.363	−29.387	68.303	1.00	28.09	D000	C
ATOM	7992	CD2	PHE	P	200	−21.279	−28.247	68.172	1.00	31.84	D000	C
ATOM	7993	CE1	PHE	P	200	−22.747	−30.561	67.943	1.00	30.20	D000	C
ATOM	7994	CE2	PHE	P	200	−20.647	−29.415	67.799	1.00	31.13	D000	C
ATOM	7995	CZ	PHE	P	200	−21.385	−30.577	67.682	1.00	33.34	D000	C
ATOM	7996	N	VAL	P	201	−21.220	−26.478	71.083	1.00	30.80	D000	N
ATOM	7997	CA	VAL	P	201	−20.015	−26.900	71.787	1.00	31.26	D000	C
ATOM	7998	C	VAL	P	201	−20.277	−26.989	73.295	1.00	31.79	D000	C
ATOM	7999	O	VAL	P	201	−19.849	−27.947	73.948	1.00	29.59	D000	O
ATOM	8000	CB	VAL	P	201	−18.836	−25.959	71.458	1.00	30.91	D000	C
ATOM	8001	CG1	VAL	P	201	−17.611	−26.260	72.345	1.00	32.04	D000	C
ATOM	8002	CG2	VAL	P	201	−18.433	−26.104	70.020	1.00	33.28	D000	C
ATOM	8003	N	GLN	P	202	−21.001	−26.012	73.862	1.00	30.50	D000	N
ATOM	8004	CA	GLN	P	202	−21.323	−26.044	75.290	1.00	30.37	D000	C
ATOM	8005	C	GLN	P	202	−22.040	−27.327	75.670	1.00	25.89	D000	C
ATOM	8006	O	GLN	P	202	−21.755	−27.903	76.719	1.00	33.97	D000	O
ATOM	8007	CB	GLN	P	202	−22.203	−24.865	75.701	1.00	35.09	D000	C
ATOM	8008	CG	GLN	P	202	−21.566	−23.520	75.783	1.00	35.69	D000	C
ATOM	8009	CD	GLN	P	202	−22.490	−22.528	76.480	1.00	47.70	D000	C
ATOM	8010	OE1	GLN	P	202	−22.615	−21.351	76.078	1.00	41.49	D000	O
ATOM	8011	NE2	GLN	P	202	−23.110	−22.990	77.575	1.00	49.12	D000	N
ATOM	8012	N	HIS	P	203	−23.025	−27.742	74.871	1.00	25.10	D000	N
ATOM	8013	CA	HIS	P	203	−23.731	−29.000	75.117	1.00	27.41	D000	C
ATOM	8014	C	HIS	P	203	−22.780	−30.154	75.316	1.00	32.74	D000	C
ATOM	8015	O	HIS	P	203	−22.919	−30.940	76.262	1.00	37.16	D000	O
ATOM	8016	CB	HIS	P	203	−24.638	−29.354	73.947	1.00	31.40	D000	C
ATOM	8017	CG	HIS	P	203	−26.051	−28.936	74.117	1.00	37.58	D000	C
ATOM	8018	ND1	HIS	P	203	−26.725	−28.198	73.167	1.00	46.93	D000	N
ATOM	8019	CD2	HIS	P	203	−26.942	−29.204	75.098	1.00	43.64	D000	C
ATOM	8020	CE1	HIS	P	203	−27.963	−27.992	73.576	1.00	52.72	D000	C
ATOM	8021	NE2	HIS	P	203	−28.122	−28.598	74.742	1.00	57.54	D000	N
ATOM	8022	N	HIS	P	204	−21.809	−30.280	74.406	1.00	33.87	D000	N
ATOM	8023	CA	HIS	P	204	−20.952	−31.453	74.375	1.00	32.62	D000	C
ATOM	8024	C	HIS	P	204	−19.857	−31.394	75.428	1.00	30.65	D000	C
ATOM	8025	O	HIS	P	204	−19.399	−32.445	75.880	1.00	27.67	D000	O
ATOM	8026	CB	HIS	P	204	−20.373	−31.635	72.969	1.00	25.37	D000	C
ATOM	8027	CG	HIS	P	204	−21.341	−32.234	71.995	1.00	29.38	D000	C
ATOM	8028	ND1	HIS	P	204	−21.525	−33.593	71.869	1.00	30.92	D000	N
ATOM	8029	CD2	HIS	P	204	−22.217	−31.661	71.137	1.00	32.57	D000	C
ATOM	8030	CE1	HIS	P	204	−22.445	−33.835	70.953	1.00	28.23	D000	C
ATOM	8031	NE2	HIS	P	204	−22.883	−32.678	70.494	1.00	34.46	D000	N
ATOM	8032	N	ILE	P	205	−19.424	−30.197	75.830	1.00	28.24	D000	N
ATOM	8033	CA	ILE	P	205	−18.324	−30.104	76.778	1.00	27.46	D000	C
ATOM	8034	C	ILE	P	205	−18.778	−30.056	78.220	1.00	33.06	D000	C
ATOM	8035	O	ILE	P	205	−17.952	−30.295	79.111	1.00	35.59	D000	O
ATOM	8036	CB	ILE	P	205	−17.392	−28.907	76.513	1.00	33.12	D000	C
ATOM	8037	CG1	ILE	P	205	−18.123	−27.564	76.648	1.00	26.96	D000	C
ATOM	8038	CG2	ILE	P	205	−16.702	−29.080	75.173	1.00	25.98	D000	C
ATOM	8039	CD1	ILE	P	205	−17.174	−26.412	76.624	1.00	23.08	D000	C
ATOM	8040	N	GLY	P	206	−20.043	−29.713	78.482	1.00	35.40	D000	N
ATOM	8041	CA	GLY	P	206	−20.536	−29.649	79.837	1.00	29.75	D000	C
ATOM	8042	C	GLY	P	206	−19.906	−28.523	80.620	1.00	32.65	D000	C
ATOM	8043	O	GLY	P	206	−19.313	−27.601	80.053	1.00	35.11	D000	O
ATOM	8044	N	PRO	P	207	−20.032	−28.568	81.948	1.00	33.48	D000	N
ATOM	8045	CA	PRO	P	207	−19.544	−27.464	82.797	1.00	31.43	D000	C
ATOM	8046	C	PRO	P	207	−18.059	−27.610	83.123	1.00	36.17	D000	C
ATOM	8047	O	PRO	P	207	−17.637	−27.650	84.288	1.00	38.20	D000	O
ATOM	8048	CB	PRO	P	207	−20.443	−27.590	84.032	1.00	35.30	D000	C
ATOM	8049	CG	PRO	P	207	−20.723	−29.073	84.132	1.00	31.37	D000	C
ATOM	8050	CD	PRO	P	207	−20.694	−29.628	82.727	1.00	30.51	D000	C
ATOM	8051	N	VAL	P	208	−17.242	−27.622	82.071	1.00	35.28	D000	N
ATOM	8052	CA	VAL	P	208	−15.854	−28.057	82.127	1.00	31.19	D000	C
ATOM	8053	C	VAL	P	208	−14.990	−27.043	81.389	1.00	32.34	D000	C
ATOM	8054	O	VAL	P	208	−15.252	−26.754	80.217	1.00	30.13	D000	O
ATOM	8055	CB	VAL	P	208	−15.733	−29.454	81.493	1.00	24.39	D000	C
ATOM	8056	CG1	VAL	P	208	−14.304	−29.927	81.433	1.00	19.72	D000	C
ATOM	8057	CG2	VAL	P	208	−16.623	−30.417	82.259	1.00	26.85	D000	C
ATOM	8058	N	ASN	P	209	−13.955	−26.514	82.065	1.00	33.01	D000	N
ATOM	8059	CA	ASN	P	209	−12.987	−25.628	81.404	1.00	28.33	D000	C
ATOM	8060	C	ASN	P	209	−12.325	−26.339	80.224	1.00	28.70	D000	C
ATOM	8061	O	ASN	P	209	−11.666	−27.369	80.409	1.00	26.30	D000	O
ATOM	8062	CB	ASN	P	209	−11.911	−25.165	82.388	1.00	26.60	D000	C
ATOM	8063	CG	ASN	P	209	−12.401	−24.116	83.370	1.00	27.81	D000	C
ATOM	8064	OD1	ASN	P	209	−13.324	−23.343	83.094	1.00	31.03	D000	O
ATOM	8065	ND2	ASN	P	209	−11.774	−24.083	84.528	1.00	22.70	D000	N
ATOM	8066	N	THR	P	210	−12.487	−25.786	79.017	1.00	27.48	D000	N
ATOM	8067	CA	THR	P	210	−12.049	−26.451	77.790	1.00	27.53	D000	C
ATOM	8068	C	THR	P	210	−11.385	−25.441	76.860	1.00	29.97	D000	C
ATOM	8069	O	THR	P	210	−11.918	−24.350	76.656	1.00	28.86	D000	O
ATOM	8070	CB	THR	P	210	−13.223	−27.156	77.082	1.00	28.24	D000	C
ATOM	8071	OG1	THR	P	210	−13.710	−28.226	77.908	1.00	30.12	D000	O
ATOM	8072	CG2	THR	P	210	−12.801	−27.746	75.755	1.00	23.19	D000	C
ATOM	8073	N	TRP	P	211	−10.219	−25.797	76.313	1.00	29.85	D000	N
ATOM	8074	CA	TRP	P	211	−9.514	−24.902	75.399	1.00	31.37	D000	C
ATOM	8075	C	TRP	P	211	−10.280	−24.746	74.099	1.00	34.18	D000	C
ATOM	8076	O	TRP	P	211	−10.884	−25.707	73.604	1.00	32.26	D000	O
ATOM	8077	CB	TRP	P	211	−8.122	−25.430	75.046	1.00	26.53	D000	C
ATOM	8078	CG	TRP	P	211	−7.115	−25.421	76.131	1.00	30.84	D000	C
ATOM	8079	CD1	TRP	P	211	−6.341	−26.470	76.523	1.00	29.48	D000	C
ATOM	8080	CD2	TRP	P	211	−6.740	−24.312	76.959	1.00	29.42	D000	C
ATOM	8081	NE1	TRP	P	211	−5.507	−26.084	77.538	1.00	29.42	D000	N
ATOM	8082	CE2	TRP	P	211	−5.740	−24.768	77.832	1.00	29.17	D000	C
ATOM	8083	CE3	TRP	P	211	−7.150	−22.979	77.041	1.00	31.34	D000	C
ATOM	8084	CZ2	TRP	P	211	−5.145	−23.942	78.778	1.00	31.63	D000	C
ATOM	8085	CZ3	TRP	P	211	−6.563	−22.163	77.977	1.00	28.33	D000	C
ATOM	8086	CH2	TRP	P	211	−5.568	−22.642	78.830	1.00	30.22	D000	C
ATOM	8087	N	MET	P	212	−10.227	−23.530	73.540	1.00	33.06	D000	N
ATOM	8088	CA	MET	P	212	−10.647	−23.222	72.175	1.00	33.50	D000	C
ATOM	8089	C	MET	P	212	−9.461	−22.623	71.415	1.00	35.69	D000	C
ATOM	8090	O	MET	P	212	−8.401	−22.362	71.985	1.00	33.28	D000	O
ATOM	8091	CB	MET	P	212	−11.841	−22.265	72.153	1.00	27.35	D000	C
ATOM	8092	CG	MET	P	212	−11.442	−20.835	72.335	1.00	34.07	D000	C
ATOM	8093	SD	MET	P	212	−12.807	−19.717	72.680	1.00	33.50	D000	S
ATOM	8094	CE	MET	P	212	−13.264	−20.227	74.323	1.00	34.96	D000	C
ATOM	8095	N	GLY	P	213	−9.615	−22.465	70.099	1.00	38.96	D000	N
ATOM	8096	CA	GLY	P	213	−8.538	−21.941	69.266	1.00	36.71	D000	C
ATOM	8097	C	GLY	P	213	−8.297	−20.437	69.293	1.00	36.61	D000	C
ATOM	8098	O	GLY	P	213	−8.265	−19.807	68.237	1.00	34.15	D000	O
ATOM	8099	N	LEU	P	214	−8.113	−19.847	70.472	1.00	37.22	D000	N
ATOM	8100	CA	LEU	P	214	−7.994	−18.399	70.609	1.00	40.19	D000	C
ATOM	8101	C	LEU	P	214	−6.897	−18.065	71.618	1.00	44.61	D000	C
ATOM	8102	O	LEU	P	214	−6.928	−18.534	72.761	1.00	42.53	D000	O
ATOM	8103	CB	LEU	P	214	−9.340	−17.783	71.019	1.00	36.46	D000	C
ATOM	8104	CG	LEU	P	214	−9.420	−16.273	71.253	1.00	39.49	D000	C
ATOM	8105	CD1	LEU	P	214	−9.308	−15.528	69.943	1.00	39.79	D000	C
ATOM	8106	CD2	LEU	P	214	−10.692	−15.890	71.983	1.00	37.37	D000	C
ATOM	8107	N	HIS	P	215	−5.914	−17.274	71.191	1.00	47.99	D000	N
ATOM	8108	CA	HIS	P	215	−4.787	−16.902	72.042	1.00	53.52	D000	C
ATOM	8109	C	HIS	P	215	−4.270	−15.525	71.632	1.00	50.41	D000	C
ATOM	8110	O	HIS	P	215	−4.496	−15.076	70.506	1.00	50.05	D000	O
ATOM	8111	CB	HIS	P	215	−3.668	−17.963	71.988	1.00	48.40	D000	C
ATOM	8112	CG	HIS	P	215	−3.026	−18.112	70.645	1.00	51.27	D000	C
ATOM	8113	ND1	HIS	P	215	−1.709	−18.488	70.490	1.00	52.99	D000	N
ATOM	8114	CD2	HIS	P	215	−3.517	−17.937	69.394	1.00	48.48	D000	C
ATOM	8115	CE1	HIS	P	215	−1.417	−18.539	69.203	1.00	55.12	D000	C
ATOM	8116	NE2	HIS	P	215	−2.496	−18.205	68.517	1.00	52.31	D000	N
ATOM	8117	N	ASP	P	216	−3.639	−14.826	72.579	1.00	50.32	D000	N
ATOM	8118	CA	ASP	P	216	−2.999	−13.547	72.283	1.00	62.90	D000	C
ATOM	8119	C	ASP	P	216	−1.529	−13.584	72.680	1.00	66.62	D000	C
ATOM	8120	O	ASP	P	216	−0.957	−12.579	73.111	1.00	70.47	D000	O
ATOM	8121	CB	ASP	P	216	−3.730	−12.376	72.949	1.00	58.20	D000	C
ATOM	8122	CG	ASP	P	216	−3.387	−12.201	74.428	1.00	62.56	D000	C
ATOM	8123	OD1	ASP	P	216	−2.915	−13.156	75.088	1.00	67.95	D000	O
ATOM	8124	OD2	ASP	P	216	−3.613	−11.088	74.942	1.00	66.89	D000	O1−
ATOM	8125	N	GLN	P	217	−0.907	−14.751	72.520	1.00	64.97	D000	N
ATOM	8126	CA	GLN	P	217	0.521	−14.866	72.771	1.00	76.33	D000	C
ATOM	8127	C	GLN	P	217	1.312	−13.867	71.944	1.00	79.09	D000	C
ATOM	8128	O	GLN	P	217	2.439	−13.521	72.314	1.00	84.36	D000	O
ATOM	8129	CB	GLN	P	217	0.981	−16.309	72.509	1.00	76.19	D000	C
ATOM	8130	CG	GLN	P	217	0.950	−17.206	73.776	1.00	69.70	D000	C
ATOM	8131	CD	GLN	P	217	0.539	−18.645	73.498	1.00	61.34	D000	C
ATOM	8132	OE1	GLN	P	217	−0.353	−18.897	72.690	1.00	62.21	D000	O
ATOM	8133	NE2	GLN	P	217	1.177	−19.597	74.185	1.00	61.50	D000	N
ATOM	8134	N	ASN	P	218	0.722	−13.361	70.863	1.00	80.19	D000	N
ATOM	8135	CA	ASN	P	218	1.363	−12.319	70.073	1.00	87.85	D000	C
ATOM	8136	C	ASN	P	218	1.275	−10.964	70.775	1.00	79.48	D000	C
ATOM	8137	O	ASN	P	218	2.294	−10.367	71.140	1.00	80.45	D000	O
ATOM	8138	CB	ASN	P	218	0.705	−12.268	68.689	1.00	84.56	D000	C
ATOM	8139	CG	ASN	P	218	1.684	−11.916	67.594	1.00	89.88	D000	C
ATOM	8140	OD1	ASN	P	218	1.373	−12.042	66.404	1.00	90.71	D000	O
ATOM	8141	ND2	ASN	P	218	2.891	−11.507	67.986	1.00	84.53	D000	N
ATOM	8142	N	GLY	P	219	0.059	−10.514	71.040	1.00	74.18	D000	N
ATOM	8143	CA	GLY	P	219	−0.212	−9.187	71.530	1.00	68.61	D000	C
ATOM	8144	C	GLY	P	219	−1.710	−8.949	71.462	1.00	73.97	D000	C
ATOM	8145	O	GLY	P	219	−2.366	−8.740	72.489	1.00	71.33	D000	O
ATOM	8146	N	PRO	P	220	−2.285	−9.017	70.255	1.00	69.70	D000	N
ATOM	8147	CA	PRO	P	220	−3.745	−9.029	70.112	1.00	69.83	D000	C
ATOM	8148	C	PRO	P	220	−4.304	−10.446	70.009	1.00	67.70	D000	C
ATOM	8149	O	PRO	P	220	−3.608	−11.402	69.652	1.00	66.31	D000	O
ATOM	8150	CB	PRO	P	220	−3.967	−8.274	68.792	1.00	64.94	D000	C
ATOM	8151	CG	PRO	P	220	−2.674	−8.444	68.009	1.00	60.23	D000	C
ATOM	8152	CD	PRO	P	220	−1.625	−9.035	68.933	1.00	70.78	D000	C
ATOM	8153	N	TRP	P	221	−5.595	−10.568	70.309	1.00	58.78	D000	N
ATOM	8154	CA	TRP	P	221	−6.244	−11.868	70.228	1.00	52.55	D000	C
ATOM	8155	C	TRP	P	221	−6.415	−12.290	68.778	1.00	51.19	D000	C
ATOM	8156	O	TRP	P	221	−6.795	−11.486	67.920	1.00	53.28	D000	O
ATOM	8157	CB	TRP	P	221	−7.601	−11.831	70.940	1.00	52.62	D000	C
ATOM	8158	CG	TRP	P	221	−7.438	−11.729	72.425	1.00	50.70	D000	C
ATOM	8159	CD1	TRP	P	221	−7.477	−10.597	73.179	1.00	52.92	D000	C
ATOM	8160	CD2	TRP	P	221	−7.164	−12.807	73.332	1.00	48.63	D000	C
ATOM	8161	NE1	TRP	P	221	−7.256	−10.901	74.505	1.00	54.57	D000	N
ATOM	8162	CE2	TRP	P	221	−7.058	−12.251	74.624	1.00	49.93	D000	C
ATOM	8163	CE3	TRP	P	221	−7.001	−14.189	73.177	1.00	46.93	D000	C
ATOM	8164	CZ2	TRP	P	221	−6.796	−13.029	75.757	1.00	50.65	D000	C
ATOM	8165	CZ3	TRP	P	221	−6.739	−14.960	74.303	1.00	46.92	D000	C
ATOM	8166	CH2	TRP	P	221	−6.643	−14.377	75.575	1.00	48.14	D000	C
ATOM	8167	N	LYS	P	222	−6.132	−13.568	68.513	1.00	50.38	D000	N
ATOM	8168	CA	LYS	P	222	−6.213	−14.155	67.178	1.00	52.36	D000	C
ATOM	8169	C	LYS	P	222	−6.785	−15.564	67.274	1.00	48.11	D000	C
ATOM	8170	O	LYS	P	222	−6.551	−16.277	68.253	1.00	43.41	D000	O
ATOM	8171	CB	LYS	P	222	−4.842	−14.247	66.473	1.00	48.15	D000	C
ATOM	8172	CG	LYS	P	222	−3.989	−13.006	66.480	1.00	49.51	D000	C
ATOM	8173	CD	LYS	P	222	−2.623	−13.343	65.879	1.00	63.49	D000	C
ATOM	8174	CE	LYS	P	222	−1.744	−12.107	65.682	1.00	74.29	D000	C
ATOM	8175	NZ	LYS	P	222	−0.559	−12.385	64.812	1.00	71.05	D000	N1+
ATOM	8176	N	TRP	P	223	−7.518	−15.967	66.239	1.00	46.69	D000	N
ATOM	8177	CA	TRP	P	223	−7.966	−17.345	66.081	1.00	40.92	D000	C
ATOM	8178	C	TRP	P	223	−6.901	−18.155	65.334	1.00	42.46	D000	C
ATOM	8179	O	TRP	P	223	−6.100	−17.605	64.578	1.00	42.65	D000	O
ATOM	8180	CB	TRP	P	223	−9.314	−17.398	65.346	1.00	38.25	D000	C
ATOM	8181	CG	TRP	P	223	−10.464	−16.803	66.160	1.00	46.60	D000	C
ATOM	8182	CD1	TRP	P	223	−10.918	−15.508	66.115	1.00	44.78	D000	C
ATOM	8183	CD2	TRP	P	223	−11.284	−17.476	67.141	1.00	41.63	D000	C
ATOM	8184	NE1	TRP	P	223	−11.954	−15.337	67.003	1.00	45.05	D000	N
ATOM	8185	CE2	TRP	P	223	−12.203	−16.526	67.641	1.00	43.02	D000	C
ATOM	8186	CE3	TRP	P	223	−11.328	−18.786	67.644	1.00	40.53	D000	C
ATOM	8187	CZ2	TRP	P	223	−13.152	−16.843	68.628	1.00	38.24	D000	C
ATOM	8188	CZ3	TRP	P	223	−12.271	−19.097	68.619	1.00	38.15	D000	C
ATOM	8189	CH2	TRP	P	223	−13.165	−18.125	69.103	1.00	37.47	D000	C
ATOM	8190	N	VAL	P	224	−6.863	−19.466	65.601	1.00	41.18	D000	N
ATOM	8191	CA	VAL	P	224	−5.813	−20.316	65.049	1.00	40.27	D000	C
ATOM	8192	C	VAL	P	224	−5.952	−20.568	63.553	1.00	43.70	D000	C
ATOM	8193	O	VAL	P	224	−4.977	−20.993	62.918	1.00	45.37	D000	O
ATOM	8194	CB	VAL	P	224	−5.738	−21.679	65.760	1.00	35.45	D000	C
ATOM	8195	CG1	VAL	P	224	−5.402	−21.490	67.200	1.00	39.13	D000	C
ATOM	8196	CG2	VAL	P	224	−7.025	−22.441	65.581	1.00	35.78	D000	C
ATOM	8197	N	ASP	P	225	−7.132	−20.379	62.966	1.00	45.80	D000	N
ATOM	8198	CA	ASP	P	225	−7.297	−20.628	61.535	1.00	47.35	D000	C
ATOM	8199	C	ASP	P	225	−7.260	−19.343	60.721	1.00	44.18	D000	C
ATOM	8200	O	ASP	P	225	−7.418	−19.380	59.496	1.00	41.75	D000	O
ATOM	8201	CB	ASP	P	225	−8.590	−21.431	61.261	1.00	42.90	D000	C
ATOM	8202	CG	ASP	P	225	−9.864	−20.593	61.367	1.00	45.62	D000	C
ATOM	8203	OD1	ASP	P	225	−9.832	−19.473	61.933	1.00	42.32	D000	O
ATOM	8204	OD2	ASP	P	225	−10.912	−21.079	60.878	1.00	49.08	D000	O1−
ATOM	8205	N	GLY	P	226	−7.023	−18.215	61.373	1.00	42.84	D000	N
ATOM	8206	CA	GLY	P	226	−6.919	−16.957	60.693	1.00	37.63	D000	C
ATOM	8207	C	GLY	P	226	−8.168	−16.131	60.725	1.00	40.53	D000	C
ATOM	8208	O	GLY	P	226	−8.089	−14.938	60.408	1.00	43.36	D000	O
ATOM	8209	N	THR	P	227	−9.315	−16.725	61.089	1.00	42.48	D000	N
ATOM	8210	CA	THR	P	227	−10.562	−15.973	61.156	1.00	39.26	D000	C
ATOM	8211	C	THR	P	227	−10.348	−14.706	61.974	1.00	43.02	D000	C
ATOM	8212	O	THR	P	227	−9.666	−14.722	63.005	1.00	41.15	D000	O
ATOM	8213	CB	THR	P	227	−11.684	−16.819	61.760	1.00	38.82	D000	C
ATOM	8214	OG1	THR	P	227	−11.803	−18.060	61.044	1.00	45.33	D000	O
ATOM	8215	CG2	THR	P	227	−13.015	−16.065	61.694	1.00	30.94	D000	C
ATOM	8216	N	ASP	P	228	−10.899	−13.600	61.485	1.00	35.97	D000	N
ATOM	8217	CA	ASP	P	228	−10.647	−12.323	62.128	1.00	43.82	D000	C
ATOM	8218	C	ASP	P	228	−11.342	−12.271	63.487	1.00	45.21	D000	C
ATOM	8219	O	ASP	P	228	−12.534	−12.577	63.606	1.00	44.16	D000	O
ATOM	8220	CB	ASP	P	228	−11.127	−11.167	61.243	1.00	38.78	D000	C
ATOM	8221	CG	ASP	P	228	−10.940	−9.817	61.909	1.00	49.28	D000	C
ATOM	8222	OD1	ASP	P	228	−9.775	−9.419	62.162	1.00	54.97	D000	O
ATOM	8223	OD2	ASP	P	228	−11.958	−9.175	62.242	1.00	50.80	D000	O1−
ATOM	8224	N	TYR	P	229	−10.601	−11.828	64.501	1.00	48.02	D000	N
ATOM	8225	CA	TYR	P	229	−11.132	−11.730	65.857	1.00	49.96	D000	C
ATOM	8226	C	TYR	P	229	−11.979	−10.481	66.041	1.00	49.04	D000	C
ATOM	8227	O	TYR	P	229	−13.064	−10.540	66.628	1.00	53.87	D000	O
ATOM	8228	CB	TYR	P	229	−9.995	−11.743	66.883	1.00	44.05	D000	C
ATOM	8229	CG	TYR	P	229	−10.439	−11.358	68.269	1.00	45.49	D000	C
ATOM	8230	CD2	TYR	P	229	−10.286	−10.061	68.725	1.00	53.43	D000	C
ATOM	8231	CD1	TYR	P	229	−10.994	−12.296	69.132	1.00	44.65	D000	C
ATOM	8232	CE2	TYR	P	229	−10.684	−9.695	69.997	1.00	56.58	D000	C
ATOM	8233	CE1	TYR	P	229	−11.403	−11.944	70.406	1.00	46.74	D000	C
ATOM	8234	CZ	TYR	P	229	−11.243	−10.638	70.838	1.00	52.93	D000	C
ATOM	8235	OH	TYR	P	229	−11.634	−10.250	72.104	1.00	43.44	D000	O
ATOM	8236	N	GLU	P	230	−11.503	−9.341	65.555	1.00	51.91	D000	N
ATOM	8237	CA	GLU	P	230	−12.119	−8.087	65.968	1.00	56.16	D000	C
ATOM	8238	C	GLU	P	230	−13.560	−7.995	65.476	1.00	54.64	D000	C
ATOM	8239	O	GLU	P	230	−14.468	−7.629	66.236	1.00	52.29	D000	O
ATOM	8240	CB	GLU	P	230	−11.292	−6.908	65.456	1.00	50.78	D000	C
ATOM	8241	CG	GLU	P	230	−11.547	−5.640	66.240	1.00	59.32	D000	C
ATOM	8242	CD	GLU	P	230	−11.610	−5.897	67.751	1.00	65.21	D000	C
ATOM	8243	OE1	GLU	P	230	−10.556	−6.220	68.353	1.00	63.19	D000	O
ATOM	8244	OE2	GLU	P	230	−12.718	−5.790	68.330	1.00	66.54	D000	O1−
ATOM	8245	N	THR	P	231	−13.797	−8.382	64.231	1.00	49.30	D000	N
ATOM	8246	CA	THR	P	231	−15.125	−8.335	63.651	1.00	49.06	D000	C
ATOM	8247	C	THR	P	231	−15.943	−9.595	63.913	1.00	48.66	D000	C
ATOM	8248	O	THR	P	231	−17.084	−9.685	63.450	1.00	46.72	D000	O
ATOM	8249	CB	THR	P	231	−14.999	−8.096	62.145	1.00	51.91	D000	C
ATOM	8250	OG1	THR	P	231	−14.418	−9.247	61.519	1.00	49.55	D000	O
ATOM	8251	CG2	THR	P	231	−14.092	−6.893	61.895	1.00	44.25	D000	C
ATOM	8252	N	GLY	P	232	−15.374	−10.596	64.593	1.00	53.28	D000	N
ATOM	8253	CA	GLY	P	232	−16.057	−11.861	64.770	1.00	51.71	D000	C
ATOM	8254	C	GLY	P	232	−16.832	−11.982	66.082	1.00	49.39	D000	C
ATOM	8255	O	GLY	P	232	−16.750	−11.136	66.974	1.00	45.77	D000	O
ATOM	8256	N	PHE	P	233	−17.569	−13.087	66.178	1.00	46.98	D000	N
ATOM	8257	CA	PHE	P	233	−18.353	−13.412	67.362	1.00	45.41	D000	C
ATOM	8258	C	PHE	P	233	−17.477	−13.478	68.610	1.00	43.09	D000	C
ATOM	8259	O	PHE	P	233	−16.350	−13.978	68.572	1.00	40.14	D000	O
ATOM	8260	CB	PHE	P	233	−19.050	−14.755	67.133	1.00	43.80	D000	C
ATOM	8261	CG	PHE	P	233	−19.795	−15.261	68.318	1.00	41.20	D000	C
ATOM	8262	CD1	PHE	P	233	−21.056	−14.778	68.620	1.00	42.87	D000	C
ATOM	8263	CD2	PHE	P	233	−19.235	−16.234	69.130	1.00	41.22	D000	C
ATOM	8264	CE1	PHE	P	233	−21.746	−15.250	69.718	1.00	43.07	D000	C
ATOM	8265	CE2	PHE	P	233	−19.917	−16.712	70.232	1.00	42.28	D000	C
ATOM	8266	CZ	PHE	P	233	−21.179	−16.221	70.526	1.00	42.72	D000	C
ATOM	8267	N	LYS	P	234	−18.005	−12.976	69.728	1.00	42.82	D000	N
ATOM	8268	CA	LYS	P	234	−17.292	−12.988	71.000	1.00	37.90	D000	C
ATOM	8269	C	LYS	P	234	−18.268	−13.294	72.133	1.00	41.60	D000	C
ATOM	8270	O	LYS	P	234	−19.440	−12.901	72.093	1.00	44.48	D000	O
ATOM	8271	CB	LYS	P	234	−16.596	−11.656	71.279	1.00	35.56	D000	C
ATOM	8272	CG	LYS	P	234	−15.570	−11.240	70.265	1.00	40.67	D000	C
ATOM	8273	CD	LYS	P	234	−14.974	−9.900	70.655	1.00	45.48	D000	C
ATOM	8274	CE	LYS	P	234	−14.396	−9.152	69.453	1.00	51.18	D000	C
ATOM	8275	NZ	LYS	P	234	−15.432	−8.815	68.436	1.00	50.83	D000	N1+
ATOM	8276	N	ASN	P	235	−17.770	−13.978	73.161	1.00	41.60	D000	N
ATOM	8277	CA	ASN	P	235	−18.619	−14.402	74.273	1.00	37.71	D000	C
ATOM	8278	C	ASN	P	235	−17.822	−14.433	75.583	1.00	37.90	D000	C
ATOM	8279	O	ASN	P	235	−17.903	−15.379	76.370	1.00	37.72	D000	O
ATOM	8280	CB	ASN	P	235	−19.249	−15.757	73.947	1.00	35.17	D000	C
ATOM	8281	CG	ASN	P	235	−20.286	−16.187	74.963	1.00	40.71	D000	C
ATOM	8282	OD1	ASN	P	235	−20.393	−17.373	75.280	1.00	40.09	D000	O
ATOM	8283	ND2	ASN	P	235	−21.034	−15.228	75.504	1.00	41.85	D000	N
ATOM	8284	N	TRP	P	236	−17.096	−13.353	75.867	1.00	39.79	D000	N
ATOM	8285	CA	TRP	P	236	−16.261	−13.296	77.062	1.00	46.37	D000	C
ATOM	8286	C	TRP	P	236	−17.096	−13.235	78.337	1.00	41.70	D000	C
ATOM	8287	O	TRP	P	236	−18.198	−12.687	78.359	1.00	49.28	D000	O
ATOM	8288	CB	TRP	P	236	−15.335	−12.082	77.009	1.00	45.14	D000	C
ATOM	8289	CG	TRP	P	236	−14.278	−12.168	75.954	1.00	47.98	D000	C
ATOM	8290	CD1	TRP	P	236	−14.263	−11.524	74.742	1.00	45.52	D000	C
ATOM	8291	CD2	TRP	P	236	−13.076	−12.948	76.010	1.00	46.16	D000	C
ATOM	8292	NE1	TRP	P	236	−13.122	−11.854	74.047	1.00	47.86	D000	N
ATOM	8293	CE2	TRP	P	236	−12.377	−12.728	74.800	1.00	48.95	D000	C
ATOM	8294	CE3	TRP	P	236	−12.524	−13.813	76.961	1.00	44.69	D000	C
ATOM	8295	CZ2	TRP	P	236	−11.155	−13.347	74.517	1.00	41.16	D000	C
ATOM	8296	CZ3	TRP	P	236	−11.303	−14.427	76.679	1.00	46.91	D000	C
ATOM	8297	CH2	TRP	P	236	−10.630	−14.180	75.469	1.00	44.61	D000	C
ATOM	8298	N	ARG	P	237	−16.554	−13.787	79.415	1.00	41.38	D000	N
ATOM	8299	CA	ARG	P	237	−17.130	−13.493	80.718	1.00	53.87	D000	C
ATOM	8300	C	ARG	P	237	−16.928	−12.007	80.992	1.00	61.28	D000	C
ATOM	8301	O	ARG	P	237	−15.886	−11.452	80.630	1.00	66.27	D000	O
ATOM	8302	CB	ARG	P	237	−16.478	−14.322	81.833	1.00	53.42	D000	C
ATOM	8303	CG	ARG	P	237	−16.800	−15.823	81.816	1.00	47.57	D000	C
ATOM	8304	CD	ARG	P	237	−18.062	−16.175	82.614	1.00	51.09	D000	C
ATOM	8305	NE	ARG	P	237	−17.828	−16.314	84.057	1.00	58.37	D000	N
ATOM	8306	CZ	ARG	P	237	−17.838	−17.466	84.735	1.00	56.45	D000	C
ATOM	8307	NH1	ARG	P	237	−18.083	−18.621	84.123	1.00	48.82	D000	N1+
ATOM	8308	NH2	ARG	P	237	−17.612	−17.462	86.046	1.00	63.83	D000	N
ATOM	8309	N	PRO	P	238	−17.893	−11.331	81.605	1.00	62.76	D000	N
ATOM	8310	CA	PRO	P	238	−17.707	−9.908	81.907	1.00	69.38	D000	C
ATOM	8311	C	PRO	P	238	−16.409	−9.654	82.665	1.00	74.57	D000	C
ATOM	8312	O	PRO	P	238	−16.040	−10.408	83.571	1.00	71.66	D000	O
ATOM	8313	CB	PRO	P	238	−18.942	−9.573	82.746	1.00	64.98	D000	C
ATOM	8314	CG	PRO	P	238	−19.987	−10.474	82.171	1.00	64.63	D000	C
ATOM	8315	CD	PRO	P	238	−19.285	−11.760	81.814	1.00	57.83	D000	C
ATOM	8316	N	GLU	P	239	−15.705	−8.593	82.248	1.00	76.88	D000	N
ATOM	8317	CA	GLU	P	239	−14.381	−8.126	82.688	1.00	83.12	D000	C
ATOM	8318	C	GLU	P	239	−13.208	−8.804	81.960	1.00	80.80	D000	C
ATOM	8319	O	GLU	P	239	−12.049	−8.510	82.297	1.00	84.63	D000	O
ATOM	8320	CB	GLU	P	239	−14.170	−8.253	84.207	1.00	83.81	D000	C
ATOM	8321	CG	GLU	P	239	−14.580	−6.991	84.959	1.00	91.55	D000	C
ATOM	8322	CD	GLU	P	239	−13.794	−6.763	86.239	1.00	97.32	D000	C
ATOM	8323	OE1	GLU	P	239	−14.226	−7.250	87.308	1.00	93.15	D000	O
ATOM	8324	OE2	GLU	P	239	−12.745	−6.086	86.172	1.00	96.55	D000	O1−
ATOM	8325	N	GLN	P	240	−13.452	−9.674	80.980	1.00	74.55	D000	N
ATOM	8326	CA	GLN	P	240	−12.388	−10.436	80.304	1.00	70.87	D000	C
ATOM	8327	C	GLN	P	240	−12.327	−10.058	78.811	1.00	70.85	D000	C
ATOM	8328	O	GLN	P	240	−13.346	−9.637	78.253	1.00	75.89	D000	O
ATOM	8329	CB	GLN	P	240	−12.619	−11.949	80.462	1.00	68.58	D000	C
ATOM	8330	CG	GLN	P	240	−12.717	−12.433	81.899	1.00	68.41	D000	C
ATOM	8331	CD	GLN	P	240	−11.414	−12.251	82.660	1.00	75.96	D000	C
ATOM	8332	OE1	GLN	P	240	−10.466	−13.018	82.480	1.00	70.60	D000	O
ATOM	8333	NE2	GLN	P	240	−11.359	−11.226	83.518	1.00	77.27	D000	N
ATOM	8334	N	PRO	P	241	−11.147	−10.193	78.150	1.00	69.18	D000	N
ATOM	8335	CA	PRO	P	241	−9.849	−10.736	78.592	1.00	66.74	D000	C
ATOM	8336	C	PRO	P	241	−9.056	−9.841	79.559	1.00	73.69	D000	C
ATOM	8337	O	PRO	P	241	−9.074	−8.611	79.454	1.00	81.53	D000	O
ATOM	8338	CB	PRO	P	241	−9.088	−10.907	77.273	1.00	58.34	D000	C
ATOM	8339	CG	PRO	P	241	−9.646	−9.842	76.388	1.00	54.80	D000	C
ATOM	8340	CD	PRO	P	241	−11.106	−9.787	76.727	1.00	57.51	D000	C
ATOM	8341	N	GLU	P	253	−1.712	−15.376	81.188	1.00	57.88	D000	N
ATOM	8342	CA	GLU	P	253	−3.063	−15.516	80.648	1.00	58.93	D000	C
ATOM	8343	C	GLU	P	253	−3.184	−15.191	79.148	1.00	57.34	D000	C
ATOM	8344	O	GLU	P	253	−3.809	−14.204	78.771	1.00	60.57	D000	O
ATOM	8345	CB	GLU	P	253	−4.028	−14.606	81.410	1.00	67.05	D000	C
ATOM	8346	CG	GLU	P	253	−4.239	−14.925	82.886	1.00	65.01	D000	C
ATOM	8347	CD	GLU	P	253	−4.871	−13.746	83.619	1.00	78.11	D000	C
ATOM	8348	OE1	GLU	P	253	−6.039	−13.406	83.290	1.00	74.19	D000	O
ATOM	8349	OE2	GLU	P	253	−4.210	−13.174	84.525	1.00	80.72	D000	O1−
ATOM	8350	N	ASP	P	254	−2.582	−16.015	78.297	1.00	59.04	D000	N
ATOM	8351	CA	ASP	P	254	−2.582	−15.774	76.863	1.00	57.72	D000	C
ATOM	8352	C	ASP	P	254	−3.509	−16.705	76.087	1.00	51.09	D000	C
ATOM	8353	O	ASP	P	254	−3.528	−16.640	74.857	1.00	48.82	D000	O
ATOM	8354	CB	ASP	P	254	−1.159	−15.911	76.296	1.00	61.92	D000	C
ATOM	8355	CG	ASP	P	254	−0.161	−14.973	76.935	1.00	62.66	D000	C
ATOM	8356	OD1	ASP	P	254	−0.567	−13.960	77.547	1.00	61.96	D000	O
ATOM	8357	OD2	ASP	P	254	1.048	−15.281	76.834	1.00	65.49	D000	O1−
ATOM	8358	N	CYS	P	255	−4.265	−17.574	76.753	1.00	47.05	D000	N
ATOM	8359	CA	CYS	P	255	−5.063	−18.571	76.051	1.00	41.26	D000	C
ATOM	8360	C	CYS	P	255	−6.488	−18.590	76.580	1.00	38.11	D000	C
ATOM	8361	O	CYS	P	255	−6.716	−18.454	77.783	1.00	39.54	D000	O
ATOM	8362	CB	CYS	P	255	−4.450	−19.956	76.186	1.00	44.58	D000	C
ATOM	8363	SG	CYS	P	255	−2.846	−20.164	75.353	1.00	52.24	D000	S
ATOM	8364	N	ALA	P	256	−7.440	−18.776	75.674	1.00	36.50	D000	N
ATOM	8365	CA	ALA	P	256	−8.857	−18.645	75.980	1.00	35.39	D000	C
ATOM	8366	C	ALA	P	256	−9.527	−20.010	76.077	1.00	31.26	D000	C
ATOM	8367	O	ALA	P	256	−9.240	−20.914	75.281	1.00	30.62	D000	O
ATOM	8368	CB	ALA	P	256	−9.555	−17.793	74.921	1.00	38.76	D000	C
ATOM	8369	N	HIS	P	257	−10.412	−20.157	77.066	1.00	30.17	D000	N
ATOM	8370	CA	HIS	P	257	−11.139	−21.406	77.272	1.00	32.66	D000	C
ATOM	8371	C	HIS	P	257	−12.600	−21.131	77.611	1.00	33.59	D000	C
ATOM	8372	O	HIS	P	257	−12.962	−20.057	78.108	1.00	31.39	D000	O
ATOM	8373	CB	HIS	P	257	−10.517	−22.263	78.384	1.00	28.03	D000	C
ATOM	8374	CG	HIS	P	257	−10.526	−21.604	79.727	1.00	34.24	D000	C
ATOM	8375	ND1	HIS	P	257	−11.562	−21.751	80.621	1.00	34.37	D000	N
ATOM	8376	CD2	HIS	P	257	−9.620	−20.802	80.335	1.00	38.40	D000	C
ATOM	8377	CE1	HIS	P	257	−11.298	−21.068	81.718	1.00	34.64	D000	C
ATOM	8378	NE2	HIS	P	257	−10.128	−20.479	81.569	1.00	37.12	D000	N
ATOM	8379	N	PHE	P	258	−13.444	−22.124	77.309	1.00	33.23	D000	N
ATOM	8380	CA	PHE	P	258	−14.808	−22.141	77.823	1.00	32.25	D000	C
ATOM	8381	C	PHE	P	258	−14.773	−22.392	79.319	1.00	32.26	D000	C
ATOM	8382	O	PHE	P	258	−13.956	−23.171	79.811	1.00	29.18	D000	O
ATOM	8383	CB	PHE	P	258	−15.652	−23.232	77.153	1.00	30.58	D000	C
ATOM	8384	CG	PHE	P	258	−15.651	−23.174	75.659	1.00	27.36	D000	C
ATOM	8385	CD1	PHE	P	258	−16.550	−22.394	74.987	1.00	28.97	D000	C
ATOM	8386	CD2	PHE	P	258	−14.738	−23.912	74.931	1.00	28.24	D000	C
ATOM	8387	CE1	PHE	P	258	−16.541	−22.343	73.614	1.00	34.71	D000	C
ATOM	8388	CE2	PHE	P	258	−14.723	−23.869	73.566	1.00	30.59	D000	C
ATOM	8389	CZ	PHE	P	258	−15.623	−23.079	72.902	1.00	33.75	D000	C
ATOM	8390	N	THR	P	259	−15.684	−21.742	80.033	1.00	36.07	D000	N
ATOM	8391	CA	THR	P	259	−15.852	−21.887	81.471	1.00	37.54	D000	C
ATOM	8392	C	THR	P	259	−17.106	−22.709	81.741	1.00	38.73	D000	C
ATOM	8393	O	THR	P	259	−17.882	−23.018	80.828	1.00	40.70	D000	O
ATOM	8394	CB	THR	P	259	−15.949	−20.510	82.148	1.00	41.98	D000	C
ATOM	8395	OG1	THR	P	259	−17.200	−19.888	81.813	1.00	41.80	D000	O
ATOM	8396	CG2	THR	P	259	−14.799	−19.598	81.696	1.00	30.57	D000	C
ATOM	8397	N	ASP	P	260	−17.342	−23.006	83.020	1.00	37.73	D000	N
ATOM	8398	CA	ASP	P	260	−18.446	−23.894	83.380	1.00	37.79	D000	C
ATOM	8399	C	ASP	P	260	−19.814	−23.404	82.896	1.00	38.90	D000	C
ATOM	8400	O	ASP	P	260	−20.758	−24.201	82.869	1.00	41.70	D000	O
ATOM	8401	CB	ASP	P	260	−18.483	−24.128	84.901	1.00	35.64	D000	C
ATOM	8402	CG	ASP	P	260	−18.619	−22.834	85.712	1.00	42.82	D000	C
ATOM	8403	OD1	ASP	P	260	−18.241	−21.740	85.225	1.00	48.13	D000	O
ATOM	8404	OD2	ASP	P	260	−19.161	−22.907	86.836	1.00	44.48	D000	O1−
ATOM	8405	N	ASP	P	261	−19.955	−22.136	82.499	1.00	41.54	D000	N
ATOM	8406	CA	ASP	P	261	−21.226	−21.648	81.973	1.00	42.82	D000	C
ATOM	8407	C	ASP	P	261	−21.155	−21.336	80.487	1.00	41.84	D000	C
ATOM	8408	O	ASP	P	261	−22.099	−20.769	79.939	1.00	43.69	D000	O
ATOM	8409	CB	ASP	P	261	−21.727	−20.412	82.738	1.00	43.58	D000	C
ATOM	8410	CG	ASP	P	261	−20.950	−19.119	82.416	1.00	49.58	D000	C
ATOM	8411	OD1	ASP	P	261	−19.993	−19.120	81.605	1.00	52.04	D000	O
ATOM	8412	OD2	ASP	P	261	−21.333	−18.065	82.974	1.00	48.73	D000	O1−
ATOM	8413	N	GLY	P	262	−20.046	−21.659	79.826	1.00	41.79	D000	N
ATOM	8414	CA	GLY	P	262	−19.923	−21.469	78.406	1.00	35.80	D000	C
ATOM	8415	C	GLY	P	262	−19.239	−20.181	78.005	1.00	34.51	D000	C
ATOM	8416	O	GLY	P	262	−18.649	−20.125	76.926	1.00	35.57	D000	O
ATOM	8417	N	ARG	P	263	−19.315	−19.141	78.829	1.00	35.18	D000	N
ATOM	8418	CA	ARG	P	263	−18.644	−17.901	78.475	1.00	39.45	D000	C
ATOM	8419	C	ARG	P	263	−17.120	−18.052	78.581	1.00	36.67	D000	C
ATOM	8420	O	ARG	P	263	−16.588	−18.949	79.235	1.00	34.59	D000	O
ATOM	8421	CB	ARG	P	263	−19.177	−16.755	79.332	1.00	39.46	D000	C
ATOM	8422	CG	ARG	P	263	−20.633	−16.427	79.008	1.00	41.29	D000	C
ATOM	8423	CD	ARG	P	263	−21.171	−15.300	79.852	1.00	41.58	D000	C
ATOM	8424	NE	ARG	P	263	−21.060	−15.629	81.269	1.00	57.11	D000	N
ATOM	8425	CZ	ARG	P	263	−21.316	−14.794	82.274	1.00	54.20	D000	C
ATOM	8426	NH1	ARG	P	263	−21.702	−13.543	82.039	1.00	46.67	D000	N1+
ATOM	8427	NH2	ARG	P	263	−21.168	−15.216	83.524	1.00	49.65	D000	N
ATOM	8428	N	TRP	P	264	−16.414	−17.184	77.879	1.00	39.86	D000	N
ATOM	8429	CA	TRP	P	264	−14.984	−17.349	77.652	1.00	38.07	D000	C
ATOM	8430	C	TRP	P	264	−14.144	−16.707	78.750	1.00	36.92	D000	C
ATOM	8431	O	TRP	P	264	−14.565	−15.769	79.434	1.00	38.51	D000	O
ATOM	8432	CB	TRP	P	264	−14.596	−16.743	76.311	1.00	36.59	D000	C
ATOM	8433	CG	TRP	P	264	−15.334	−17.316	75.157	1.00	33.59	D000	C
ATOM	8434	CD1	TRP	P	264	−16.124	−18.422	75.156	1.00	28.12	D000	C
ATOM	8435	CD2	TRP	P	264	−15.343	−16.808	73.823	1.00	37.35	D000	C
ATOM	8436	NE1	TRP	P	264	−16.627	−18.635	73.909	1.00	31.66	D000	N
ATOM	8437	CE2	TRP	P	264	−16.158	−17.661	73.064	1.00	38.06	D000	C
ATOM	8438	CE3	TRP	P	264	−14.736	−15.714	73.194	1.00	34.20	D000	C
ATOM	8439	CZ2	TRP	P	264	−16.384	−17.455	71.697	1.00	36.24	D000	C
ATOM	8440	CZ3	TRP	P	264	−14.966	−15.510	71.854	1.00	34.62	D000	C
ATOM	8441	CH2	TRP	P	264	−15.783	−16.375	71.118	1.00	35.86	D000	C
ATOM	8442	N	ASN	P	265	−12.908	−17.179	78.854	1.00	32.60	D000	N
ATOM	8443	CA	ASN	P	265	−11.991	−16.649	79.844	1.00	35.02	D000	C
ATOM	8444	C	ASN	P	265	−10.562	−16.955	79.416	1.00	35.40	D000	C
ATOM	8445	O	ASN	P	265	−10.303	−17.966	78.762	1.00	34.37	D000	O
ATOM	8446	CB	ASN	P	265	−12.302	−17.268	81.206	1.00	41.49	D000	C
ATOM	8447	CG	ASN	P	265	−11.391	−16.785	82.295	1.00	45.67	D000	C
ATOM	8448	OD1	ASN	P	265	−11.470	−15.634	82.725	1.00	46.99	D000	O
ATOM	8449	ND2	ASN	P	265	−10.486	−17.660	82.730	1.00	42.25	D000	N
ATOM	8450	N	ASP	P	266	−9.635	−16.081	79.804	1.00	41.02	D000	N
ATOM	8451	CA	ASP	P	266	−8.210	−16.284	79.555	1.00	44.53	D000	C
ATOM	8452	C	ASP	P	266	−7.533	−16.874	80.790	1.00	44.46	D000	C
ATOM	8453	O	ASP	P	266	−7.836	−16.493	81.922	1.00	42.76	D000	O
ATOM	8454	CB	ASP	P	266	−7.513	−14.977	79.143	1.00	48.13	D000	C
ATOM	8455	CG	ASP	P	266	−7.889	−13.788	80.036	1.00	60.01	D000	C
ATOM	8456	OD1	ASP	P	266	−9.096	−13.510	80.179	1.00	60.58	D000	O
ATOM	8457	OD2	ASP	P	266	−6.988	−13.158	80.633	1.00	64.47	D000	O1−
ATOM	8458	N	ASP	P	267	−6.622	−17.815	80.563	1.00	44.24	D000	N
ATOM	8459	CA	ASP	P	267	−5.909	−18.469	81.647	1.00	42.61	D000	C
ATOM	8460	C	ASP	P	267	−4.508	−18.821	81.152	1.00	44.14	D000	C
ATOM	8461	O	ASP	P	267	−4.233	−18.787	79.952	1.00	41.89	D000	O
ATOM	8462	CB	ASP	P	267	−6.688	−19.697	82.122	1.00	38.52	D000	C
ATOM	8463	CG	ASP	P	267	−6.223	−20.188	83.464	1.00	45.95	D000	C
ATOM	8464	OD1	ASP	P	267	−5.365	−19.510	84.068	1.00	48.74	D000	O
ATOM	8465	OD2	ASP	P	267	−6.710	−21.244	83.919	1.00	43.95	D000	O1−
ATOM	8466	N	VAL	P	268	−3.612	−19.180	82.076	1.00	47.41	D000	N
ATOM	8467	CA	VAL	P	268	−2.258	−19.507	81.643	1.00	46.28	D000	C
ATOM	8468	C	VAL	P	268	−2.306	−20.765	80.793	1.00	45.81	D000	C
ATOM	8469	O	VAL	P	268	−3.051	−21.717	81.079	1.00	42.24	D000	O
ATOM	8470	CB	VAL	P	268	−1.274	−19.643	82.822	1.00	45.28	D000	C
ATOM	8471	CG1	VAL	P	268	−1.359	−18.423	83.707	1.00	40.04	D000	C
ATOM	8472	CG2	VAL	P	268	−1.489	−20.937	83.609	1.00	40.72	D000	C
ATOM	8473	N	CYS	P	269	−1.525	−20.756	79.717	1.00	45.30	D000	N
ATOM	8474	CA	CYS	P	269	−1.620	−21.777	78.695	1.00	34.95	D000	C
ATOM	8475	C	CYS	P	269	−1.113	−23.121	79.167	1.00	39.62	D000	C
ATOM	8476	O	CYS	P	269	−1.267	−24.107	78.438	1.00	44.44	D000	O
ATOM	8477	CB	CYS	P	269	−0.849	−21.317	77.456	1.00	47.03	D000	C
ATOM	8478	SG	CYS	P	269	−1.435	−19.698	76.766	1.00	60.08	D000	S
ATOM	8479	N	GLN	P	270	−0.551	−23.199	80.371	1.00	40.97	D000	N
ATOM	8480	CA	GLN	P	270	0.007	−24.461	80.837	1.00	39.29	D000	C
ATOM	8481	C	GLN	P	270	−1.038	−25.378	81.448	1.00	33.15	D000	C
ATOM	8482	O	GLN	V	270	−0.769	−26.577	81.579	1.00	30.99	D000	O
ATOM	8483	CB	GLN	P	270	1.128	−24.207	81.857	1.00	52.36	D000	C
ATOM	8484	CG	GLN	P	270	2.531	−23.978	81.256	1.00	68.27	D000	C
ATOM	8485	CD	GLN	P	270	3.672	−24.458	82.188	1.00	90.18	D000	C
ATOM	8486	OE1	GLN	P	270	3.426	−25.009	83.272	1.00	96.23	D000	O
ATOM	8487	NE2	GLN	P	270	4.921	−24.250	81.760	1.00	83.33	D000	N
ATOM	8488	N	ARG	P	271	−2.213	−24.847	81.803	1.00	35.97	D000	N
ATOM	8489	CA	ARG	P	271	−3.258	−25.641	82.453	1.00	35.38	D000	C
ATOM	8490	C	ARG	P	271	−3.614	−26.831	81.577	1.00	34.50	D000	C
ATOM	8491	O	ARG	P	271	−3.835	−26.657	80.369	1.00	35.09	D000	O
ATOM	8492	CB	ARG	P	271	−4.533	−24.825	82.699	1.00	32.78	D000	C
ATOM	8493	CG	ARG	P	271	−4.404	−23.700	83.663	1.00	35.79	D000	C
ATOM	8494	CD	ARG	P	271	−4.885	−24.052	85.062	1.00	38.85	D000	C
ATOM	8495	NE	ARG	P	271	−4.351	−23.079	86.026	1.00	53.17	D000	N
ATOM	8496	CZ	ARG	P	271	−3.487	−23.363	87.009	1.00	57.60	D000	C
ATOM	8497	NH1	ARG	P	271	−3.061	−24.616	87.211	1.00	48.15	D000	N1+
ATOM	8498	NH2	ARG	P	271	−3.054	−22.387	87.805	1.00	54.98	D000	N
ATOM	8499	N	PRO	P	272	−3.709	−27.959	82.102	1.00	34.18	D000	N
ATOM	8500	CA	PRO	P	272	−4.104	−29.152	81.304	1.00	30.39	D000	C
ATOM	8501	C	PRO	P	272	−5.617	−29.326	81.191	1.00	30.82	D000	C
ATOM	8502	O	PRO	P	272	−6.222	−30.227	81.774	1.00	30.88	D000	O
ATOM	8503	CB	PRO	P	272	−3.446	−30.296	82.079	1.00	29.98	D000	C
ATOM	8504	CG	PRO	P	272	−3.279	−29.776	83.527	1.00	33.19	D000	C
ATOM	8505	CD	PRO	P	272	−3.502	−28.269	83.527	1.00	30.33	D000	C
ATOM	8506	N	TYR	P	273	−6.260	−28.438	80.435	1.00	29.69	D000	N
ATOM	8507	CA	TYR	P	273	−7.685	−28.556	80.183	1.00	26.06	D000	C
ATOM	8508	C	TYR	P	273	−7.957	−29.510	79.021	1.00	31.32	D000	C
ATOM	8509	O	TYR	P	273	−7.075	−29.834	78.220	1.00	34.09	D000	O
ATOM	8510	CB	TYR	P	273	−8.289	−27.199	79.848	1.00	29.36	D000	C
ATOM	8511	CG	TYR	P	273	−8.313	−26.189	80.968	1.00	31.45	D000	C
ATOM	8512	CD1	TYR	P	273	−8.404	−26.586	82.310	1.00	29.10	D000	C
ATOM	8513	CD2	TYR	P	273	−8.243	−24.832	80.685	1.00	26.14	D000	C
ATOM	8514	CE1	TYR	P	273	−8.422	−25.650	83.325	1.00	23.99	D000	C
ATOM	8515	CE2	TYR	P	273	−8.275	−23.900	81.688	1.00	30.08	D000	C
ATOM	8516	CZ	TYR	P	273	−8.364	−24.312	83.001	1.00	27.73	D000	C
ATOM	8517	OH	TYR	P	273	−8.380	−23.357	83.973	1.00	30.77	D000	O
ATOM	8518	N	ARG	P	274	−9.208	−29.949	78.931	1.00	28.38	D000	N
ATOM	8519	CA	ARG	P	274	−9.699	−30.608	77.733	1.00	26.38	D000	C
ATOM	8520	C	ARG	P	274	−9.755	−29.604	76.570	1.00	28.97	D000	C
ATOM	8521	O	ARG	P	274	−9.693	−28.383	76.762	1.00	29.05	D000	O
ATOM	8522	CB	ARG	P	274	−11.090	−31.183	78.003	1.00	26.93	D000	C
ATOM	8523	CG	ARG	P	274	−11.108	−32.298	78.990	1.00	27.16	D000	C
ATOM	8524	CD	ARG	P	274	−12.512	−32.728	79.284	1.00	29.23	D000	C
ATOM	8525	NE	ARG	P	274	−12.531	−33.815	80.262	1.00	31.79	D000	N
ATOM	8526	CZ	ARG	P	274	−13.610	−34.234	80.917	1.00	28.61	D000	C
ATOM	8527	NH1	ARG	P	274	−14.801	−33.662	80.721	1.00	27.83	D000	N1+
ATOM	8528	NH2	ARG	P	274	−13.495	−35.241	81.767	1.00	30.68	D000	N
ATOM	8529	N	TRP	P	275	−9.894	−30.113	75.345	1.00	23.49	D000	N
ATOM	8530	CA	TRP	P	275	−9.938	−29.226	74.188	1.00	25.18	D000	C
ATOM	8531	C	TRP	P	275	−10.855	−29.837	73.136	1.00	28.35	D000	C
ATOM	8532	O	TRP	P	275	−11.240	−31.009	73.214	1.00	27.63	D000	O
ATOM	8533	CB	TRP	P	275	−8.524	−28.953	73.614	1.00	26.97	D000	C
ATOM	8534	CG	TRP	P	275	−7.949	−30.164	72.960	1.00	26.87	D000	C
ATOM	8535	CD1	TRP	P	275	−7.973	−30.473	71.628	1.00	25.57	D000	C
ATOM	8536	CD2	TRP	P	275	−7.346	−31.284	73.625	1.00	26.80	D000	C
ATOM	8537	NE1	TRP	P	275	−7.403	−31.713	71.419	1.00	26.56	D000	N
ATOM	8538	CE2	TRP	P	275	−7.008	−32.230	72.626	1.00	28.11	D000	C
ATOM	8539	CE3	TRP	P	275	−7.044	−31.573	74.966	1.00	24.47	D000	C
ATOM	8540	CZ2	TRP	P	275	−6.388	−33.439	72.926	1.00	26.32	D000	C
ATOM	8541	CZ3	TRP	P	275	−6.439	−32.772	75.265	1.00	25.01	D000	C
ATOM	8542	CH2	TRP	P	275	−6.114	−33.692	74.250	1.00	29.39	D000	C
ATOM	8543	N	VAL	P	276	−11.186	−29.023	72.135	1.00	27.49	D000	N
ATOM	8544	CA	VAL	P	276	−12.064	−29.405	71.039	1.00	29.28	D000	C
ATOM	8545	C	VAL	P	276	−11.347	−29.157	69.720	1.00	32.15	D000	C
ATOM	8546	O	VAL	P	276	−11.010	−28.009	69.399	1.00	30.70	D000	O
ATOM	8547	CB	VAL	P	276	−13.381	−28.615	71.076	1.00	32.24	D000	C
ATOM	8548	CG1	VAL	P	276	−14.255	−28.997	69.881	1.00	28.45	D000	C
ATOM	8549	CG2	VAL	P	276	−14.099	−28.838	72.418	1.00	27.44	D000	C
ATOM	8550	N	CYS	P	277	−11.188	−30.212	68.926	1.00	31.02	D000	N
ATOM	8551	CA	CYS	P	277	−10.688	−30.089	67.560	1.00	33.70	D000	C
ATOM	8552	C	CYS	P	277	−11.856	−29.883	66.594	1.00	36.60	D000	C
ATOM	8553	O	CYS	P	277	−12.924	−30.476	66.769	1.00	35.91	D000	O
ATOM	8554	CB	CYS	P	277	−9.893	−31.339	67.158	1.00	33.14	D000	C
ATOM	8555	SG	CYS	P	277	−8.261	−31.627	67.947	1.00	35.59	D000	S
ATOM	8556	N	GLU	P	278	−11.644	−29.037	65.572	1.00	36.89	D000	N
ATOM	8557	CA	GLU	P	278	−12.627	−28.753	64.525	1.00	39.14	D000	C
ATOM	8558	C	GLU	P	278	−11.998	−28.940	63.144	1.00	44.48	D000	C
ATOM	8559	O	GLU	P	278	−10.812	−28.657	62.944	1.00	39.34	D000	O
ATOM	8560	CB	GLU	P	278	−13.201	−27.309	64.639	1.00	33.16	D000	C
ATOM	8561	CG	GLU	P	278	−14.353	−26.998	63.675	1.00	36.59	D000	C
ATOM	8562	CD	GLU	P	278	−14.820	−25.530	63.719	1.00	44.66	D000	C
ATOM	8563	OE1	GLU	P	278	−14.202	−24.714	64.445	1.00	39.06	D000	O
ATOM	8564	OE2	GLU	P	278	−15.829	−25.200	63.049	1.00	41.28	D000	O1−
ATOM	8565	N	THR	P	279	−12.790	−29.443	62.197	1.00	50.44	D000	N
ATOM	8566	CA	THR	P	279	−12.402	−29.459	60.790	1.00	53.12	D000	C
ATOM	8567	C	THR	P	279	−13.617	−29.195	59.898	1.00	49.51	D000	C
ATOM	8568	O	THR	P	279	−14.703	−29.717	60.154	1.00	53.00	D000	O
ATOM	8569	CB	THR	P	279	−11.717	−30.798	60.436	1.00	45.79	D000	C
ATOM	8570	OG1	THR	P	279	−11.049	−30.673	59.179	1.00	51.68	D000	O
ATOM	8571	CG2	THR	P	279	−12.709	−31.937	60.373	1.00	41.88	D000	C
ATOM	8572	N	GLU	P	280	−13.431	−28.398	58.839	1.00	54.11	D000	N
ATOM	8573	CA	GLU	P	280	−14.518	−28.026	57.929	1.00	55.44	D000	C
ATOM	8574	C	GLU	P	280	−14.664	−29.061	56.808	1.00	60.78	D000	C
ATOM	8575	O	GLU	P	280	−13.673	−29.610	56.323	1.00	66.29	D000	O
ATOM	8576	CB	GLU	P	280	−14.275	−26.632	57.350	1.00	58.37	D000	C
ATOM	8577	CG	GLU	P	280	−14.341	−25.476	58.376	1.00	56.42	D000	C
ATOM	8578	CD	GLU	P	280	−13.124	−25.396	59.315	1.00	59.60	D000	C
ATOM	8579	OE1	GLU	P	280	−12.166	−26.179	59.134	1.00	63.77	D000	O
ATOM	8580	OE2	GLU	P	280	−13.129	−24.553	60.247	1.00	61.91	D000	O1−
ATOM	8581	N	LEU	P	281	−15.911	−29.308	56.389	1.00	64.56	D000	N
ATOM	8582	CA	LEU	P	281	−16.292	−30.535	55.682	1.00	69.60	D000	C
ATOM	8583	C	LEU	P	281	−16.310	−30.448	54.149	1.00	73.85	D000	C
ATOM	8584	O	LEU	P	281	−16.945	−31.306	53.521	1.00	77.45	D000	O
ATOM	8585	CB	LEU	P	281	−17.662	−31.015	56.164	1.00	60.03	D000	C
ATOM	8586	CG	LEU	P	281	−17.690	−32.374	56.863	1.00	56.08	D000	C
ATOM	8587	CD1	LEU	P	281	−19.116	−32.776	57.171	1.00	66.41	D000	C
ATOM	8588	CD2	LEU	P	281	−17.006	−33.448	56.066	1.00	58.00	D000	C
ATOM	8589	N	ASP	P	282	−15.668	−29.445	53.538	1.00	74.94	D000	N
ATOM	8590	CA	ASP	P	282	−15.590	−29.289	52.056	1.00	74.61	D000	C
ATOM	8591	C	ASP	P	282	−16.879	−28.715	51.457	1.00	69.05	D000	C
ATOM	8592	O	ASP	P	282	−17.285	−27.589	51.750	1.00	68.03	D000	O
ATOM	8593	CB	ASP	P	282	−15.291	−30.618	51.327	1.00	75.72	D000	C
ATOM	8594	CG	ASP	P	282	−13.973	−31.262	51.748	1.00	83.45	D000	C
ATOM	8595	OD2	ASP	P	282	−14.017	−32.153	52.639	1.00	81.11	D000	O
ATOM	8596	OD1	ASP	P	282	−12.912	−30.910	51.169	1.00	76.47	D000	O1−
TER
HETATM	8597	CA	CA	E	1	−46.046	−40.018	63.255	1.00	40.77		Ca
HETATM	8598	CA	CA	E	2	−15.968	−22.911	63.354	1.00	43.19		Ca
TER

TABLE 15
Antibody Constant Regions
	SEQ ID
Designation	NO:	CL Domain Amino Acid Sequence
CL-1	32681	GQPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSP
		VKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTV
		EKTVAPTECS
CL-2	32682	GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPV
		KAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEK
		TVAPTECS
CL-2.1	32683	QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVK
		AGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKT
		VAPTECS
CL-3	32684	GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPV
		KAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEK
		TVAPTECS
CL-7	32685	GQPKAAPSVTLFPPSSEELQANKATLVCLVSDFYPGAVTVAWKADGSP
		VKVGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCRVTHEGSTVE
		KTVAPAECS
Human	32686	TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQS
kappa v1		GNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVT
		KSFNRGEC
Human	32687	RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ
kappa v2		SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPV
		TKSFNRGEC
	SEQ ID
Ig isotype	NO:	Heavy Chain Constant Region Amino Acid Sequence
Human IgG1z	32688	ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV
		HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP
		KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS
		HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWL
		NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVS
		LTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDK
		SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Human	32689	ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV
IgG1za		HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP
		KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS
		HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWL
		NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSL
		TCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS
		RWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Human IgG1f	32690	ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV
		HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEP
		KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS
		HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWL
		NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVS
		LTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDK
		SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Human	32691	ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV
IgG1fa		HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEP
		KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS
		HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWL
		NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSL
		TCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS
		RWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Human IgG2	32692	ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGV
		HTFPAVLOSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTVER
		KCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDP
		EVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLV
		KGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRW
		QQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Human IgG4	32693	ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGV
		HTFPAVLOSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVES
		KYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQED
		PEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGK
		EYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRW
		QEGNVFSCSVMHEALHNHYTQKSLSLSLGK
Human	32694	ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV
IgG1-SEFL2		HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP
		KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS
		HEDPEVKFNWYVDGVEVHNAKTKPCEEQYGSTYRCVSVLTVLHQDWL
		NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVS
		LTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDK
		SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

Each reference cited herein is hereby incorporated by reference in its entirety for all that it teaches and for all purposes.

The present invention is not to be limited in scope by the specific embodiments described herein, which are intended as single illustrations of individual embodiments of the invention, and functionally equivalent methods and components are invention. Indeed, various modifications of the invention, in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description and accompanying drawings. Such modifications are intended to fall within the scope of the appended claims.

Claims

1. An isolated antigen binding protein that binds to human ASGR-1 comprising the amino acid sequence of SEQ ID NO:5, wherein the antigen binding protein inhibits ASGR-1 binding to ligand.

2. The isolated antigen binding protein of claim 1, wherein the isolated antigen binding protein binds to a carbohydrate recognition domain of human ASGR-1.

3. The isolated antigen binding protein of claim 1, wherein the isolated antigen binding protein inhibits the internalization of ASGR.

4. The isolated antigen binding protein of claim 1, wherein the isolated antigen binding protein further binds ASGR-2.

5. The isolated antigen binding protein of claim 1, wherein the isolated antigen binding protein is a monoclonal antibody.

6. An isolated antigen binding protein that binds to human ASGR-2, wherein the isolated antigen binding protein inhibits ASGR-2 binding to ligand.

7. The isolated antigen binding protein of claim 6, wherein the isolated antigen binding protein inhibits the internalization of ASGR.

8. The isolated antigen binding protein of claim 6, wherein the isolated antigen binding protein is a monoclonal antibody.

9. An isolated antigen binding protein that binds to human ASGR and inhibits human ASGR binding to ligand.

10. The isolated antigen binding protein of claim 9, wherein the isolated antigen binding protein inhibits internalization of ASGR.

11. The isolated antigen binding protein of claim 9, wherein the isolated antigen binding protein is a monoclonal antibody.

12. An isolated antigen binding protein that binds to human ASGR-1 and human ASGR-2, and inhibits human ASGR-1 and/or human ASGR-2 binding to ligand.

13. The isolated antigen binding protein of claim 12, wherein the isolated antigen binding protein inhibits internalization of human ASGR-1 or human ASGR-2.

14. The isolated antigen binding protein of claim 12, wherein the isolated antigen binding protein is a monoclonal antibody.

15. An isolated monoclonal antibody, wherein the isolated monoclonal antibody specifically binds to human ASGR-1 and comprises a VH CDR1, VH CDR2 and VH CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions in each CDR relative to the antibody VH of any of the sequences set forth in Tables 3-7.

16. The isolated monoclonal antibody of claim 15, wherein said isolated monoclonal antibody further comprises a VL CDR1, VL CDR2 and VL CDR3 having an amino acid sequence identical to or comprising 1, 2, or 3 amino acid residue substitutions in each CDR relative to the antibody VL of any of the sequences set forth in Tables 3-7.

17. The isolated monoclonal antibody of claim 16, wherein said VH CDRs and said VL CDRs are the corresponding paired VH and VL CDRs as set forth in Table 2.

18. An isolated monoclonal antibody, wherein the isolated monoclonal antibody specifically binds human ASGR-1 and comprises a heavy chain variable domain having at least 90% identity to any of the VH domain amino acid sequences set forth in Table 3-7.

19. The isolated monoclonal antibody of claim 18, further comprising a light chain variable domain having at least 90% identity to any of the VL domain amino acid sequences set forth in Table 3-7.

20. The isolated monoclonal antibody of claim 19, wherein the light chain variable domain and the heavy chain variable domain are the corresponding paired VL and VH as set forth in Table 3-7.

21. An isolated monoclonal antibody that competes for binding with the isolated monoclonal antibody of claim 20.

22. An isolated neutralizing monoclonal antibody that binds to human ASGR-1 comprising the amino acid sequence of SEQ ID NO:5, wherein the isolated neutralizing monoclonal antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: D216, Q217, N218, G219, P220, W221, Y229, E230, K234, W236, E239, Q240, P241, D242, D243, W244, Y245, G246, L249, G250, G251, G252, D254, Q270, W195, N209, R237, P238, H257, T259, D260, D261, R263, N265, D267, R271, Y273, H161, E162, E196, Q198, K199, F200, Q202, H203, H204, G232, F233, N235, G262, W167, S171, G172, K173, A174, A176, D177, N180, Y181, R183, L184, E185, D186, P272, W275, R170, I205, G206, P207, V208, R274, S194, T193, T231, G226, T227 or D228 (SEQ ID NO:5).

23. An isolated neutralizing monoclonal antibody that binds to human ASGR-1 comprising the amino acid sequence of SEQ ID NO:5, wherein the isolated neutralizing monoclonal antibody binds to human ASGR-1 at an epitope comprising at least one of the following amino acid residues: Q240, D242, W244, E253, N265, D266, D267, R237, N209, H257, T259 or Y273 (SEQ ID NO:5).

24. An isolated neutralizing monoclonal antibody that binds to human ASGR-1 comprising the amino acid sequence of SEQ ID NO:5 but does not bind to a variant human ASGR-1, wherein the variant human ASGR-1 comprises a single mutation of a residue selected the group consisting of: R170, S171, G172, R183, L184, W195, E196, K199, H203, H204, P207, V208, N209, H215, D216, P220, D225, D228, R237, P238, E239, P241, D242, D243, Y245, G246, H247, G248, L249, G251, E253, T259, D260, R263, N265, Q270, R271, P272, R274 and E280 as shown in SEQ ID NO:5.

25. The isolated neutralizing monoclonal antibody of claim 24, wherein the single mutation is selected from the group consisting of: W195, E196, K199, H203, H204, P207, P220, G251, and R263 as shown in SEQ ID NO:5.

26. The isolated antigen binding protein or antibody of any one of claims 1, 6, 9, 12, 15, 18, 21, 22, 23, and 24, wherein the antigen binding protein or antibody is a chimeric antibody, a humanized antibody, or a human antibody.

27. A pharmaceutical composition comprising the isolated antigen binding protein or antibody of any one of claims 1, 6, 9, 12, 15, 18, 21, 22, 23, and 24, and a pharmaceutically acceptable excipient.

28. An isolated nucleic acid encoding the isolated antigen binding protein or antibody of any one of claims 1, 6, 9, 12, 15, 18, 21, 22, 23, and 24.

29. A vector comprising the nucleic acid of claim 28.

30. A host cell comprising the vector of claim 29 or nucleic acid of claim 28.

31. A method for producing an antigen binding protein or an antibody comprising culturing the host cell of claim 30 under suitable conditions and recovering said antigen binding protein or antibody.

32. A method of treating or preventing a cardiovascular disease comprising administering to a patient in need thereof a therapeutically effective dose of an inhibitor of ASGR, ASGR-1, and/or ASGR-2.

33. The method of claim 32, wherein said cardiovascular disease is coronary artery disease or myocardial infarction.

34. A method of reducing LDL cholesterol levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an inhibitor of ASGR, ASGR-1, and/or ASGR-2.

35. A method of reducing non-HDL cholesterol levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an inhibitor of ASGR, ASGR-1, and/or ASGR-2.

36. A method of increasing ALP levels in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an inhibitor of ASGR, ASGR-1, and/or ASGR-2.

37. A method of antagonizing ASGR-1 in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an inhibitor of ASGR, ASGR-1, and/or ASGR-2.

38. A method of antagonizing ASGR-2 in a patient comprising administering to a patient in need thereof a therapeutically effective dose of an inhibitor of ASGR, ASGR-1, and/or ASGR-2.

39. The methods of any one of claims 32-38, wherein the inhibitor is an interfering RNA (e.g., siRNA or shRNA) that reduces expression of ASGR, ASGR-1 and/or ASGR-2.

40. The methods of any one of claims 32-38, wherein the inhibitor is an isolated neutralizing antigen binding protein that binds to human ASGR, ASGR-1 and/or ASGR-2.

41. The methods of claim 40, wherein the inhibitor is administered simultaneously or sequentially with at least one agent that lowers cholesterol.

42. The methods of claim 41, wherein the at least one agent is a statin, an anti-PCSK9 inhibitor or a combination thereof.

43. The methods of claim 42, wherein the at least one agent is selected from the group consisting of evolocumab, alirocumab, bococizumab, ALN-PCS, atorvastatin, cerivastatin, fluvastatin, lovastatin, mevastatin, pitavastatin, pravastatin, rosuvastatin, simvastatin, and some combination thereof.